ID UBAP1_HUMAN Reviewed; 502 AA. AC Q9NZ09; B7Z348; B7Z8N9; D3DRL7; F5GXE2; F5H0J8; Q4V759; Q53FP7; Q5T7B3; AC Q6FI75; Q8NC52; Q8NCG6; Q8NCH9; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 28-JAN-2026, entry version 195. DE RecName: Full=Ubiquitin-associated protein 1 {ECO:0000303|PubMed:11599797}; DE Short=UBAP-1 {ECO:0000303|PubMed:11599797}; DE AltName: Full=Nasopharyngeal carcinoma-associated gene 20 protein; GN Name=UBAP1 {ECO:0000303|PubMed:11599797, ECO:0000312|HGNC:HGNC:12461}; GN ORFNames=NAG20; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=11599797; DOI=10.1007/s004320100252; RA Qian J., Yang J., Zhang X., Zhang B., Wang J., Zhou M., Tang K., Li W., RA Zeng Z., Zhao X., Shen S., Li G.; RT "Isolation and characterization of a novel cDNA, UBAP1, derived from the RT tumor suppressor locus in human chromosome 9p21-22."; RL J. Cancer Res. Clin. Oncol. 127:613-618(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 11-502 (ISOFORM 3). RC TISSUE=Hippocampus, and Kidney; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-357. RC TISSUE=Stomach; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2). RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP FUNCTION, INTERACTION WITH PTPN23, IDENTIFICATION IN ESCRT-I COMPLEX, RP SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF PRO-37; GLU-59; RP TYR-404 AND PHE-472. RX PubMed=21757351; DOI=10.1016/j.cub.2011.06.028; RA Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A., RA Brownhill K., Bennion J., Pickering-Brown S., Woodman P.; RT "UBAP1 is a component of an endosome-specific ESCRT-I complex that is RT essential for MVB sorting."; RL Curr. Biol. 21:1245-1250(2011). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-289, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP FUNCTION, AND INTERACTION WITH VPS37A. RX PubMed=24284069; DOI=10.1242/jcs.140673; RA Wunderley L., Brownhill K., Stefani F., Tabernero L., Woodman P.; RT "The molecular basis for selective assembly of the UBAP1-containing RT endosome-specific ESCRT-I complex."; RL J. Cell Sci. 127:663-672(2014). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP STRUCTURE BY NMR OF 381-430. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of UBA domain of human ubiquitin associated protein 1 RT (UBAP1)."; RL Submitted (NOV-2004) to the PDB data bank. RN [14] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 389-502, FUNCTION, IDENTIFICATION RP IN ESCRT-I COMPLEX, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 17-LEU--ASP-19 AND RP 20-VAL--PHE-22. RX PubMed=22405001; DOI=10.1016/j.str.2011.12.013; RA Agromayor M., Soler N., Caballe A., Kueck T., Freund S.M., Allen M.D., RA Bycroft M., Perisic O., Ye Y., McDonald B., Scheel H., Hofmann K., RA Neil S.J., Martin-Serrano J., Williams R.L.; RT "The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA RT domain."; RL Structure 20:414-428(2012). RN [15] {ECO:0007744|PDB:5LM1} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 261-280 IN COMPLEX WITH PTPN23, RP AND MUTAGENESIS OF PHE-268; PRO-269 AND LEU-271. RX PubMed=27839950; DOI=10.1016/j.str.2016.10.006; RA Gahloth D., Levy C., Heaven G., Stefani F., Wunderley L., Mould P., RA Cliff M.J., Bella J., Fielding A.J., Woodman P., Tabernero L.; RT "Structural basis for selective interaction between the ESCRT regulator HD- RT PTP and UBAP1."; RL Structure 24:2115-2126(2016). RN [16] RP INVOLVEMENT IN SPG80, VARIANT SPG80 125-GLN--SER-502 DEL, INTERACTION WITH RP VPS28, AND UBIQUITIN-BINDING. RX PubMed=30929741; DOI=10.1016/j.ajhg.2019.03.001; RA Farazi Fard M.A., Rebelo A.P., Buglo E., Nemati H., Dastsooz H., RA Gehweiler I., Reich S., Reichbauer J., Quintans B., Ordonez-Ugalde A., RA Cortese A., Courel S., Abreu L., Powell E., Danzi M.C., Martuscelli N.B., RA Bis-Brewer D.M., Tao F., Zarei F., Habibzadeh P., Yavarian M., RA Modarresi F., Silawi M., Tabatabaei Z., Yousefi M., Farpour H.R., RA Kessler C., Mangold E., Kobeleva X., Tournev I., Chamova T., Mueller A.J., RA Haack T.B., Tarnopolsky M., Gan-Or Z., Rouleau G.A., Synofzik M., RA Sobrido M.J., Jordanova A., Schuele R., Zuchner S., Faghihi M.A.; RT "Truncating mutations in UBAP1 cause hereditary spastic paraplegia."; RL Am. J. Hum. Genet. 104:767-773(2019). RN [17] RP VARIANT SPG80 176-GLU--SER-502 DEL, FUNCTION, AND SUBUNIT. RX PubMed=31203368; DOI=10.1093/brain/awz158; RA Lin X., Su H.Z., Dong E.L., Lin X.H., Zhao M., Yang C., Wang C., Wang J., RA Chen Y.J., Yu H., Xu J., Ma L.X., Xiong Z.Q., Wang N., Chen W.J.; RT "Stop-gain mutations in UBAP1 cause pure autosomal-dominant spastic RT paraplegia."; RL Brain 142:2238-2252(2019). CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular CC trafficking process (PubMed:21757351, PubMed:22405001, CC PubMed:31203368). Binds to ubiquitinated cargo proteins and is required CC for the sorting of endocytic ubiquitinated cargos into multivesicular CC bodies (MVBs) (PubMed:21757351, PubMed:22405001). Plays a role in the CC proteasomal degradation of ubiquitinated cell-surface proteins, such as CC EGFR and BST2 (PubMed:22405001, PubMed:24284069, PubMed:31203368). CC {ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22405001, CC ECO:0000269|PubMed:24284069, ECO:0000269|PubMed:31203368}. CC -!- SUBUNIT: Component of an ESCRT-I complex (endosomal sorting complex CC required for transport I) which consists of TSG101, VPS28, VPS37A and CC UBAP1 in a 1:1:1:1 stoichiometry (Probable) (PubMed:21757351, CC PubMed:22405001, PubMed:24284069, PubMed:31203368). Interacts with CC PTPN23 (PubMed:21757351, PubMed:27839950). Interacts (via UBA domains) CC with ubiquitinated proteins (PubMed:22405001, PubMed:30929741). CC {ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22405001, CC ECO:0000269|PubMed:24284069, ECO:0000269|PubMed:27839950, CC ECO:0000269|PubMed:30929741, ECO:0000269|PubMed:31203368, CC ECO:0000305|PubMed:30929741}. CC -!- INTERACTION: CC Q9NZ09; P45877: PPIC; NbExp=3; IntAct=EBI-9641159, EBI-953909; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21757351}. CC Endosome {ECO:0000269|PubMed:21757351}. Note=Predominantly cytosolic CC (PubMed:21757351). Recruited to endosomes as part of the ESCRT-I CC complex (PubMed:21757351). {ECO:0000269|PubMed:21757351}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9NZ09-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NZ09-2; Sequence=VSP_013650; CC Name=3; CC IsoId=Q9NZ09-3; Sequence=VSP_046866; CC Name=4; CC IsoId=Q9NZ09-4; Sequence=VSP_046867; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, brain, CC placenta, lung, liver, skeletal muscle and pancreas. CC {ECO:0000269|PubMed:11599797}. CC -!- DOMAIN: The UMA domain mediates association with the ESCRT-I complex. CC {ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22405001}. CC -!- DISEASE: Spastic paraplegia 80, autosomal dominant (SPG80) CC [MIM:618418]: A form of spastic paraplegia, a neurodegenerative CC disorder characterized by a slow, gradual, progressive weakness and CC spasticity of the lower limbs. Rate of progression and the severity of CC symptoms are quite variable. Initial symptoms may include difficulty CC with balance, weakness and stiffness in the legs, muscle spasms, and CC dragging the toes when walking. In some forms of the disorder, bladder CC symptoms (such as incontinence) may appear, or the weakness and CC stiffness may spread to other parts of the body. CC {ECO:0000269|PubMed:30929741, ECO:0000269|PubMed:31203368}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- CAUTION: According to a report, can also be a component of ESCRT-I CC complexes containing VPS37B, VPS37C or VPS37D (PubMed:22405001). CC However, another publication showed that UBAP1 has specificity for CC complexes containing VPS37A and not VPS37 paralogs (PubMed:24284069). CC {ECO:0000269|PubMed:22405001, ECO:0000269|PubMed:24284069}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC11162.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAH12084.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF222043; AAF37827.2; -; mRNA. DR EMBL; AL136733; CAB66667.1; -; mRNA. DR EMBL; AK074724; BAC11162.1; ALT_INIT; mRNA. DR EMBL; AK074745; BAC11176.1; -; mRNA. DR EMBL; AK074812; BAC11224.1; -; mRNA. DR EMBL; AK074969; BAC11323.1; -; mRNA. DR EMBL; AK074995; BAC11342.1; -; mRNA. DR EMBL; AK295482; BAH12084.1; ALT_INIT; mRNA. DR EMBL; AK303711; BAH14025.1; -; mRNA. DR EMBL; CR533551; CAG38582.1; -; mRNA. DR EMBL; AK223235; BAD96955.1; -; mRNA. DR EMBL; AL353662; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58467.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58468.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58469.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58470.1; -; Genomic_DNA. DR EMBL; BC020950; AAH20950.1; -; mRNA. DR EMBL; BC098141; AAH98141.1; -; mRNA. DR EMBL; BC098316; AAH98316.1; -; mRNA. DR EMBL; BC099726; AAH99726.1; -; mRNA. DR EMBL; BC100668; AAI00669.1; -; mRNA. DR CCDS; CCDS55303.1; -. [Q9NZ09-4] DR CCDS; CCDS6550.1; -. [Q9NZ09-1] DR RefSeq; NP_001164672.1; NM_001171201.1. [Q9NZ09-4] DR RefSeq; NP_001164673.1; NM_001171202.1. [Q9NZ09-3] DR RefSeq; NP_001164674.1; NM_001171203.3. [Q9NZ09-1] DR RefSeq; NP_001164675.1; NM_001171204.3. [Q9NZ09-1] DR RefSeq; NP_057609.2; NM_016525.4. [Q9NZ09-1] DR RefSeq; XP_006716842.1; XM_006716779.5. [Q9NZ09-1] DR RefSeq; XP_047279413.1; XM_047423457.1. [Q9NZ09-1] DR RefSeq; XP_047279414.1; XM_047423458.1. [Q9NZ09-1] DR RefSeq; XP_054219056.1; XM_054363081.1. [Q9NZ09-1] DR RefSeq; XP_054219057.1; XM_054363082.1. [Q9NZ09-1] DR PDB; 1WGN; NMR; -; A=381-430. DR PDB; 4AE4; X-ray; 1.65 A; A/B=389-502. DR PDB; 5LM1; X-ray; 2.55 A; B=261-280. DR PDBsum; 1WGN; -. DR PDBsum; 4AE4; -. DR PDBsum; 5LM1; -. DR AlphaFoldDB; Q9NZ09; -. DR BMRB; Q9NZ09; -. DR SMR; Q9NZ09; -. DR BioGRID; 119424; 40. DR ComplexPortal; CPX-7181; ESCRT-I complex, VPS37A-UBAP1 variant. DR ComplexPortal; CPX-7201; ESCRT-I complex, VPS37B-UBAP1 variant. DR ComplexPortal; CPX-7202; ESCRT-I complex, VPS37C-UBAP1 variant. DR ComplexPortal; CPX-7203; ESCRT-I complex, VPS37D-UBAP1 variant. DR DIP; DIP-47291N; -. DR FunCoup; Q9NZ09; 2949. DR IntAct; Q9NZ09; 14. DR MINT; Q9NZ09; -. DR STRING; 9606.ENSP00000486574; -. DR GlyGen; Q9NZ09; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q9NZ09; -. DR PhosphoSitePlus; Q9NZ09; -. DR BioMuta; UBAP1; -. DR DMDM; 67475018; -. DR jPOST; Q9NZ09; -. DR MassIVE; Q9NZ09; -. DR PaxDb; 9606-ENSP00000297661; -. DR PeptideAtlas; Q9NZ09; -. DR ProteomicsDB; 24396; -. DR ProteomicsDB; 25363; -. DR ProteomicsDB; 83314; -. [Q9NZ09-1] DR ProteomicsDB; 83315; -. [Q9NZ09-2] DR Pumba; Q9NZ09; -. DR Antibodypedia; 11158; 208 antibodies from 30 providers. DR DNASU; 51271; -. DR Ensembl; ENST00000297661.9; ENSP00000297661.4; ENSG00000165006.15. [Q9NZ09-1] DR Ensembl; ENST00000359544.2; ENSP00000352541.2; ENSG00000165006.15. [Q9NZ09-1] DR Ensembl; ENST00000379186.8; ENSP00000368484.3; ENSG00000165006.15. [Q9NZ09-2] DR Ensembl; ENST00000625521.2; ENSP00000486574.1; ENSG00000165006.15. [Q9NZ09-4] DR GeneID; 51271; -. DR KEGG; hsa:51271; -. DR MANE-Select; ENST00000297661.9; ENSP00000297661.4; NM_016525.5; NP_057609.2. DR UCSC; uc003ztx.4; human. [Q9NZ09-1] DR AGR; HGNC:12461; -. DR ClinPGx; PA37111; -. DR CTD; 51271; -. DR DisGeNET; 51271; -. DR GeneCards; UBAP1; -. DR HGNC; HGNC:12461; UBAP1. DR HPA; ENSG00000165006; Low tissue specificity. DR MalaCards; UBAP1; -. DR MIM; 609787; gene. DR MIM; 618418; phenotype. DR OpenTargets; ENSG00000165006; -. DR Orphanet; 100993; Autosomal dominant spastic paraplegia type 12. DR Orphanet; 631068; Autosomal dominant spastic paraplegia type 80. DR VEuPathDB; HostDB:ENSG00000165006; -. DR eggNOG; ENOG502QTJC; Eukaryota. DR GeneTree; ENSGT00390000008092; -. DR HOGENOM; CLU_041679_0_0_1; -. DR InParanoid; Q9NZ09; -. DR OMA; ENWKPWP; -. DR OrthoDB; 2018023at2759; -. DR PAN-GO; Q9NZ09; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q9NZ09; -. DR PathwayCommons; Q9NZ09; -. DR Reactome; R-HSA-162588; Budding and maturation of HIV virion. DR Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins. DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT). DR Reactome; R-HSA-9610379; HCMV Late Events. DR Reactome; R-HSA-9615710; Late endosomal microautophagy. DR SignaLink; Q9NZ09; -. DR Agora; ENSG00000165006; -. DR BioGRID-ORCS; 51271; 618 hits in 1163 CRISPR screens. DR ChiTaRS; UBAP1; human. DR EvolutionaryTrace; Q9NZ09; -. DR GeneWiki; UBAP1; -. DR GenomeRNAi; 51271; -. DR Pharos; Q9NZ09; Tbio. DR PRO; PR:Q9NZ09; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9NZ09; protein. DR Bgee; ENSG00000165006; Expressed in lower esophagus mucosa and 200 other cell types or tissues. DR ExpressionAtlas; Q9NZ09; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0010008; C:endosome membrane; TAS:Reactome. DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB. DR GO; GO:0090148; P:membrane fission; NAS:ComplexPortal. DR GO; GO:0036258; P:multivesicular body assembly; NAS:ComplexPortal. DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; NAS:ComplexPortal. DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB. DR CDD; cd14315; UBA1_UBAP1; 1. DR CDD; cd14316; UBA2_UBAP1_like; 1. DR FunFam; 1.20.120.1920:FF:000001; Ubiquitin associated protein 1; 1. DR Gene3D; 1.20.120.1920; UBAP1 SOUBA domain; 1. DR InterPro; IPR015940; UBA. DR InterPro; IPR009060; UBA-like_sf. DR InterPro; IPR049467; UBAP-1-like_UBA2. DR InterPro; IPR038870; UBAP1. DR InterPro; IPR042575; UBAP1_C. DR InterPro; IPR023340; UMA. DR PANTHER; PTHR15960; LD44032P; 1. DR PANTHER; PTHR15960:SF2; UBIQUITIN-ASSOCIATED PROTEIN 1; 1. DR Pfam; PF22567; UBA_9; 1. DR Pfam; PF21267; UBAP-1_UBA2; 1. DR SUPFAM; SSF46934; UBA-like; 2. DR PROSITE; PS50030; UBA; 2. DR PROSITE; PS51497; UMA; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; Endosome; KW Hereditary spastic paraplegia; Neurodegeneration; Phosphoprotein; KW Protein transport; Proteomics identification; Reference proteome; Repeat; KW Transport. FT CHAIN 1..502 FT /note="Ubiquitin-associated protein 1" FT /id="PRO_0000211017" FT DOMAIN 17..63 FT /note="UMA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00830" FT DOMAIN 389..430 FT /note="UBA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212" FT DOMAIN 451..498 FT /note="UBA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212" FT REGION 1..95 FT /note="Interaction with ESCRT-I" FT /evidence="ECO:0000269|PubMed:24284069" FT REGION 86..117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 260..290 FT /note="Interaction with PTPN23" FT /evidence="ECO:0000269|PubMed:27839950" FT COMPBIAS 86..100 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 102..112 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 146 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 289 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..53 FT /note="MASKKLGADFHGTFSYLDDVPFKTGDKFKTPAKVGLPIGFSLPDCLQVVREV FT Q -> MSGAVRGRRREVGLQHGGCGTGGGYGDGLARSGQSWRWWRSLSLGAVGSSAGTE FT PGRPAGASTFRLLRRRQQRHSGSKWLLRSWVQIFM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046866" FT VAR_SEQ 1..11 FT /note="MASKKLGADFH -> MSGAVRGRRREVGLQHGGCGTGGGYGDGLARSGQSWR FT WWRSLSLGAVGSSAGTEPGRPAGASTFRLLRRRQQRHS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046867" FT VAR_SEQ 362..422 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_013650" FT VARIANT 125..502 FT /note="Missing (in SPG80)" FT /evidence="ECO:0000269|PubMed:30929741" FT /id="VAR_082199" FT VARIANT 176..502 FT /note="Missing (in SPG80; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31203368" FT /id="VAR_082200" FT VARIANT 357 FT /note="N -> K (in dbSNP:rs16935457)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_034577" FT MUTAGEN 17..19 FT /note="LDD->AAA: Abolishes association with the ESCRT-I FT complex." FT /evidence="ECO:0000269|PubMed:22405001" FT MUTAGEN 20..22 FT /note="VPF->AAA: Abolishes association with the ESCRT-I FT complex." FT /evidence="ECO:0000269|PubMed:22405001" FT MUTAGEN 37 FT /note="P->A: Abolishes association with the ESCRT-I FT complex." FT /evidence="ECO:0000269|PubMed:21757351" FT MUTAGEN 59 FT /note="E->G: Abolishes association with the ESCRT-I FT complex." FT /evidence="ECO:0000269|PubMed:21757351" FT MUTAGEN 268 FT /note="F->S: Abolished interaction with PTPN23." FT /evidence="ECO:0000269|PubMed:27839950" FT MUTAGEN 269 FT /note="P->A: Does not affect interaction with PTPN23." FT /evidence="ECO:0000269|PubMed:27839950" FT MUTAGEN 271 FT /note="L->A: Does not affect interaction with PTPN23." FT /evidence="ECO:0000269|PubMed:27839950" FT MUTAGEN 404 FT /note="Y->A: Strongly reduced interaction with FT ubiquitinated proteins." FT /evidence="ECO:0000269|PubMed:21757351" FT MUTAGEN 472 FT /note="F->A: Strongly reduced interaction with FT ubiquitinated proteins." FT /evidence="ECO:0000269|PubMed:21757351" FT CONFLICT 81 FT /note="C -> R (in Ref. 4; CAG38582)" FT /evidence="ECO:0000305" FT CONFLICT 187 FT /note="T -> N (in Ref. 3; BAH14025)" FT /evidence="ECO:0000305" FT CONFLICT 331 FT /note="E -> D (in Ref. 3; BAC11176)" FT /evidence="ECO:0000305" FT CONFLICT 398 FT /note="T -> M (in Ref. 3; BAH12084)" FT /evidence="ECO:0000305" FT CONFLICT 403 FT /note="G -> C (in Ref. 3; BAC11323)" FT /evidence="ECO:0000305" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:5LM1" FT HELIX 383..386 FT /evidence="ECO:0007829|PDB:1WGN" FT HELIX 390..401 FT /evidence="ECO:0007829|PDB:4AE4" FT HELIX 406..416 FT /evidence="ECO:0007829|PDB:4AE4" FT HELIX 420..435 FT /evidence="ECO:0007829|PDB:4AE4" FT HELIX 440..449 FT /evidence="ECO:0007829|PDB:4AE4" FT HELIX 454..469 FT /evidence="ECO:0007829|PDB:4AE4" FT HELIX 474..483 FT /evidence="ECO:0007829|PDB:4AE4" FT TURN 484..486 FT /evidence="ECO:0007829|PDB:4AE4" FT HELIX 488..498 FT /evidence="ECO:0007829|PDB:4AE4" SQ SEQUENCE 502 AA; 55084 MW; 548457B0B2ABC0F4 CRC64; MASKKLGADF HGTFSYLDDV PFKTGDKFKT PAKVGLPIGF SLPDCLQVVR EVQYDFSLEK KTIEWAEEIK KIEEAEREAE CKIAEAEAKV NSKSGPEGDS KMSFSKTHST ATMPPPINPI LASLQHNSIL TPTRVSSSAT KQKVLSPPHI KADFNLADFE CEEDPFDNLE LKTIDEKEEL RNILVGTTGP IMAQLLDNNL PRGGSGSVLQ DEEVLASLER ATLDFKPLHK PNGFITLPQL GNCEKMSLSS KVSLPPIPAV SNIKSLSFPK LDSDDSNQKT AKLASTFHST SCLRNGTFQN SLKPSTQSSA SELNGHHTLG LSALNLDSGT EMPALTSSQM PSLSVLSVCT EESSPPNTGP TVTPPNFSVS QVPNMPSCPQ AYSELQMLSP SERQCVETVV NMGYSYECVL RAMKKKGENI EQILDYLFAH GQLCEKGFDP LLVEEALEMH QCSEEKMMEF LQLMSKFKEM GFELKDIKEV LLLHNNDQDN ALEDLMARAG AS //