ID   AKIR1_HUMAN             Reviewed;         192 AA.
AC   Q9H9L7; B4DZU6; Q0VDB3; Q53FK8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   28-JAN-2026, entry version 147.
DE   RecName: Full=Akirin-1 {ECO:0000305};
GN   Name=AKIRIN1 {ECO:0000303|PubMed:18066067,
GN   ECO:0000312|HGNC:HGNC:25744};
GN   Synonyms=C1orf108 {ECO:0000312|HGNC:HGNC:25744};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Thymus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=18066067; DOI=10.1038/ni1543;
RA   Goto A., Matsushita K., Gesellchen V., El Chamy L., Kuttenkeuler D.,
RA   Takeuchi O., Hoffmann J.A., Akira S., Boutros M., Reichhart J.-M.;
RT   "Akirins are highly conserved nuclear proteins required for NF-kappaB-
RT   dependent gene expression in Drosophila and mice.";
RL   Nat. Immunol. 9:97-104(2008).
RN   [5]
RP   ERRATUM OF PUBMED:18066067.
RA   Goto A., Matsushita K., Gesellchen V., El Chamy L., Kuttenkeuler D.,
RA   Takeuchi O., Hoffmann J.A., Akira S., Boutros M., Reichhart J.-M.;
RL   Nat. Immunol. 9:216-216(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND THR-72, 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   [9]
RP   FUNCTION.
RX   PubMed=34711951; DOI=10.1038/s41586-021-04035-8;
RA   de Almeida M., Hinterndorfer M., Brunner H., Grishkovskaya I., Singh K.,
RA   Schleiffer A., Jude J., Deswal S., Kalis R., Vunjak M., Lendl T., Imre R.,
RA   Roitinger E., Neumann T., Kandolf S., Schutzbier M., Mechtler K.,
RA   Versteeg G.A., Haselbach D., Zuber J.;
RT   "AKIRIN2 controls the nuclear import of proteasomes in vertebrates.";
RL   Nature 599:491-496(2021).
CC   -!- FUNCTION: Molecular adapter that acts as a bridge between proteins, and
CC       which is involved skeletal muscle development (By similarity).
CC       Functions as a signal transducer for MSTN during skeletal muscle
CC       regeneration and myogenesis (By similarity). May regulate chemotaxis of
CC       both macrophages and myoblasts by reorganising actin cytoskeleton,
CC       leading to more efficient lamellipodia formation via a PI3 kinase
CC       dependent pathway (By similarity). In contrast to AKIRIN2, not involved
CC       in nuclear import of proteasomes (PubMed:34711951).
CC       {ECO:0000250|UniProtKB:Q99LF1, ECO:0000269|PubMed:34711951}.
CC   -!- INTERACTION:
CC       Q9H9L7; Q9HD26: GOPC; NbExp=3; IntAct=EBI-10309796, EBI-349832;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18066067}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H9L7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H9L7-2; Sequence=VSP_042769;
CC   -!- TISSUE SPECIFICITY: Widely expressed with the highest expression in
CC       heart, liver, placenta and peripheral blood leukocytes.
CC       {ECO:0000269|PubMed:18066067}.
CC   -!- MISCELLANEOUS: 'Akiraka ni suru' means 'making things clear' in
CC       Japanese. The name is given based on the presence of the clear nuclear
CC       localization signal. {ECO:0000305|PubMed:18066067}.
CC   -!- SIMILARITY: Belongs to the akirin family.
CC       {ECO:0000305|PubMed:18066067}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI19747.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK022728; BAB14208.1; -; mRNA.
DR   EMBL; AK223276; BAD96996.1; -; mRNA.
DR   EMBL; AK303098; BAG64208.1; -; mRNA.
DR   EMBL; AL606465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC119745; AAI19746.1; -; mRNA.
DR   EMBL; BC119746; AAI19747.1; ALT_INIT; mRNA.
DR   CCDS; CCDS433.1; -. [Q9H9L7-1]
DR   CCDS; CCDS44113.1; -. [Q9H9L7-2]
DR   RefSeq; NP_001129747.1; NM_001136275.2. [Q9H9L7-2]
DR   RefSeq; NP_078871.1; NM_024595.3. [Q9H9L7-1]
DR   AlphaFoldDB; Q9H9L7; -.
DR   SMR; Q9H9L7; -.
DR   BioGRID; 122775; 26.
DR   FunCoup; Q9H9L7; 4432.
DR   IntAct; Q9H9L7; 11.
DR   STRING; 9606.ENSP00000392678; -.
DR   GlyGen; Q9H9L7; 1 site.
DR   iPTMnet; Q9H9L7; -.
DR   PhosphoSitePlus; Q9H9L7; -.
DR   BioMuta; AKIRIN1; -.
DR   DMDM; 74752744; -.
DR   jPOST; Q9H9L7; -.
DR   MassIVE; Q9H9L7; -.
DR   PaxDb; 9606-ENSP00000392678; -.
DR   PeptideAtlas; Q9H9L7; -.
DR   ProteomicsDB; 81331; -. [Q9H9L7-1]
DR   ProteomicsDB; 81332; -. [Q9H9L7-2]
DR   Antibodypedia; 31846; 125 antibodies from 21 providers.
DR   DNASU; 79647; -.
DR   Ensembl; ENST00000432648.8; ENSP00000392678.3; ENSG00000174574.17. [Q9H9L7-1]
DR   Ensembl; ENST00000446189.6; ENSP00000389866.2; ENSG00000174574.17. [Q9H9L7-2]
DR   GeneID; 79647; -.
DR   KEGG; hsa:79647; -.
DR   MANE-Select; ENST00000432648.8; ENSP00000392678.3; NM_024595.3; NP_078871.1.
DR   UCSC; uc001ccw.4; human. [Q9H9L7-1]
DR   AGR; HGNC:25744; -.
DR   ClinPGx; PA162376180; -.
DR   CTD; 79647; -.
DR   DisGeNET; 79647; -.
DR   GeneCards; AKIRIN1; -.
DR   HGNC; HGNC:25744; AKIRIN1.
DR   HPA; ENSG00000174574; Low tissue specificity.
DR   MIM; 615164; gene.
DR   OpenTargets; ENSG00000174574; -.
DR   VEuPathDB; HostDB:ENSG00000174574; -.
DR   eggNOG; KOG4330; Eukaryota.
DR   GeneTree; ENSGT00940000158787; -.
DR   InParanoid; Q9H9L7; -.
DR   OMA; PMGGEHR; -.
DR   OrthoDB; 10039914at2759; -.
DR   PAN-GO; Q9H9L7; 9 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9H9L7; -.
DR   PathwayCommons; Q9H9L7; -.
DR   SignaLink; Q9H9L7; -.
DR   Agora; ENSG00000174574; -.
DR   BioGRID-ORCS; 79647; 74 hits in 1156 CRISPR screens.
DR   ChiTaRS; AKIRIN1; human.
DR   GenomeRNAi; 79647; -.
DR   Pharos; Q9H9L7; Tbio.
DR   PRO; PR:Q9H9L7; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9H9L7; protein.
DR   Bgee; ENSG00000174574; Expressed in sperm and 197 other cell types or tissues.
DR   ExpressionAtlas; Q9H9L7; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; ISS:UniProtKB.
DR   GO; GO:1902725; P:negative regulation of satellite cell differentiation; ISS:UniProtKB.
DR   GO; GO:1902723; P:negative regulation of skeletal muscle satellite cell proliferation; ISS:UniProtKB.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR   GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISS:UniProtKB.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   CDD; cd22243; akirin-1; 1.
DR   InterPro; IPR024132; Akirin.
DR   PANTHER; PTHR13293:SF9; AKIRIN-1; 1.
DR   PANTHER; PTHR13293; AKIRIN-RELATED; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein; Proteomics identification;
KW   Reference proteome.
FT   CHAIN           1..192
FT                   /note="Akirin-1"
FT                   /id="PRO_0000274318"
FT   REGION          17..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           23..28
FT                   /note="Nuclear localization signal"
FT   MOTIF           189..192
FT                   /note="SYVS motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H80"
FT   COMPBIAS        31..49
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..60
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         72
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         121..165
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042769"
FT   CONFLICT        39
FT                   /note="R -> G (in Ref. 1; BAD96996)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   192 AA;  21867 MW;  21D7B2E6E026A802 CRC64;
     MACGATLKRP MEFEAALLSP GSPKRRRCAP LPGPTPGLRP PDAEPPPPFQ TQTPPQSLQQ
     PAPPGSERRL PTPEQIFQNI KQEYSRYQRW RHLEVVLNQS EACASESQPH SSALTAPSSP
     GSSWMKKDQP TFTLRQVGII CERLLKDYED KIREEYEQIL NTKLAEQYES FVKFTHDQIM
     RRYGTRPTSY VS
//