ID   DJC21_HUMAN             Reviewed;         531 AA.
AC   Q5F1R6; Q3B7J9; Q6P086; Q6ZS43; Q86VC6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   28-JAN-2026, entry version 162.
DE   RecName: Full=DnaJ homolog subfamily C member 21;
DE   AltName: Full=DnaJ homolog subfamily A member 5;
DE   AltName: Full=Protein GS3;
GN   Name=DNAJC21; Synonyms=DNAJA5;
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.
RC   TISSUE=Fetal brain;
RX   PubMed=15067379;
RA   Chen J., Yin G., Lu Y., Lou M., Cheng H., Ni X., Hu G., Luo C., Ying K.,
RA   Xie Y., Mao Y.;
RT   "Cloning and characterization of a novel human cDNA encoding a J-domain
RT   protein (DNAJA5) from the fetal brain.";
RL   Int. J. Mol. Med. 13:735-740(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Chen J., Xie Y., Mao Y.;
RT   "Cloning and characterization of a novel GS3 protein.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 126-458 (ISOFORM 3).
RC   TISSUE=Skin, and Uterus;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-531 (ISOFORM 2).
RC   TISSUE=Brain;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-302 AND SER-370, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION BY
RP   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-370, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-370, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, 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   [12]
RP   VARIANT [LARGE SCALE ANALYSIS] ASN-214.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [13]
RP   VARIANT BMFS3 ALA-32, INVOLVEMENT IN BMFS3, INTERACTION WITH HSPA8; PA2G4
RP   AND ZNF622, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT BMFS3 ALA-32,
RP   AND FUNCTION.
RX   PubMed=27346687; DOI=10.1016/j.ajhg.2016.05.002;
RA   Tummala H., Walne A.J., Williams M., Bockett N., Collopy L., Cardoso S.,
RA   Ellison A., Wynn R., Leblanc T., Fitzgibbon J., Kelsell D.P.,
RA   van Heel D.A., Payne E., Plagnol V., Dokal I., Vulliamy T.;
RT   "DNAJC21 mutations link a cancer-prone bone marrow failure syndrome to
RT   corruption in 60S ribosome subunit maturation.";
RL   Am. J. Hum. Genet. 99:115-124(2016).
CC   -!- FUNCTION: May act as a co-chaperone for HSP70. May play a role in
CC       ribosomal RNA (rRNA) biogenesis, possibly in the maturation of the 60S
CC       subunit. Binds the precursor 45S rRNA. {ECO:0000269|PubMed:27346687}.
CC   -!- SUBUNIT: Interacts with HSPA8, PA2G4 and ZNF622.
CC       {ECO:0000269|PubMed:27346687}.
CC   -!- INTERACTION:
CC       Q5F1R6; P42858: HTT; NbExp=6; IntAct=EBI-2654581, EBI-466029;
CC       Q5F1R6; Q99551: MTERF1; NbExp=2; IntAct=EBI-2654581, EBI-2690033;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27346687}. Nucleus
CC       {ECO:0000269|PubMed:27346687}. Nucleus, nucleolus
CC       {ECO:0000269|PubMed:27346687}. Note=Within the nucleus, localizes
CC       primarily to the nucleolus. {ECO:0000269|PubMed:27346687}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5F1R6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5F1R6-2; Sequence=VSP_024005;
CC       Name=3;
CC         IsoId=Q5F1R6-3; Sequence=VSP_024004;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, placenta, kidney and pancreas.
CC       {ECO:0000269|PubMed:15067379}.
CC   -!- DISEASE: Bone marrow failure syndrome 3 (BMFS3) [MIM:617052]: A form of
CC       bone marrow failure syndrome, a heterogeneous group of life-threatening
CC       disorders characterized by hematopoietic defects in association with a
CC       range of variable extra-hematopoietic manifestations. BMFS3 is
CC       characterized by pancytopenia with onset in early childhood. Some
CC       patients have additional variable non-specific features, including poor
CC       growth, microcephaly, and skin anomalies. BMFS3 inheritance is
CC       autosomal recessive. {ECO:0000269|PubMed:27346687}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH65745.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAI07578.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAC87112.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY258422; AAP81807.1; -; mRNA.
DR   EMBL; AY177688; AAO46910.1; -; mRNA.
DR   EMBL; BC050472; AAH50472.1; -; mRNA.
DR   EMBL; BC065745; AAH65745.1; ALT_SEQ; mRNA.
DR   EMBL; BC107577; AAI07578.1; ALT_SEQ; mRNA.
DR   EMBL; AK127749; BAC87112.1; ALT_INIT; mRNA.
DR   CCDS; CCDS34144.1; -. [Q5F1R6-1]
DR   CCDS; CCDS3907.2; -. [Q5F1R6-2]
DR   CCDS; CCDS87294.1; -. [Q5F1R6-3]
DR   RefSeq; NP_001012339.2; NM_001012339.3. [Q5F1R6-1]
DR   RefSeq; NP_001335349.1; NM_001348420.2. [Q5F1R6-3]
DR   RefSeq; NP_919259.3; NM_194283.4. [Q5F1R6-2]
DR   AlphaFoldDB; Q5F1R6; -.
DR   SMR; Q5F1R6; -.
DR   BioGRID; 126389; 87.
DR   FunCoup; Q5F1R6; 1930.
DR   IntAct; Q5F1R6; 35.
DR   STRING; 9606.ENSP00000371451; -.
DR   iPTMnet; Q5F1R6; -.
DR   PhosphoSitePlus; Q5F1R6; -.
DR   BioMuta; DNAJC21; -.
DR   DMDM; 296434479; -.
DR   jPOST; Q5F1R6; -.
DR   MassIVE; Q5F1R6; -.
DR   PeptideAtlas; Q5F1R6; -.
DR   ProteomicsDB; 62776; -. [Q5F1R6-1]
DR   ProteomicsDB; 62777; -. [Q5F1R6-2]
DR   ProteomicsDB; 62778; -. [Q5F1R6-3]
DR   Pumba; Q5F1R6; -.
DR   Antibodypedia; 22862; 56 antibodies from 14 providers.
DR   DNASU; 134218; -.
DR   Ensembl; ENST00000382021.2; ENSP00000371451.2; ENSG00000168724.19. [Q5F1R6-2]
DR   Ensembl; ENST00000642851.1; ENSP00000496545.1; ENSG00000168724.19. [Q5F1R6-3]
DR   Ensembl; ENST00000648817.1; ENSP00000497410.1; ENSG00000168724.19. [Q5F1R6-1]
DR   GeneID; 134218; -.
DR   KEGG; hsa:134218; -.
DR   MANE-Select; ENST00000648817.1; ENSP00000497410.1; NM_001012339.3; NP_001012339.2.
DR   UCSC; uc003jjb.3; human. [Q5F1R6-1]
DR   AGR; HGNC:27030; -.
DR   ClinPGx; PA162383874; -.
DR   CTD; 134218; -.
DR   DisGeNET; 134218; -.
DR   GeneCards; DNAJC21; -.
DR   GeneReviews; DNAJC21; -.
DR   HGNC; HGNC:27030; DNAJC21.
DR   HPA; ENSG00000168724; Low tissue specificity.
DR   MalaCards; DNAJC21; -.
DR   MIM; 617048; gene.
DR   MIM; 617052; phenotype.
DR   OpenTargets; ENSG00000168724; -.
DR   Orphanet; 811; Shwachman-Diamond syndrome.
DR   VEuPathDB; HostDB:ENSG00000168724; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   eggNOG; KOG0717; Eukaryota.
DR   GeneTree; ENSGT00510000047097; -.
DR   HOGENOM; CLU_009539_1_0_1; -.
DR   InParanoid; Q5F1R6; -.
DR   OMA; RANHEES; -.
DR   OrthoDB; 5894at2759; -.
DR   PAN-GO; Q5F1R6; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; Q5F1R6; -.
DR   PathwayCommons; Q5F1R6; -.
DR   SignaLink; Q5F1R6; -.
DR   Agora; ENSG00000168724; -.
DR   BioGRID-ORCS; 134218; 60 hits in 1159 CRISPR screens.
DR   CD-CODE; 91857CE7; Nucleolus.
DR   ChiTaRS; DNAJC21; human.
DR   GenomeRNAi; 134218; -.
DR   Pharos; Q5F1R6; Tdark.
DR   PRO; PR:Q5F1R6; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q5F1R6; protein.
DR   Bgee; ENSG00000168724; Expressed in epithelial cell of pancreas and 185 other cell types or tissues.
DR   ExpressionAtlas; Q5F1R6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005840; C:ribosome; NAS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; NAS:UniProtKB.
DR   CDD; cd06257; DnaJ; 1.
DR   FunFam; 1.10.287.110:FF:000046; dnaJ homolog subfamily C member 21; 1.
DR   FunFam; 3.30.160.60:FF:001809; dnaJ homolog subfamily C member 21 isoform X1; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   InterPro; IPR051964; Chaperone_stress_response.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR054076; ZUO1-like_ZHD.
DR   PANTHER; PTHR44029; DNAJ HOMOLOG SUBFAMILY C MEMBER 21; 1.
DR   PANTHER; PTHR44029:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 21; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   Pfam; PF21884; ZUO1-like_ZHD; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SMART; SM00451; ZnF_U1; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chaperone; Cytoplasm; Metal-binding; Nucleus;
KW   Phosphoprotein; Proteomics identification; Reference proteome; Repeat;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..531
FT                   /note="DnaJ homolog subfamily C member 21"
FT                   /id="PRO_0000281475"
FT   DOMAIN          3..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   ZN_FING         314..338
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         482..506
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          279..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..311
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..375
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..392
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..464
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..522
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983"
FT   MOD_RES         370
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         381
FT                   /note="K -> KVKYLTFRFIFALR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024004"
FT   VAR_SEQ         395
FT                   /note="Q -> QDVPGKDSYLPAAHFQMAWGKKCVLGERRDGESEHKCAKMLLENRQ
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_024005"
FT   VARIANT         32
FT                   /note="P -> A (in BMFS3; loss of HSPA8-binding; no effect
FT                   on PA2G4-, nor on ZNF622-binding; dbSNP:rs879253818)"
FT                   /evidence="ECO:0000269|PubMed:27346687"
FT                   /id="VAR_076802"
FT   VARIANT         214
FT                   /note="D -> N (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036163"
FT   VARIANT         433
FT                   /note="E -> K (in dbSNP:rs34908091)"
FT                   /id="VAR_061145"
FT   CONFLICT        509
FT                   /note="A -> V (in Ref. 1; AAP81807 and 2; AAO46910)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   531 AA;  62028 MW;  D1D3ED9AD6505613 CRC64;
     MKCHYEALGV RRDASEEELK KAYRKLALKW HPDKNLDNAA EAAEQFKLIQ AAYDVLSDPQ
     ERAWYDNHRE ALLKGGFDGE YQDDSLDLLR YFTVTCYSGY GDDEKGFYTV YRNVFEMIAK
     EELESVLEEE VDDFPTFGDS QSDYDTVVHP FYAYWQSFCT QKNFAWKEEY DTRQASNRWE
     KRAMEKENKK IRDKARKEKN ELVRQLVAFI RKRDKRVQAH RKLVEEQNAE KARKAEEMRR
     QQKLKQAKLV EQYREQSWMT MANLEKELQE MEARYEKEFG DGSDENEMEE HELKDEEDGK
     DSDEAEDAEL YDDLYCPACD KSFKTEKAMK NHEKSKKHRE MVALLKQQLE EEEENFSRPQ
     IDENPLDDNS EEEMEDAPKQ KLSKKQKKKK QKPAQNYDDN FNVNGPGEGV KVDPEDTNLN
     QDSAKELEDS PQENVSVTEI IKPCDDPKSE AKSVPKPKGK KTKDMKKPVR VPAEPQTMSV
     LISCTTCHSE FPSRNKLFDH LKATGHARAP SSSSLNSATS SQSKKEKRKN R
//