COG3_HUMAN
ID COG3_HUMAN Reviewed; 828 AA.
AC Q96JB2; B2RAW5; Q5VT70; Q8IXX4; Q9BZ92;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Conserved oligomeric Golgi complex subunit 3;
DE Short=COG complex subunit 3;
DE AltName: Full=Component of oligomeric Golgi complex 3;
DE AltName: Full=Vesicle-docking protein SEC34 homolog;
DE AltName: Full=p94;
GN Name=COG3; Synonyms=SEC34;
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11292827; DOI=10.1074/jbc.m011624200;
RA Suvorova E.S., Kurten R.C., Lupashin V.V.;
RT "Identification of a human ortholog of Sec34p as a component of the cis-
RT Golgi vesicle tethering machinery.";
RL J. Biol. Chem. 276:22810-22818(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT SER-747.
RX PubMed=11929878; DOI=10.1074/jbc.m202326200;
RA Loh E., Hong W.;
RT "Sec34 is implicated in traffic from the endoplasmic reticulum to the Golgi
RT and exists in a complex with GTC-90 and ldlBp.";
RL J. Biol. Chem. 277:21955-21961(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Leukocyte;
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 [6]
RP PROTEIN SEQUENCE OF 2-16, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [14]
RP INTERACTION WITH TMEM115.
RX PubMed=24806965; DOI=10.1242/jcs.136754;
RA Ong Y.S., Tran T.H., Gounko N.V., Hong W.;
RT "TMEM115 is an integral membrane protein of the Golgi complex involved in
RT retrograde transport.";
RL J. Cell Sci. 127:2825-2839(2014).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-620.
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).
CC -!- FUNCTION: Involved in ER-Golgi transport.
CC {ECO:0000269|PubMed:11929878}.
CC -!- SUBUNIT: Component of the conserved oligomeric Golgi complex which is
CC composed of eight different subunits and is required for normal Golgi
CC morphology and localization. Interacts with TMEM115. {ECO:0000250,
CC ECO:0000269|PubMed:24806965}.
CC -!- INTERACTION:
CC Q96JB2-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-9091495, EBI-11096309;
CC Q96JB2-2; Q9BW66: CINP; NbExp=3; IntAct=EBI-9091495, EBI-739784;
CC Q96JB2-2; Q13561: DCTN2; NbExp=3; IntAct=EBI-9091495, EBI-715074;
CC Q96JB2-2; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-9091495, EBI-14069005;
CC Q96JB2-2; O14901: KLF11; NbExp=3; IntAct=EBI-9091495, EBI-948266;
CC Q96JB2-2; Q9BVL2: NUP58; NbExp=6; IntAct=EBI-9091495, EBI-2811583;
CC Q96JB2-2; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-9091495, EBI-742688;
CC Q96JB2-2; Q9C040: TRIM2; NbExp=3; IntAct=EBI-9091495, EBI-749840;
CC Q96JB2-2; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-9091495, EBI-10687282;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:11292827}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11292827}. Note=Associated with the peripheral
CC membrane of cis/medial cisternae.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96JB2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JB2-2; Sequence=VSP_013652, VSP_013653;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in pancreas
CC and testis and lowest levels in lung. {ECO:0000269|PubMed:11292827}.
CC -!- SIMILARITY: Belongs to the COG3 family. {ECO:0000305}.
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DR EMBL; AF349676; AAK66974.1; -; mRNA.
DR EMBL; AF332595; AAK06848.1; -; mRNA.
DR EMBL; AK314387; BAG37012.1; -; mRNA.
DR EMBL; AL139326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038953; AAH38953.1; -; mRNA.
DR CCDS; CCDS9398.1; -. [Q96JB2-1]
DR RefSeq; NP_113619.2; NM_031431.3. [Q96JB2-1]
DR AlphaFoldDB; Q96JB2; -.
DR SMR; Q96JB2; -.
DR BioGRID; 123680; 106.
DR ComplexPortal; CPX-6199; COG tethering complex.
DR CORUM; Q96JB2; -.
DR IntAct; Q96JB2; 44.
DR MINT; Q96JB2; -.
DR STRING; 9606.ENSP00000258654; -.
DR ChEMBL; CHEMBL4105842; -.
DR GlyGen; Q96JB2; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q96JB2; -.
DR PhosphoSitePlus; Q96JB2; -.
DR BioMuta; COG3; -.
DR DMDM; 85701302; -.
DR EPD; Q96JB2; -.
DR jPOST; Q96JB2; -.
DR MassIVE; Q96JB2; -.
DR MaxQB; Q96JB2; -.
DR PaxDb; Q96JB2; -.
DR PeptideAtlas; Q96JB2; -.
DR PRIDE; Q96JB2; -.
DR ProteomicsDB; 76926; -. [Q96JB2-1]
DR ProteomicsDB; 76927; -. [Q96JB2-2]
DR Antibodypedia; 23637; 164 antibodies from 25 providers.
DR DNASU; 83548; -.
DR Ensembl; ENST00000349995.10; ENSP00000258654.8; ENSG00000136152.15. [Q96JB2-1]
DR Ensembl; ENST00000617493.1; ENSP00000481332.1; ENSG00000136152.15. [Q96JB2-2]
DR GeneID; 83548; -.
DR KEGG; hsa:83548; -.
DR MANE-Select; ENST00000349995.10; ENSP00000258654.8; NM_031431.4; NP_113619.3.
DR UCSC; uc001vai.4; human. [Q96JB2-1]
DR CTD; 83548; -.
DR DisGeNET; 83548; -.
DR GeneCards; COG3; -.
DR HGNC; HGNC:18619; COG3.
DR HPA; ENSG00000136152; Low tissue specificity.
DR MIM; 606975; gene.
DR neXtProt; NX_Q96JB2; -.
DR OpenTargets; ENSG00000136152; -.
DR PharmGKB; PA38602; -.
DR VEuPathDB; HostDB:ENSG00000136152; -.
DR eggNOG; KOG2604; Eukaryota.
DR GeneTree; ENSGT00390000015682; -.
DR HOGENOM; CLU_011639_1_1_1; -.
DR InParanoid; Q96JB2; -.
DR OMA; LDEFELW; -.
DR OrthoDB; 692986at2759; -.
DR PhylomeDB; Q96JB2; -.
DR TreeFam; TF314200; -.
DR PathwayCommons; Q96JB2; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; Q96JB2; -.
DR BioGRID-ORCS; 83548; 608 hits in 1099 CRISPR screens.
DR ChiTaRS; COG3; human.
DR GeneWiki; COG3; -.
DR GenomeRNAi; 83548; -.
DR Pharos; Q96JB2; Tbio.
DR PRO; PR:Q96JB2; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q96JB2; protein.
DR Bgee; ENSG00000136152; Expressed in body of pancreas and 159 other tissues.
DR ExpressionAtlas; Q96JB2; baseline and differential.
DR Genevisible; Q96JB2; HS.
DR GO; GO:0005801; C:cis-Golgi network; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0017119; C:Golgi transport complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0070085; P:glycosylation; IMP:ComplexPortal.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IMP:UniProtKB.
DR GO; GO:0033365; P:protein localization to organelle; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:ComplexPortal.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR InterPro; IPR007265; COG_su3.
DR PANTHER; PTHR13302; PTHR13302; 1.
DR Pfam; PF04136; Sec34; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..828
FT /note="Conserved oligomeric Golgi complex subunit 3"
FT /id="PRO_0000213500"
FT REGION 504..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 443..444
FT /note="AE -> GK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013652"
FT VAR_SEQ 445..828
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013653"
FT VARIANT 620
FT /note="R -> C (in a breast cancer sample; somatic mutation;
FT dbSNP:rs747042102)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036454"
FT VARIANT 747
FT /note="N -> S (in dbSNP:rs2274285)"
FT /evidence="ECO:0000269|PubMed:11929878"
FT /id="VAR_055663"
FT CONFLICT 106..107
FT /note="QQ -> HE (in Ref. 1; AAK66974)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="L -> S (in Ref. 1; AAK66974, 2; AAK06848 and 3;
FT BAG37012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 828 AA; 94096 MW; B3DCF03FD4DC6A60 CRC64;
MAEAALLLLP EAAAERDARE KLALWDRRPD TTAPLTDRQT DSVLELKAAA ENLPVPAELP
IEDLCSLTSQ SLPIELTSVV PESTEDILLK GFTSLGMEEE RIETAQQFFS WFAKLQTQMD
QDEGTKYRQM RDYLSGFQEQ CDAILNDVNS ALQHLESLQK QYLFVSNKTG TLHEACEQLL
KEQSELVDLA ENIQQKLSYF NELETINTKL NSPTLSVNSD GFIPMLAKLD DCITYISSHP
NFKDYPIYLL KFKQCLSKAL HLMKTYTVNT LQTLTSQLLK RDPSSVPNAD NAFTLFYVKF
RAAAPKVRTL IEQIELRSEK IPEYQQLLND IHQCYLDQRE LLLGPSIACT VAELTSQNNR
DHCALVRSGC AFMVHVCQDE HQLYNEFFTK PTSKLDELLE KLCVSLYDVF RPLIIHVIHL
ETLSELCGIL KNEVLEDHVQ NNAEQLGAFA AGVKQMLEDV QERLVYRTHI YIQTDITGYK
PAPGDLAYPD KLVMMEQIAQ SLKDEQKKVP SEASFSDVHL EEGESNSLTK SGSTESLNPR
PQTTISPADL HGMWYPTVRR TLVCLSKLYR CIDRAVFQGL SQEALSACIQ SLLGASESIS
KNKTQIDGQL FLIKHLLILR EQIAPFHTEF TIKEISLDLK KTRDAAFKIL NPMTVPRFFR
LNSNNALIEF LLEGTPEIRE HYLDSKKDVD RHLKSACEQF IQQQTKLFVE QLEEFMTKVS
ALKTMASQGG PKYTLSQQPW AQPAKVNDLA ATAYKTIKTK LPVTLRSMSL YLSNKDTEFI
LFKPVRNNIQ QVFQKFHALL KEEFSPEDIQ IIACPSMEQL SLLLLVSK
