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Keratin, type II cytoskeletal 7 (Cytokeratin-7) (CK-7) (Keratin-7) (K7) (Sarcolectin) (Type-II keratin Kb7)

 K2C7_HUMAN              Reviewed;         469 AA.
P08729; Q92676; Q9BUD8; Q9Y3R7;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 5.
25-OCT-2017, entry version 190.
RecName: Full=Keratin, type II cytoskeletal 7;
AltName: Full=Cytokeratin-7;
Short=CK-7;
AltName: Full=Keratin-7;
Short=K7;
AltName: Full=Sarcolectin;
AltName: Full=Type-II keratin Kb7;
Name=KRT7; Synonyms=SCL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS ARG-186
AND ALA-364.
TISSUE=Mesothelium;
PubMed=2415537; DOI=10.1083/jcb.101.6.2366;
Glass C., Kim K.H., Fuchs E.;
"Sequence and expression of a human type II mesothelial keratin.";
J. Cell Biol. 101:2366-2373(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION,
AND VARIANTS ARG-186 AND ALA-364.
PubMed=2459129; DOI=10.1083/jcb.107.4.1337;
Glass C., Fuchs E.;
"Isolation, sequence, and differential expression of a human K7 gene
in simple epithelial cells.";
J. Cell Biol. 107:1337-1350(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANTS ARG-186 AND
ALA-364.
TISSUE=Placenta;
PubMed=10492017; DOI=10.1016/S0300-9084(99)80128-X;
Kaba A., Jiang P., Chany-Fournier F., Chany C.;
"Sarcolectin (SCL): structure and expression of the recombinant
molecule.";
Biochimie 81:709-715(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
VARIANTS ARG-186 AND ALA-364.
TISSUE=Keratinocyte;
PubMed=12359226; DOI=10.1016/S0006-291X(02)02288-X;
Smith F.J.D., Porter R.M., Corden L.D., Lunny D.P., Lane E.B.,
McLean W.H.I.;
"Cloning of human, murine, and marsupial keratin 7 and a survey of K7
expression in the mouse.";
Biochem. Biophys. Res. Commun. 297:818-827(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-186 AND
ALA-364.
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-48; 53-96; 102-110; 123-130; 137-161; 178-208;
215-273; 277-296; 306-313; 318-326; 330-348; 352-363 AND 374-402,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT
ARG-20, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A.,
Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[8]
INTERACTION WITH EIF3S10.
PubMed=11169732;
DOI=10.1002/1097-4644(20010315)80:4<483::AID-JCB1002>3.0.CO;2-B;
Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.;
"Molecular interaction between human tumor marker protein p150, the
largest subunit of eIF3, and intermediate filament protein K7.";
J. Cell. Biochem. 80:483-490(2001).
[9]
FUNCTION, AND INTERACTION WITH HPV16 E7.
PubMed=12072504; DOI=10.1128/JVI.76.14.7040-7048.2002;
Kanduc D.;
"Translational regulation of human papillomavirus type 16 E7 mRNA by
the peptide SEQIKA, shared by rabbit alpha(1)-globin and human
cytokeratin 7.";
J. Virol. 76:7040-7048(2002).
[10]
MASS SPECTROMETRY.
TISSUE=Mammary cancer;
PubMed=11840567;
DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H;
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
Zvelebil M.J.;
"Cluster analysis of an extensive human breast cancer cell line
protein expression map database.";
Proteomics 2:212-223(2002).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-254, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
INTERACTION WITH GPER1.
PubMed=21149639; DOI=10.1124/mol.110.069500;
Sanden C., Broselid S., Cornmark L., Andersson K.,
Daszkiewicz-Nilsson J., Martensson U.E., Olde B., Leeb-Lundberg L.M.;
"G protein-coupled estrogen receptor 1/G protein-coupled receptor 30
localizes in the plasma membrane and traffics intracellularly on
cytokeratin intermediate filaments.";
Mol. Pharmacol. 79:400-410(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-6; SER-7; SER-53;
SER-71; SER-83; THR-97; SER-254 AND THR-289, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130; LYS-265; LYS-286;
LYS-296 AND LYS-331, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[21]
VARIANT [LARGE SCALE ANALYSIS] ARG-186, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Blocks interferon-dependent interphase and stimulates
DNA synthesis in cells. Involved in the translational regulation
of the human papillomavirus type 16 E7 mRNA (HPV16 E7).
{ECO:0000269|PubMed:10492017, ECO:0000269|PubMed:12072504}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
Interacts with eukaryotic translation initiator factor 3 (eIF3)
subunit EIF3S10 and with HPV16 E7. Interacts with GPER1.
{ECO:0000269|PubMed:11169732, ECO:0000269|PubMed:12072504,
ECO:0000269|PubMed:21149639}.
-!- INTERACTION:
Q14152:EIF3A; NbExp=3; IntAct=EBI-297833, EBI-366617;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2459129}.
-!- TISSUE SPECIFICITY: Expressed in cultured epidermal, bronchial and
mesothelial cells but absent in colon, ectocervix and liver.
Observed throughout the glandular cells in the junction between
stomach and esophagus but is absent in the esophagus.
{ECO:0000269|PubMed:12359226, ECO:0000269|PubMed:2415537}.
-!- INDUCTION: Up-regulated by retinoic acid.
{ECO:0000269|PubMed:2459129}.
-!- PTM: Arg-20 is dimethylated, probably to asymmetric
dimethylarginine.
-!- MASS SPECTROMETRY: Mass=51203.48; Method=MALDI; Range=2-469;
Evidence={ECO:0000269|PubMed:11840567};
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-!- SEQUENCE CAUTION:
Sequence=CAA26956.2; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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EMBL; X03212; CAA26956.2; ALT_SEQ; mRNA.
EMBL; X13320; CAA31695.1; -; Genomic_DNA.
EMBL; X13346; CAA31695.1; JOINED; Genomic_DNA.
EMBL; X13347; CAA31695.1; JOINED; Genomic_DNA.
EMBL; X13348; CAA31695.1; JOINED; Genomic_DNA.
EMBL; X13349; CAA31695.1; JOINED; Genomic_DNA.
EMBL; X13350; CAA31695.1; JOINED; Genomic_DNA.
EMBL; X13351; CAA31695.1; JOINED; Genomic_DNA.
EMBL; X13352; CAA31695.1; JOINED; Genomic_DNA.
EMBL; X13353; CAA31695.1; JOINED; Genomic_DNA.
EMBL; AJ238246; CAB41416.1; -; mRNA.
EMBL; AF509887; AAN64031.1; -; mRNA.
EMBL; AF509892; AAN64035.1; -; Genomic_DNA.
EMBL; AF509891; AAN64035.1; JOINED; Genomic_DNA.
EMBL; AC007338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002700; AAH02700.1; -; mRNA.
CCDS; CCDS8822.1; -.
PIR; B24177; B24177.
PIR; S05602; S05602.
RefSeq; NP_005547.3; NM_005556.3.
UniGene; Hs.411501; -.
PDB; 4XIF; X-ray; 3.20 A; E/F/G/H=8-16.
PDBsum; 4XIF; -.
ProteinModelPortal; P08729; -.
SMR; P08729; -.
BioGrid; 110053; 11.
IntAct; P08729; 7.
MINT; MINT-256895; -.
STRING; 9606.ENSP00000329243; -.
DrugBank; DB04959; HspE7.
DrugBank; DB01087; Primaquine.
iPTMnet; P08729; -.
PhosphoSitePlus; P08729; -.
SwissPalm; P08729; -.
BioMuta; KRT7; -.
DMDM; 317373583; -.
SWISS-2DPAGE; P08729; -.
PaxDb; P08729; -.
PeptideAtlas; P08729; -.
PRIDE; P08729; -.
TopDownProteomics; P08729; -.
DNASU; 3855; -.
Ensembl; ENST00000331817; ENSP00000329243; ENSG00000135480.
GeneID; 3855; -.
KEGG; hsa:3855; -.
UCSC; uc001saa.2; human.
CTD; 3855; -.
DisGeNET; 3855; -.
EuPathDB; HostDB:ENSG00000135480.14; -.
GeneCards; KRT7; -.
H-InvDB; HIX0010643; -.
H-InvDB; HIX0079487; -.
HGNC; HGNC:6445; KRT7.
HPA; CAB000028; -.
HPA; HPA007272; -.
MIM; 148059; gene.
neXtProt; NX_P08729; -.
OpenTargets; ENSG00000135480; -.
PharmGKB; PA30233; -.
eggNOG; ENOG410IG4R; Eukaryota.
eggNOG; ENOG410YY6B; LUCA.
GeneTree; ENSGT00760000118796; -.
HOGENOM; HOG000230976; -.
HOVERGEN; HBG013015; -.
InParanoid; P08729; -.
KO; K07605; -.
OMA; PGIFEAQ; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; P08729; -.
TreeFam; TF317854; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
SIGNOR; P08729; -.
ChiTaRS; KRT7; human.
GeneWiki; Keratin_7; -.
GenomeRNAi; 3855; -.
PRO; PR:P08729; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135480; -.
CleanEx; HS_KRT7; -.
Genevisible; P08729; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; NAS:UniProtKB.
GO; GO:0045095; C:keratin filament; IEA:InterPro.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR032444; Keratin_2_head.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF16208; Keratin_2_head; 1.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; Host-virus interaction;
Intermediate filament; Isopeptide bond; Keratin; Methylation;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.7}.
CHAIN 2 469 Keratin, type II cytoskeletal 7.
/FTId=PRO_0000063725.
DOMAIN 91 403 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 2 90 Head.
REGION 90 126 Coil 1A.
REGION 92 97 Interaction with HPV16 E7.
{ECO:0000269|PubMed:12072504}.
REGION 127 144 Linker 1.
REGION 145 236 Coil 1B.
REGION 237 260 Linker 12.
REGION 261 399 Coil 2.
REGION 400 469 Tail.
SITE 343 343 Stutter.
MOD_RES 2 2 N-acetylserine. {ECO:0000269|Ref.7}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 20 20 Dimethylated arginine; alternate.
{ECO:0000269|Ref.7}.
MOD_RES 20 20 Omega-N-methylarginine; alternate.
{ECO:0000269|Ref.7}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 97 97 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 179 179 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 254 254 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 289 289 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 286 286 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 296 296 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 331 331 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 186 186 H -> R (in dbSNP:rs6580870).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:10492017,
ECO:0000269|PubMed:12359226,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2415537,
ECO:0000269|PubMed:2459129}.
/FTId=VAR_060731.
VARIANT 364 364 G -> A (in dbSNP:rs2608009).
{ECO:0000269|PubMed:10492017,
ECO:0000269|PubMed:12359226,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2415537,
ECO:0000269|PubMed:2459129}.
/FTId=VAR_016321.
CONFLICT 79 79 D -> G (in Ref. 3; CAB41416).
{ECO:0000305}.
CONFLICT 83 84 SL -> FS (in Ref. 3; CAB41416).
{ECO:0000305}.
CONFLICT 97 97 T -> A (in Ref. 1; CAA26956 and 2;
CAA31695). {ECO:0000305}.
CONFLICT 155 155 L -> M (in Ref. 3; CAB41416).
{ECO:0000305}.
CONFLICT 164 164 A -> Q (in Ref. 1; CAA26956, 2; CAA31695
and 3; CAB41416). {ECO:0000305}.
CONFLICT 165 165 E -> G (in Ref. 1; CAA26956, 2; CAA31695
and 3; CAB41416). {ECO:0000305}.
CONFLICT 168 168 S -> T (in Ref. 1; CAA26956, 2; CAA31695
and 3; CAB41416). {ECO:0000305}.
CONFLICT 342 342 R -> C (in Ref. 1; CAA26956 and 2;
CAA31695). {ECO:0000305}.
CONFLICT 411 411 V -> A (in Ref. 3; CAB41416).
{ECO:0000305}.
CONFLICT 467 467 A -> T (in Ref. 3; CAB41416).
{ECO:0000305}.
SEQUENCE 469 AA; 51386 MW; 070CBE8F66A62497 CRC64;
MSIHFSSPVF TSRSAAFSGR GAQVRLSSAR PGGLGSSSLY GLGASRPRVA VRSAYGGPVG
AGIREVTINQ SLLAPLRLDA DPSLQRVRQE ESEQIKTLNN KFASFIDKVR FLEQQNKLLE
TKWTLLQEQK SAKSSRLPDI FEAQIAGLRG QLEALQVDGG RLEAELRSMQ DVVEDFKNKY
EDEINHRTAA ENEFVVLKKD VDAAYMSKVE LEAKVDALND EINFLRTLNE TELTELQSQI
SDTSVVLSMD NSRSLDLDGI IAEVKAQYEE MAKCSRAEAE AWYQTKFETL QAQAGKHGDD
LRNTRNEISE MNRAIQRLQA EIDNIKNQRA KLEAAIAEAE ERGELALKDA RAKQEELEAA
LQRGKQDMAR QLREYQELMS VKLALDIEIA TYRKLLEGEE SRLAGDGVGA VNISVMNSTG
GSSSGGGIGL TLGGTMGSNA LSFSSSAGPG LLKAYSIRTA SASRRSARD


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