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ZNRD2_HUMAN
ID   ZNRD2_HUMAN             Reviewed;         199 AA.
AC   O60232;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Protein ZNRD2 {ECO:0000305};
DE   AltName: Full=Autoantigen p27 {ECO:0000303|PubMed:9486406};
DE   AltName: Full=Sjoegren syndrome/scleroderma autoantigen 1;
DE   AltName: Full=Zinc ribbon domain-containing protein 2 {ECO:0000305};
GN   Name=ZNRD2 {ECO:0000312|HGNC:HGNC:11328};
GN   Synonyms=SSSCA1 {ECO:0000312|HGNC:HGNC:11328};
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], AND FUNCTION.
RX   PubMed=9486406; DOI=10.1046/j.1365-2249.1998.00517.x;
RA   Muro Y., Yamada T., Himeno M., Sugimoto K.;
RT   "cDNA cloning of a novel autoantigen targeted by a minor subset of anti-
RT   centromere antibodies.";
RL   Clin. Exp. Immunol. 111:372-376(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [4]
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=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [5]
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   [6]
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).
CC   -!- FUNCTION: Might play a role in mitosis. Antigenic molecule. Could be a
CC       centromere-associated protein. May induce anti-centromere antibodies.
CC       {ECO:0000305|PubMed:9486406}.
CC   -!- INTERACTION:
CC       O60232; P35609: ACTN2; NbExp=3; IntAct=EBI-741415, EBI-77797;
CC       O60232; P51946: CCNH; NbExp=4; IntAct=EBI-741415, EBI-741406;
CC       O60232; P78371: CCT2; NbExp=6; IntAct=EBI-741415, EBI-357407;
CC       O60232; P49368: CCT3; NbExp=6; IntAct=EBI-741415, EBI-356673;
CC       O60232; P48643: CCT5; NbExp=4; IntAct=EBI-741415, EBI-355710;
CC       O60232; Q99832: CCT7; NbExp=7; IntAct=EBI-741415, EBI-357046;
CC       O60232; V9HW96: HEL-S-100n; NbExp=3; IntAct=EBI-741415, EBI-10330207;
CC       O60232; V9HW37: HEL-S-69; NbExp=3; IntAct=EBI-741415, EBI-10186233;
CC       O60232; Q0VD86: INCA1; NbExp=3; IntAct=EBI-741415, EBI-6509505;
CC       O60232; O75928-2: PIAS2; NbExp=3; IntAct=EBI-741415, EBI-348567;
CC       O60232; P78317: RNF4; NbExp=3; IntAct=EBI-741415, EBI-2340927;
CC       O60232; O75971: SNAPC5; NbExp=3; IntAct=EBI-741415, EBI-749483;
CC       O60232; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-741415, EBI-10175576;
CC       O60232; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-741415, EBI-765817;
CC       O60232; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-741415, EBI-10180829;
CC       O60232; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-741415, EBI-17634549;
CC       O60232; Q9Q2G4: ORF; Xeno; NbExp=4; IntAct=EBI-741415, EBI-6248094;
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DR   EMBL; AB001740; BAA25263.1; -; mRNA.
DR   EMBL; BC014791; AAH14791.1; -; mRNA.
DR   CCDS; CCDS8104.1; -.
DR   RefSeq; NP_006387.1; NM_006396.2.
DR   PDB; 6HCZ; X-ray; 2.30 A; A/B=1-199.
DR   PDBsum; 6HCZ; -.
DR   AlphaFoldDB; O60232; -.
DR   SMR; O60232; -.
DR   BioGRID; 115788; 299.
DR   IntAct; O60232; 110.
DR   STRING; 9606.ENSP00000312318; -.
DR   ChEMBL; CHEMBL4105996; -.
DR   GlyGen; O60232; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O60232; -.
DR   PhosphoSitePlus; O60232; -.
DR   BioMuta; SSSCA1; -.
DR   EPD; O60232; -.
DR   jPOST; O60232; -.
DR   MassIVE; O60232; -.
DR   MaxQB; O60232; -.
DR   PaxDb; O60232; -.
DR   PeptideAtlas; O60232; -.
DR   PRIDE; O60232; -.
DR   ProteomicsDB; 49259; -.
DR   Antibodypedia; 29847; 181 antibodies from 25 providers.
DR   DNASU; 10534; -.
DR   Ensembl; ENST00000309328.8; ENSP00000312318.3; ENSG00000173465.8.
DR   GeneID; 10534; -.
DR   KEGG; hsa:10534; -.
DR   MANE-Select; ENST00000309328.8; ENSP00000312318.3; NM_006396.3; NP_006387.1.
DR   UCSC; uc001oek.4; human.
DR   CTD; 10534; -.
DR   DisGeNET; 10534; -.
DR   GeneCards; ZNRD2; -.
DR   HGNC; HGNC:11328; ZNRD2.
DR   HPA; ENSG00000173465; Low tissue specificity.
DR   MIM; 606044; gene.
DR   neXtProt; NX_O60232; -.
DR   OpenTargets; ENSG00000173465; -.
DR   PharmGKB; PA36152; -.
DR   VEuPathDB; HostDB:ENSG00000173465; -.
DR   eggNOG; KOG4537; Eukaryota.
DR   GeneTree; ENSGT00390000013169; -.
DR   HOGENOM; CLU_058702_0_0_1; -.
DR   InParanoid; O60232; -.
DR   OMA; VACQELN; -.
DR   OrthoDB; 1602560at2759; -.
DR   PhylomeDB; O60232; -.
DR   TreeFam; TF320182; -.
DR   PathwayCommons; O60232; -.
DR   SignaLink; O60232; -.
DR   BioGRID-ORCS; 10534; 57 hits in 1080 CRISPR screens.
DR   ChiTaRS; SSSCA1; human.
DR   GenomeRNAi; 10534; -.
DR   Pharos; O60232; Tdark.
DR   PRO; PR:O60232; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; O60232; protein.
DR   Bgee; ENSG00000173465; Expressed in body of pancreas and 113 other tissues.
DR   ExpressionAtlas; O60232; baseline and differential.
DR   Genevisible; O60232; HS.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
DR   InterPro; IPR009563; SSSCA1.
DR   Pfam; PF06677; Auto_anti-p27; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell cycle; Cell division; Mitosis;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..199
FT                   /note="Protein ZNRD2"
FT                   /id="PRO_0000072201"
FT   REGION          100..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   VARIANT         21
FT                   /note="T -> M (in dbSNP:rs35971725)"
FT                   /id="VAR_051383"
FT   HELIX           18..43
FT                   /evidence="ECO:0007829|PDB:6HCZ"
FT   STRAND          47..52
FT                   /evidence="ECO:0007829|PDB:6HCZ"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:6HCZ"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:6HCZ"
FT   TURN            71..75
FT                   /evidence="ECO:0007829|PDB:6HCZ"
SQ   SEQUENCE   199 AA;  21474 MW;  EF08439FDFFA1DAB CRC64;
     MALNGAEVDD FSWEPPTEAE TKVLQARRER QDRISRLMGD YLLRGYRMLG ETCADCGTIL
     LQDKQRKIYC VACQELDSDV DKDNPALNAQ AALSQAREHQ LASASELPLG SRPAPQPPVP
     RPEHCEGAAA GLKAAQGPPA PAVPPNTDVM ACTQTALLQK LTWASAELGS STSLETSIQL
     CGLIRACAEA LRSLQQLQH
 
 
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