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WTIP_HUMAN
ID   WTIP_HUMAN              Reviewed;         430 AA.
AC   A6NIX2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 3.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Wilms tumor protein 1-interacting protein;
DE            Short=WT1-interacting protein;
GN   Name=WTIP;
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 GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH LATS1; LATS2 AND SAV1.
RX   PubMed=20303269; DOI=10.1016/j.cub.2010.02.035;
RA   Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B.,
RA   Longmore G.D.;
RT   "Ajuba LIM proteins are negative regulators of the Hippo signaling
RT   pathway.";
RL   Curr. Biol. 20:657-662(2010).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20086015; DOI=10.1074/jbc.m109.061671;
RA   Kim J.H., Konieczkowski M., Mukherjee A., Schechtman S., Khan S.,
RA   Schelling J.R., Ross M.D., Bruggeman L.A., Sedor J.R.;
RT   "Podocyte injury induces nuclear translocation of WTIP via microtubule-
RT   dependent transport.";
RL   J. Biol. Chem. 285:9995-10004(2010).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EIF4E; AGO1; AGO2;
RP   DCP2 AND DDX6.
RX   PubMed=20616046; DOI=10.1073/pnas.0914987107;
RA   James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M.,
RA   Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J.,
RA   Longmore G.D., Bushell M., Sharp T.V.;
RT   "LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-
RT   mediated gene silencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010).
RN   [5]
RP   FUNCTION.
RX   PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA   Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA   Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT   "Identification and characterization of a set of conserved and new
RT   regulators of cytoskeletal organisation, cell morphology and migration.";
RL   BMC Biol. 9:54-54(2011).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH EGLN2/PHD1; EGLN3/PHD3 AND VHL.
RX   PubMed=22286099; DOI=10.1038/ncb2424;
RA   Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C., Feng Y.,
RA   Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J., Ingvarsson S.,
RA   Ratcliffe P.J., Longmore G.D., Sharp T.V.;
RT   "The LIMD1 protein bridges an association between the prolyl hydroxylases
RT   and VHL to repress HIF-1 activity.";
RL   Nat. Cell Biol. 14:201-208(2012).
CC   -!- FUNCTION: Adapter or scaffold protein which participates in the
CC       assembly of numerous protein complexes and is involved in several
CC       cellular processes such as cell fate determination, cytoskeletal
CC       organization, repression of gene transcription, cell-cell adhesion,
CC       cell differentiation, proliferation and migration. Positively regulates
CC       microRNA (miRNA)-mediated gene silencing. Negatively regulates Hippo
CC       signaling pathway and antagonizes phosphorylation of YAP1. Acts as a
CC       transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent
CC       repression of E-cadherin transcription. Acts as a hypoxic regulator by
CC       bridging an association between the prolyl hydroxylases and VHL
CC       enabling efficient degradation of HIF1A. In podocytes, may play a role
CC       in the regulation of actin dynamics and/or foot process
CC       cytoarchitecture (By similarity). In the course of podocyte injury,
CC       shuttles into the nucleus and acts as a transcription regulator that
CC       represses WT1-dependent transcription regulation, thereby translating
CC       changes in slit diaphragm structure into altered gene expression and a
CC       less differentiated phenotype. Involved in the organization of the
CC       basal body (By similarity). Involved in cilia growth and positioning
CC       (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:A9LS46,
CC       ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046,
CC       ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22286099}.
CC   -!- SUBUNIT: Forms homodimers (By similarity). Interacts with CD2AP and
CC       WT1. Interacts (via LIM domains) with SNAI1 (via SNAG domain),
CC       SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain) (By
CC       similarity). Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1,
CC       LATS2, SAV1, EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM domains)
CC       with isoform 1 and isoform 3 of VHL. Interacts with ROR2 (By
CC       similarity). Following treatment with bacterial lipopolysaccharide
CC       (LPS), forms a complex with MAPK8IP3 and dynein intermediate chain (By
CC       similarity). Interacts with PRICKLE3 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:A9LS46}.
CC   -!- INTERACTION:
CC       A6NIX2; Q9H9G7: AGO3; NbExp=3; IntAct=EBI-20730502, EBI-2267883;
CC       A6NIX2; Q14160: SCRIB; NbExp=2; IntAct=EBI-20730502, EBI-357345;
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Nucleus
CC       {ECO:0000250}. Cytoplasm, P-body. Note=Following podocyte injury,
CC       caused by treatment with LPS, puromycin aminonucleoside, ultraviolet or
CC       hydrogen peroxide, translocates from sites of cell-cell contacts into
CC       the cytosol and nucleus. The shift from cell contacts to intracellular
CC       plaques starts as early as 1 hour after LPS stimulation and
CC       intranuclear localization begins 3 hours after LPS treatment. Maximal
CC       nuclear localization is achieved 6 hours after LPS treatment. Nuclear
CC       translocation requires dynein motor activity and intact microtubule
CC       network (By similarity). Returns to cell-cell contacts 24 hours after
CC       LPS stimulation. In the presence of ROR2, localizes to the plasma
CC       membrane (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR   EMBL; AC008747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS59375.1; -.
DR   RefSeq; NP_001073905.1; NM_001080436.1.
DR   AlphaFoldDB; A6NIX2; -.
DR   BioGRID; 125985; 13.
DR   IntAct; A6NIX2; 8.
DR   STRING; 9606.ENSP00000466953; -.
DR   iPTMnet; A6NIX2; -.
DR   PhosphoSitePlus; A6NIX2; -.
DR   BioMuta; WTIP; -.
DR   EPD; A6NIX2; -.
DR   jPOST; A6NIX2; -.
DR   MassIVE; A6NIX2; -.
DR   MaxQB; A6NIX2; -.
DR   PaxDb; A6NIX2; -.
DR   PeptideAtlas; A6NIX2; -.
DR   PRIDE; A6NIX2; -.
DR   ProteomicsDB; 1294; -.
DR   Antibodypedia; 56892; 67 antibodies from 13 providers.
DR   DNASU; 126374; -.
DR   Ensembl; ENST00000590071.7; ENSP00000466953.2; ENSG00000142279.13.
DR   GeneID; 126374; -.
DR   KEGG; hsa:126374; -.
DR   MANE-Select; ENST00000590071.7; ENSP00000466953.2; NM_001080436.2; NP_001073905.1.
DR   UCSC; uc002nvm.4; human.
DR   CTD; 126374; -.
DR   DisGeNET; 126374; -.
DR   GeneCards; WTIP; -.
DR   HGNC; HGNC:20964; WTIP.
DR   HPA; ENSG00000142279; Low tissue specificity.
DR   MIM; 614790; gene.
DR   neXtProt; NX_A6NIX2; -.
DR   OpenTargets; ENSG00000142279; -.
DR   VEuPathDB; HostDB:ENSG00000142279; -.
DR   eggNOG; KOG1701; Eukaryota.
DR   GeneTree; ENSGT00940000160924; -.
DR   HOGENOM; CLU_001357_11_3_1; -.
DR   InParanoid; A6NIX2; -.
DR   OMA; QENEWHR; -.
DR   OrthoDB; 326249at2759; -.
DR   TreeFam; TF320310; -.
DR   PathwayCommons; A6NIX2; -.
DR   Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   SignaLink; A6NIX2; -.
DR   BioGRID-ORCS; 126374; 15 hits in 1075 CRISPR screens.
DR   ChiTaRS; WTIP; human.
DR   GenomeRNAi; 126374; -.
DR   Pharos; A6NIX2; Tbio.
DR   PRO; PR:A6NIX2; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; A6NIX2; protein.
DR   Bgee; ENSG00000142279; Expressed in popliteal artery and 139 other tissues.
DR   ExpressionAtlas; A6NIX2; baseline and differential.
DR   Genevisible; A6NIX2; HS.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; IDA:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0035195; P:miRNA-mediated gene silencing; IMP:MGI.
DR   GO; GO:0035331; P:negative regulation of hippo signaling; IDA:UniProtKB.
DR   GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IMP:UniProtKB.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF00412; LIM; 3.
DR   SMART; SM00132; LIM; 3.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE   1: Evidence at protein level;
KW   Cell junction; Cilium biogenesis/degradation; Cytoplasm; LIM domain;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW   RNA-mediated gene silencing; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..430
FT                   /note="Wilms tumor protein 1-interacting protein"
FT                   /id="PRO_0000328860"
FT   DOMAIN          223..284
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          288..348
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          349..417
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          22..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..190
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   430 AA;  45124 MW;  B95E162B3009B886 CRC64;
     MQRSRAGADE AALLLAGLAL RELEPGCGSP GRGRRGPRPG PGDEAAPALG RRGKGSGGPE
     AGADGLSRGE RGPRRAAVPE LSAQPAGSPR ASLAGSDGGG GGGSARSSGI SLGYDQRHGS
     PRSGRSDPRP GPGPPSVGSA RSSVSSLGSR GSAGAYADFL PPGACPAPAR SPEPAGPAPF
     PLPALPLPPG REGGPSAAER RLEALTRELE RALEARTARD YFGICIKCGL GIYGAQQACQ
     AMGSLYHTDC FTCDSCGRRL RGKAFYNVGE KVYCQEDFLY SGFQQTADKC SVCGHLIMEM
     ILQALGKSYH PGCFRCSVCN ECLDGVPFTV DVENNIYCVR DYHTVFAPKC ASCARPILPA
     QGCETTIRVV SMDRDYHVAC YHCEDCGLQL SGEEGRRCYP LAGHLLCRRC HLRRLQPGPL
     PSPTVHVTEL
 
 
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