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CNIPF_HUMAN
ID   CNIPF_HUMAN             Reviewed;         899 AA.
AC   G9CGD6; G9CGD3; G9CGD4;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=CNK3/IPCEF1 fusion protein {ECO:0000303|PubMed:22085542};
GN   Name=CNK3/IPCEF1;
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] (ISOFORMS CNK3-IPCEF1-1; CNK3-IPCEF1-2 AND
RP   CNK3-IPCEF1-3), AND FUNCTION.
RX   PubMed=22085542; DOI=10.1016/j.yexcr.2011.10.018;
RA   Attar M.A., Salem J.C., Pursel H.S., Santy L.C.;
RT   "CNK3 and IPCEF1 produce a single protein that is required for HGF
RT   dependent Arf6 activation and migration.";
RL   Exp. Cell Res. 318:228-237(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-873, 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).
CC   -!- FUNCTION: Required for hepatocyte growth factor (HGF)-dependent
CC       activation of Arf6 and HGF-stimulated cell migration.
CC       {ECO:0000269|PubMed:22085542}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=CNK3-IPCEF1-1; Synonyms=CNK3/IPCEF1 Long-1;
CC         IsoId=G9CGD6-1; Sequence=Displayed;
CC       Name=CNK3-IPCEF1-2; Synonyms=CNK3/IPCEF1 Long-2;
CC         IsoId=G9CGD6-2; Sequence=VSP_059280;
CC       Name=CNK3-IPCEF1-3; Synonyms=CNK3/IPCEF1 Short;
CC         IsoId=G9CGD6-3; Sequence=VSP_059281;
CC       Name=CNK3;
CC         IsoId=Q6P9H4-1; Sequence=External;
CC       Name=IPCEF1-1;
CC         IsoId=Q8WWN9-1; Sequence=External;
CC       Name=IPCEF1-2;
CC         IsoId=Q8WWN9-2; Sequence=External;
CC   -!- MISCELLANEOUS: [Isoform CNK3-IPCEF1-1]: Based on a naturally occurring
CC       readthrough transcript which produces an CNK3/IPCEF1 fusion protein.
CC       {ECO:0000269|PubMed:22085542}.
CC   -!- MISCELLANEOUS: [Isoform CNK3-IPCEF1-2]: Based on a naturally occurring
CC       readthrough transcript which produces an CNK3/IPCEF1 fusion protein.
CC       {ECO:0000269|PubMed:22085542}.
CC   -!- MISCELLANEOUS: [Isoform CNK3-IPCEF1-3]: Based on a naturally occurring
CC       readthrough transcript which produces an CNK3/IPCEF1 fusion protein.
CC       Major isoform found in CaCo2-cells. {ECO:0000269|PubMed:22085542}.
CC   -!- SIMILARITY: Belongs to the CNKSR family. {ECO:0000305}.
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DR   EMBL; JF308526; AEA29623.1; -; mRNA.
DR   EMBL; JF308523; AEA29620.1; -; mRNA.
DR   EMBL; JF308524; AEA29621.1; -; mRNA.
DR   EMBL; AL033376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL132774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL357075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF510943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G9CGD6; -.
DR   SMR; G9CGD6; -.
DR   IntAct; G9CGD6; 2.
DR   iPTMnet; G9CGD6; -.
DR   PhosphoSitePlus; G9CGD6; -.
DR   jPOST; G9CGD6; -.
DR   MassIVE; G9CGD6; -.
DR   PeptideAtlas; G9CGD6; -.
DR   PRIDE; G9CGD6; -.
DR   UCSC; uc021zhc.2; human. [G9CGD6-1]
DR   HPA; ENSG00000288520; Low tissue specificity.
DR   neXtProt; NX_G9CGD6; -.
DR   VEuPathDB; HostDB:ENSG00000288520; -.
DR   GeneTree; ENSGT00940000154428; -.
DR   HOGENOM; CLU_013414_0_0_1; -.
DR   OMA; ACHPKVM; -.
DR   Pharos; G9CGD6; Tbio.
DR   Proteomes; UP000005640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:2001114; P:positive regulation of cellular response to hepatocyte growth factor stimulus; IMP:UniProtKB.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR010599; CNK2/3_dom.
DR   InterPro; IPR017874; CRIC_domain.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   Pfam; PF10534; CRIC_ras_sig; 1.
DR   Pfam; PF06663; DUF1170; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS51290; CRIC; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Reference proteome.
FT   CHAIN           1..899
FT                   /note="CNK3/IPCEF1 fusion protein"
FT                   /id="PRO_0000442776"
FT   DOMAIN          7..72
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          80..174
FT                   /note="CRIC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00621"
FT   DOMAIN          211..293
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          332..457
FT                   /note="DUF1170"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          503..602
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          309..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          851..899
FT                   /note="Required for interaction with CYTH2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWN9"
FT   REGION          868..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..749
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         873
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         474
FT                   /note="L -> LQ (in isoform CNK3-IPCEF1-2)"
FT                   /id="VSP_059280"
FT   VAR_SEQ         475..543
FT                   /note="Missing (in isoform CNK3-IPCEF1-3)"
FT                   /id="VSP_059281"
FT   CONFLICT        647
FT                   /note="S -> L (in Ref. 1; AEA29621)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   899 AA;  100365 MW;  AE0CF42C290EADD5 CRC64;
     MEPVTKWSPK QVVDWTRGLD DCLQQYVHKF EREKINGEQL LQISHQDLEE LGVTRIGHQE
     LVLEAVDLLC ALNYGLETDN MKNLVLKLRA SSHNLQNYIS SRRKSPAYDG NTSRKAPNEF
     LTSVVELIGA AKALLAWLDR APFTGITDFS VTKNKIIQLC LDLTTTVQKD CFVAEMEDKV
     LTVVKVLNGI CDKTIRSTTD PVMSQCACLE EVHLPNIKPG EGLGMYIKST YDGLHVITGT
     TENSPADRSQ KIHAGDEVIQ VNQQTVVGWQ LKNLVKKLRE NPTGVVLLLK KRPTGSFNFT
     PAPLKNLRWK PPLVQTSPPP ATTQSPESTM DTSLKKEKSA ILDLYIPPPP AVPYSPRDEN
     GSFVYGGSSK CKQPLPGPKG SESPNSFLDQ ESRRRRFTIA DSDQLPGYSV ETNILPTKMR
     EKTPSYGKPR PLSMPADGNW MGIVDPFARP RGHGRKAFVS TKMTSYMAID GSALVPLRQK
     PRRKTQGFLT MSRRRISCKD LGHADCQGWL YKKKEKGSFL SNKWKKFWVI LKGSSLYWYS
     NQMAEKADGF VNLPDFTVER ASECKKKHAF KISHPQIKTF YFAAENVQEM NVWLNKLGSA
     VIHQESTTKD EECYSESEQE DPEIAAETPP PPHASQTQSL TAQQASSSSP SLSGTSYSFS
     SLENTVKTPS SFPSSLSKER QSLPDTVNSL SAAEDEGQPI TFAVQVHSPV PSEAGIHKAL
     ENSFVTSESG FLNSLSSDDT SSLSSNHDHL TVPDKPAGSK IMDKEETKVS EDDEMEKLYK
     SLEQASLSPL GDRRPSTKKE LRKSFVKRCK NPSINEKLHK IRTLNSTLKC KEHDLAMINQ
     LLDDPKLTAR KYREWKVMNT LLIQDIYQQQ RASPAPDDTD DTPQELKKSP SSPSVENSI
 
 
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