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CARF_RAT
ID   CARF_RAT                Reviewed;         570 AA.
AC   Q5U2X0; Q4KM89;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=CDKN2A-interacting protein;
DE   AltName: Full=Collaborator of ARF;
GN   Name=Cdkn2aip; Synonyms=Carf;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Testis, and Thymus;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC   -!- FUNCTION: Regulates DNA damage response and cell proliferation in a
CC       dose-dependent manner through a number of signaling pathways involved
CC       in cell proliferation, apoptosis and senescence.
CC       {ECO:0000250|UniProtKB:Q9NXV6}.
CC   -!- SUBUNIT: Interacts with CDKN2A/p14ARF, p53/TP53 and MDM2. Interacts
CC       with CHEK2 and MAPK3. Interacts with XRN2.
CC       {ECO:0000250|UniProtKB:Q9NXV6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q9NXV6}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5U2X0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5U2X0-2; Sequence=VSP_032223, VSP_032224;
CC   -!- PTM: May be ubiquitinated. {ECO:0000250|UniProtKB:Q9NXV6}.
CC   -!- SIMILARITY: Belongs to the CARF family. {ECO:0000305}.
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DR   EMBL; BC085832; AAH85832.1; -; mRNA.
DR   EMBL; BC098694; AAH98694.1; -; mRNA.
DR   RefSeq; NP_001014022.1; NM_001014000.1. [Q5U2X0-1]
DR   RefSeq; XP_006253209.1; XM_006253147.3. [Q5U2X0-2]
DR   AlphaFoldDB; Q5U2X0; -.
DR   SMR; Q5U2X0; -.
DR   STRING; 10116.ENSRNOP00000029705; -.
DR   iPTMnet; Q5U2X0; -.
DR   PhosphoSitePlus; Q5U2X0; -.
DR   jPOST; Q5U2X0; -.
DR   PaxDb; Q5U2X0; -.
DR   PeptideAtlas; Q5U2X0; -.
DR   PRIDE; Q5U2X0; -.
DR   Ensembl; ENSRNOT00000030519; ENSRNOP00000029705; ENSRNOG00000022736. [Q5U2X0-1]
DR   GeneID; 306455; -.
DR   KEGG; rno:306455; -.
DR   CTD; 55602; -.
DR   RGD; 1305302; Cdkn2aip.
DR   eggNOG; ENOG502S4FT; Eukaryota.
DR   GeneTree; ENSGT00940000158376; -.
DR   HOGENOM; CLU_019689_0_0_1; -.
DR   InParanoid; Q5U2X0; -.
DR   OMA; CRYPPQV; -.
DR   OrthoDB; 1524198at2759; -.
DR   PhylomeDB; Q5U2X0; -.
DR   TreeFam; TF333807; -.
DR   PRO; PR:Q5U2X0; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000022736; Expressed in testis and 19 other tissues.
DR   GO; GO:0001652; C:granular component; ISO:RGD.
DR   GO; GO:0005730; C:nucleolus; ISO:RGD.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0002039; F:p53 binding; ISO:RGD.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0009967; P:positive regulation of signal transduction; ISO:RGD.
DR   GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR021859; XTBD.
DR   Pfam; PF11952; XTBD; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS51827; XTBD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV6"
FT   CHAIN           2..570
FT                   /note="CDKN2A-interacting protein"
FT                   /id="PRO_0000324341"
FT   DOMAIN          19..126
FT                   /note="XRN2-binding (XTBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01171"
FT   DOMAIN          452..527
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   REGION          122..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV6"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV6"
FT   MOD_RES         234
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BI72"
FT   MOD_RES         378
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV6"
FT   CROSSLNK        176
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV6"
FT   VAR_SEQ         118..119
FT                   /note="VK -> KG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032223"
FT   VAR_SEQ         120..570
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032224"
SQ   SEQUENCE   570 AA;  60744 MW;  E31CB97382220015 CRC64;
     MAQEVSEYLS QNPRVAAWVE TLRCEGETDK HWRHRREFLL RNAGDLVPAT EETADAESGA
     RSRQLQQLVS FSMAWANHVF LGCRYPQKVM DKILSMAEGI KVTDAPIHTT RDELVAKVKK
     RGISSSNEGV EEPSKKRSIE GKNNSSVERD HGKKSAKTDR SAQQENSSGS KGSSTKSESS
     GTSARSNSGV SHQNSSTSEG DRSVCSQSSS NSSQVTSAGS GKASEPEAPD KHGSASFVSS
     LLKSSLNSHV TKSTDSRQHS GSPRKNALEG SSVSVSQSSS EIEVPLLGSS GSSEVELPLL
     SCKSSSETAS SGLTTKASSE ANISSSVSKN SSSSGTSLLM PKSSSTNTSL LTSQVAASLL
     ASKSSSQSSG SVASKSTSLG SMSQLASKSS SQSSTSQLPS KSTSQSSESS VKFTCRKLTN
     EDIKQKQPFF NRLYKTVAWK LVAVGGFSPN VNHGELLNAA IEALKATLDV FFVPLKELAD
     LPQNKSSQES IVCELRCKSV YLGTGCGKSK ENAKAVASRE ALKLFLKKKV VVKICKRKYR
     GNEIEDLVLL DEESRPVNLP PALKHPQELL
 
 
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