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CARF_MOUSE
ID   CARF_MOUSE              Reviewed;         563 AA.
AC   Q8BI72;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=CDKN2A-interacting protein;
DE   AltName: Full=Collaborator of ARF;
GN   Name=Cdkn2aip; Synonyms=Carf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=12581788; DOI=10.1016/s0531-5565(02)00180-8;
RA   Wadhwa R., Sugihara T., Hasan M.K., Duncan E.L., Taira K., Kaul S.C.;
RT   "A novel putative collaborator of p19ARF.";
RL   Exp. Gerontol. 38:245-252(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-234, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- PTM: May be ubiquitinated. {ECO:0000250|UniProtKB:Q9NXV6}.
CC   -!- SIMILARITY: Belongs to the CARF family. {ECO:0000305}.
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DR   EMBL; AK048437; BAC33336.1; -; mRNA.
DR   CCDS; CCDS22299.1; -.
DR   RefSeq; NP_765995.1; NM_172407.3.
DR   AlphaFoldDB; Q8BI72; -.
DR   SMR; Q8BI72; -.
DR   BioGRID; 214348; 23.
DR   IntAct; Q8BI72; 17.
DR   STRING; 10090.ENSMUSP00000043713; -.
DR   iPTMnet; Q8BI72; -.
DR   PhosphoSitePlus; Q8BI72; -.
DR   EPD; Q8BI72; -.
DR   jPOST; Q8BI72; -.
DR   MaxQB; Q8BI72; -.
DR   PaxDb; Q8BI72; -.
DR   PeptideAtlas; Q8BI72; -.
DR   PRIDE; Q8BI72; -.
DR   ProteomicsDB; 265435; -.
DR   Antibodypedia; 17295; 227 antibodies from 32 providers.
DR   DNASU; 70925; -.
DR   Ensembl; ENSMUST00000212175; ENSMUSP00000148441; ENSMUSG00000038069.
DR   GeneID; 70925; -.
DR   KEGG; mmu:70925; -.
DR   UCSC; uc009lrh.2; mouse.
DR   CTD; 55602; -.
DR   MGI; MGI:1918175; Cdkn2aip.
DR   VEuPathDB; HostDB:ENSMUSG00000038069; -.
DR   eggNOG; ENOG502S4FT; Eukaryota.
DR   GeneTree; ENSGT00940000158376; -.
DR   HOGENOM; CLU_019689_0_0_1; -.
DR   InParanoid; Q8BI72; -.
DR   OMA; CRYPPQV; -.
DR   OrthoDB; 1524198at2759; -.
DR   PhylomeDB; Q8BI72; -.
DR   TreeFam; TF333807; -.
DR   BioGRID-ORCS; 70925; 6 hits in 73 CRISPR screens.
DR   ChiTaRS; Cdkn2aip; mouse.
DR   PRO; PR:Q8BI72; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8BI72; protein.
DR   Bgee; ENSMUSG00000038069; Expressed in spermatid and 215 other tissues.
DR   ExpressionAtlas; Q8BI72; baseline and differential.
DR   Genevisible; Q8BI72; MM.
DR   GO; GO:0001652; C:granular component; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
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:MGI.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0009967; P:positive regulation of signal transduction; ISO:MGI.
DR   GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
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; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV6"
FT   CHAIN           2..563
FT                   /note="CDKN2A-interacting protein"
FT                   /id="PRO_0000324340"
FT   DOMAIN          19..126
FT                   /note="XRN2-binding (XTBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01171"
FT   DOMAIN          445..520
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   REGION          122..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..351
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..286
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:0007744|PubMed:21183079"
FT   MOD_RES         234
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         340
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV6"
FT   MOD_RES         371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV6"
FT   CROSSLNK        177
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV6"
SQ   SEQUENCE   563 AA;  59745 MW;  277B979F01EB43C1 CRC64;
     MAQEVSEYLS QNPRVAAWVE TLRCEGETDK HWRHRREFLL RNAGDLVPAT DETADAESGA
     RTRQLQQLVS FSMAWANHVF LGCRYPQKVM DKILSMAEGI KVTDAPIHTT RDELVAKVKK
     RGISSSNEGV EEPSKKRAVE GKNNSSVERD HGKKSAKTDR SAAQQENSSP SRGSSTKSES
     GGTSARSSSS GSHQDSATSE GDRSVCSQSS SNSSQVTAGS GKALESEAPH KRGSASFVSS
     LLKSSMNSHM TQSTDNRQQS GSPKKGALEG SSGSASQSSS EIEVPLLGSS GSAEVELPLL
     SCKSSSETAS SGLTSKSSSE ANISSSVSKN SSSSGSSLLT PQSSSTNPSL LTSKSTAQVA
     ASLLATKSGA SLGSVSQLAA KSGSQSSTSQ LPSKSTSQAS ESSVKFACRK LTNEDIKQKQ
     PFFNRLYKTV AWKLVAVGGF SPTVNHGELL NAAIEALKAT LDVFFVPLKE LADLPQNKSS
     QESIVCELRC KSVYLGTGCG KSKENAKAVA SREALKLFLK KKVVVKICKR KYRGSEIEDL
     VLLDEEARPV NLPPALKHPQ ELL
 
 
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