Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

CDKN2A-interacting protein

Gene

CDKN2AIP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates DNA damage response in a dose-dependent manner through a number of signaling pathways involved in cell proliferation, apoptosis and senescence.2 Publications

GO - Molecular functioni

  • p53 binding Source: BHF-UCL
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • negative regulation of cell growth Source: BHF-UCL
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of signal transduction Source: BHF-UCL
  • regulation of protein stability Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
CDKN2A-interacting protein
Alternative name(s):
Collaborator of ARF
Gene namesi
Name:CDKN2AIP
Synonyms:CARF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:24325. CDKN2AIP.

Subcellular locationi

GO - Cellular componenti

  • granular component Source: BHF-UCL
  • nucleolus Source: BHF-UCL
  • nucleoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162382149.

Polymorphism and mutation databases

BioMutaiCDKN2AIP.
DMDMi327478591.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 580579CDKN2A-interacting proteinPRO_0000324339Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei131 – 1311PhosphoserineCombined sources
Modified residuei241 – 2411PhosphoserineBy similarity
Modified residuei346 – 3461PhosphothreonineCombined sources

Post-translational modificationi

May be ubiquitinated.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9NXV6.
MaxQBiQ9NXV6.
PaxDbiQ9NXV6.
PeptideAtlasiQ9NXV6.
PRIDEiQ9NXV6.

PTM databases

iPTMnetiQ9NXV6.
PhosphoSiteiQ9NXV6.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Inductioni

Up-regulated during replicative senescence, in response to DNA-damaging drugs, telomere unprotection and oncogenic Ras-induced stress. Induced by proteasomal inhibitor MG132. Up-regulated at G1 and G2 stages of cell cycle.1 Publication

Gene expression databases

BgeeiQ9NXV6.
CleanExiHS_CDKN2AIP.
ExpressionAtlasiQ9NXV6. baseline and differential.
GenevisibleiQ9NXV6. HS.

Organism-specific databases

HPAiHPA041397.

Interactioni

Subunit structurei

Interacts with CDKN2A/p14ARF, p53/TP53 and MDM2. Interacts with CHEK2 and MAPK3.5 Publications

GO - Molecular functioni

  • p53 binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi120743. 52 interactions.
DIPiDIP-24170N.
IntActiQ9NXV6. 28 interactions.
MINTiMINT-5010033.
STRINGi9606.ENSP00000427108.

Structurei

3D structure databases

ProteinModelPortaliQ9NXV6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini462 – 53776DRBMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi175 – 425251Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the CARF family.Curated
Contains 1 DRBM (double-stranded RNA-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IE8W. Eukaryota.
ENOG4111PSZ. LUCA.
GeneTreeiENSGT00530000063234.
HOGENOMiHOG000049179.
HOVERGENiHBG101830.
InParanoidiQ9NXV6.
OMAiRCEGETD.
OrthoDBiEOG7HQNBG.
PhylomeDBiQ9NXV6.
TreeFamiTF333807.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
InterProiIPR014720. dsRBD_dom.
IPR021859. XTBD.
[Graphical view]
PfamiPF11952. XTBD. 1 hit.
[Graphical view]
PROSITEiPS50137. DS_RBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NXV6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQEVSEYLS QNPRVAAWVE ALRCDGETDK HWRHRRDFLL RNAGDLAPAG
60 70 80 90 100
GAASASTDEA ADAESGTRNR QLQQLISFSM AWANHVFLGC RYPQKVMDKI
110 120 130 140 150
LSMAEGIKVT DAPTYTTRDE LVAKVKKRGI SSSNEGVEEP SKKRVIEGKN
160 170 180 190 200
SSAVEQDHAK TSAKTERASA QQENSSTCIG SAIKSESGNS ARSSGISSQN
210 220 230 240 250
SSTSDGDRSV SSQSSSSVSS QVTTAGSGKA SEAEAPDKHG SASFVSLLKS
260 270 280 290 300
SVNSHMTQST DSRQQSGSPK KSALEGSSAS ASQSSSEIEV PLLGSSGSSE
310 320 330 340 350
VELPLLSSKP SSETASSGLT SKTSSEASVS SSVAKNSSSS GTSLLTPKSS
360 370 380 390 400
SSTNTSLLTS KSTSQVAASL LASKSSSQTS GSLVSKSTSL ASVSQLASKS
410 420 430 440 450
SSQTSTSQLP SKSTSQSSES SVKFSCKLTN EDVKQKQPFF NRLYKTVAWK
460 470 480 490 500
LVAVGGFSPN VNHGELLNAA IEALKATLDV FFVPLKELAD LPQNKSSQES
510 520 530 540 550
IVCELRCKSV YLGTGCGKSK ENAKAVASRE ALKLFLKKKV VVKICKRKYR
560 570 580
GSEIEDLVLL DEESRPVNLP PALKHPQELL
Length:580
Mass (Da):61,125
Last modified:April 5, 2011 - v3
Checksum:i5CFCB5DFEE50A475
GO

Sequence cautioni

The sequence AAF68967.1 differs from that shown. Reason: Frameshift at position 4. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421Missing in EAX04691 (Ref. 3) Curated
Sequence conflicti242 – 2421Missing in AAH22270 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF246705 mRNA. Translation: AAF68967.1. Frameshift.
AK000043 mRNA. Translation: BAA90902.1.
CH471056 Genomic DNA. Translation: EAX04691.1.
BC022270 mRNA. Translation: AAH22270.1.
CCDSiCCDS34110.1.
RefSeqiNP_001304272.1. NM_001317343.1.
NP_060102.1. NM_017632.3.
UniGeneiHs.592508.
Hs.644077.

Genome annotation databases

EnsembliENST00000504169; ENSP00000427108; ENSG00000168564.
GeneIDi55602.
KEGGihsa:55602.
UCSCiuc003ivp.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF246705 mRNA. Translation: AAF68967.1. Frameshift.
AK000043 mRNA. Translation: BAA90902.1.
CH471056 Genomic DNA. Translation: EAX04691.1.
BC022270 mRNA. Translation: AAH22270.1.
CCDSiCCDS34110.1.
RefSeqiNP_001304272.1. NM_001317343.1.
NP_060102.1. NM_017632.3.
UniGeneiHs.592508.
Hs.644077.

3D structure databases

ProteinModelPortaliQ9NXV6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120743. 52 interactions.
DIPiDIP-24170N.
IntActiQ9NXV6. 28 interactions.
MINTiMINT-5010033.
STRINGi9606.ENSP00000427108.

PTM databases

iPTMnetiQ9NXV6.
PhosphoSiteiQ9NXV6.

Polymorphism and mutation databases

BioMutaiCDKN2AIP.
DMDMi327478591.

Proteomic databases

EPDiQ9NXV6.
MaxQBiQ9NXV6.
PaxDbiQ9NXV6.
PeptideAtlasiQ9NXV6.
PRIDEiQ9NXV6.

Protocols and materials databases

DNASUi55602.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000504169; ENSP00000427108; ENSG00000168564.
GeneIDi55602.
KEGGihsa:55602.
UCSCiuc003ivp.2. human.

Organism-specific databases

CTDi55602.
GeneCardsiCDKN2AIP.
H-InvDBHIX0004662.
HGNCiHGNC:24325. CDKN2AIP.
HPAiHPA041397.
MIMi615914. gene.
neXtProtiNX_Q9NXV6.
PharmGKBiPA162382149.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE8W. Eukaryota.
ENOG4111PSZ. LUCA.
GeneTreeiENSGT00530000063234.
HOGENOMiHOG000049179.
HOVERGENiHBG101830.
InParanoidiQ9NXV6.
OMAiRCEGETD.
OrthoDBiEOG7HQNBG.
PhylomeDBiQ9NXV6.
TreeFamiTF333807.

Miscellaneous databases

GenomeRNAii55602.
NextBioi60145.
PROiQ9NXV6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NXV6.
CleanExiHS_CDKN2AIP.
ExpressionAtlasiQ9NXV6. baseline and differential.
GenevisibleiQ9NXV6. HS.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
InterProiIPR014720. dsRBD_dom.
IPR021859. XTBD.
[Graphical view]
PfamiPF11952. XTBD. 1 hit.
[Graphical view]
PROSITEiPS50137. DS_RBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CARF is a novel protein that cooperates with mouse p19ARF (human p14ARF) in activating p53."
    Hasan M.K., Yaguchi T., Sugihara T., Kumar P.K.R., Taira K., Reddel R.R., Kaul S.C., Wadhwa R.
    J. Biol. Chem. 277:37765-37770(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CDKN2A, SUBCELLULAR LOCATION.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  5. Bienvenut W.V., Dozynkiewicz M., Norman J.C.
    Submitted (JUN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14; 42-68; 129-142 AND 209-229, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  6. Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH CDKN2A.
  7. "Alternative reading frame protein (ARF)-independent function of CARF (collaborator of ARF) involves its interactions with p53: evidence for a novel p53-activation pathway and its negative feedback control."
    Hasan M.K., Yaguchi T., Minoda Y., Hirano T., Taira K., Wadhwa R., Kaul S.C.
    Biochem. J. 380:605-610(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TP53, FUNCTION.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "CARF binds to three members (ARF, p53, and HDM2) of the p53 tumor-suppressor pathway."
    Kamrul H.M., Wadhwa R., Kaul S.C.
    Ann. N. Y. Acad. Sci. 1100:312-315(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MDM2.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Molecular characterization of collaborator of ARF (CARF) as a DNA damage response and cell cycle checkpoint regulatory protein."
    Singh R., Kalra R.S., Hasan K., Kaul Z., Cheung C.T., Huschtscha L., Reddel R.R., Kaul S.C., Wadhwa R.
    Exp. Cell Res. 322:324-334(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  15. "Collaborator of ARF (CARF) regulates proliferative fate of human cells by dose-dependent regulation of DNA damage signaling."
    Cheung C.T., Singh R., Kalra R.S., Kaul S.C., Wadhwa R.
    J. Biol. Chem. 289:18258-18269(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHEK2 AND MAPK3.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCARF_HUMAN
AccessioniPrimary (citable) accession number: Q9NXV6
Secondary accession number(s): Q8TBM5, Q9NYH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: April 5, 2011
Last modified: May 11, 2016
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.