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O95273 (CCDB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-D1-binding protein 1
Alternative name(s):
Grap2 and cyclin-D-interacting protein
Human homolog of Maid
Gene names
Name:CCNDBP1
Synonyms:DIP1, GCIP, HHM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May negatively regulate cell cycle progression. May act at least in part via inhibition of the cyclin-D1/CDK4 complex, thereby preventing phosphorylation of RB1 and blocking E2F-dependent transcription. Ref.3

Subunit structure

Interacts with CCND1 and GRAP2. May also interact with COPS5, RPLP0, SIRT6, SYF2 and TCF3. Ref.1 Ref.2 Ref.3 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Cytoplasm. Nucleus Ref.1 Ref.13 Ref.14.

Tissue specificity

Ubiquitously expressed. Expression is down-regulated in a variety of tumor types including breast, colon, prostate and rectal tumors, and is up-regulated in certain hepatic carcinomas. Ref.1 Ref.2 Ref.3 Ref.12 Ref.13

Developmental stage

Expression may increase during differentiation. Ref.1

Induction

Expression is induced by sodium butyrate, an inhibitor of colon cancer cell proliferation. Ref.13

Post-translational modification

Phosphorylated. Ref.1

Sequence similarities

Belongs to the CCNDBP1 family.

Sequence caution

The sequence AAD11777.1 differs from that shown. Reason: Frameshift at positions 8, 14 and 18.

The sequence AAP97163.1 differs from that shown. Reason: Frameshift at positions 17 and 40.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of cell cycle

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95273-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O95273-2)

The sequence of this isoform differs from the canonical sequence as follows:
     308-309: SA → EP
     310-360: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O95273-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: Missing.
Isoform 4 (identifier: O95273-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: Missing.
     308-333: SAKLVSVLKKALEITKASHVTPQPED → VSTGFEGIATEQMGRISLITSISCK
     334-360: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 360359Cyclin-D1-binding protein 1
PRO_0000323372

Regions

Region2 – 208207Required for interaction with CCND1
Region2 – 190189Interaction with RPLP0
Region2 – 184183Interaction with TCF3
Region150 – 360211Interaction with TCF3
Region240 – 360121Interaction with RPLP0

Amino acid modifications

Modified residue21N-acetylalanine Ref.15

Natural variations

Alternative sequence1 – 128128Missing in isoform 3 and isoform 4.
VSP_032012
Alternative sequence308 – 33326SAKLV…PQPED → VSTGFEGIATEQMGRISLIT SISCK in isoform 4.
VSP_032013
Alternative sequence308 – 3092SA → EP in isoform 2.
VSP_032014
Alternative sequence310 – 36051Missing in isoform 2.
VSP_032015
Alternative sequence334 – 36027Missing in isoform 4.
VSP_032016

Experimental info

Sequence conflict401A → D in AAD11777. Ref.1
Sequence conflict411Q → R in AAP97163. Ref.4
Sequence conflict741F → S in BAC11433. Ref.8
Sequence conflict2111N → S in BAC11433. Ref.8
Sequence conflict2351E → G in BAF83396. Ref.7
Sequence conflict2671K → R in BAC87645. Ref.7
Sequence conflict2741L → M in AAD11777. Ref.1
Sequence conflict2741L → M in AAF67182. Ref.3
Sequence conflict3101K → R in BAC11530. Ref.7
Sequence conflict3341S → I in BAF83354. Ref.7

Secondary structure

.............................. 360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 40C7C3686632F6A7

FASTA36040,262
        10         20         30         40         50         60 
MASATAPAAA VPTLASPLEQ LRHLAEELRL LLPRVRVGEA QETTEEFNRE MFWRRLNEAA 

        70         80         90        100        110        120 
VTVSREATTL TIVFSQLPLP SPQETQKFCE QVHAAIKAFI AVYYLLPKDQ GITLRKLVRG 

       130        140        150        160        170        180 
ATLDIVDGMA QLMEVLSVTP TQSPENNDLI SYNSVWVACQ QMPQIPRDNK AAALLMLTKN 

       190        200        210        220        230        240 
VDFVKDAHEE MEQAVEECDP YSGLLNDTEE NNSDNHNHED DVLGFPSNQD LYWSEDDQEL 

       250        260        270        280        290        300 
IIPCLALVRA SKACLKKIRM LVAENGKKDQ VAQLDDIVDI SDEISPSVDD LALSIYPPMC 

       310        320        330        340        350        360 
HLTVRINSAK LVSVLKKALE ITKASHVTPQ PEDSWIPLLI NAIDHCMNRI KELTQSELEL 

« Hide

Isoform 2 [UniParc].

Checksum: AD95CB0FFA840BED
Show »

FASTA30934,553
Isoform 3 [UniParc].

Checksum: 358E6410BEF74DB4
Show »

FASTA23226,038
Isoform 4 [UniParc].

Checksum: BA2C46B96005794A
Show »

FASTA20422,714

References

« Hide 'large scale' references
[1]"Cloning and characterization of DIP1, a novel protein that is related to the Id family of proteins."
Yao Y., Doki Y., Jiang W., Imoto M., Venkatraj V.S., Warburton D., Santella R.M., Lu B., Yan L., Sun X.-H., Su T., Luo J., Weinstein I.B.
Exp. Cell Res. 257:22-32(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CCND1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
[2]"Human homologue of maid: a dominant inhibitory helix-loop-helix protein associated with liver-specific gene expression."
Terai S., Aoki H., Thorgeirsson S.S.
Hepatology 32:357-366(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TCF3, TISSUE SPECIFICITY.
Tissue: Liver.
[3]"GCIP, a novel human grap2 and cyclin D interacting protein, regulates E2F-mediated transcriptional activity."
Xia C., Bao Z., Tabassam F., Ma W., Qiu M., Hua S., Liu M.
J. Biol. Chem. 275:20942-20948(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CCND1 AND GRAP2, TISSUE SPECIFICITY.
Tissue: Liver.
[4]"Cloning and characterization of a novel human cDNA homologous to murine Maid mRNA."
Gao J., Yu L., Mao N.H., Wan Y.Z., Yang Y.M., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Hypothalamus.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"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. expand/collapse author list , 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] (ISOFORMS 1; 3 AND 4).
Tissue: Hair follicle dermal papilla, Lung, Retinoblastoma and Trachea.
[8]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Placenta.
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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] (ISOFORM 1).
Tissue: Pancreas.
[11]"p29, a novel GCIP-interacting protein, localizes in the nucleus."
Chang M.-S., Chang C.-L., Huang C.-J., Yang Y.-C.
Biochem. Biophys. Res. Commun. 279:732-737(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYF2.
[12]"Human homologue of maid is a useful marker protein in hepatocarcinogenesis."
Takami T., Terai S., Yokoyama Y., Tanimoto H., Tajima K., Uchida K., Yamasaki T., Sakaida I., Nishina H., Thorgeirsson S.S., Okita K.
Gastroenterology 128:1369-1380(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH COPS5.
[13]"GCIP/CCNDBP1, a helix-loop-helix protein, suppresses tumorigenesis."
Ma W., Stafford L.J., Li D., Luo J., Li X., Ning G., Liu M.
J. Cell. Biochem. 100:1376-1386(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIRT6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[14]"Ribosomal phosphoprotein P0 interacts with GCIP and overexpression of P0 is associated with cellular proliferation in breast and liver carcinoma cells."
Chang T.-W., Chen C.-C., Chen K.-Y., Su J.-H., Chang J.-H., Chang M.-C.
Oncogene 27:332-338(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPLP0, SUBCELLULAR LOCATION.
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF082569 mRNA. Translation: AAD11777.1. Frameshift.
AF132034 mRNA. Translation: AAF77613.1.
AF246144 mRNA. Translation: AAF67182.1.
AF087852 mRNA. Translation: AAP97163.1. Frameshift.
AF113535 mRNA. Translation: AAF14872.1.
CR450331 mRNA. Translation: CAG29327.1.
AK075296 mRNA. Translation: BAC11530.1.
AK128849 mRNA. Translation: BAC87645.1.
AK290665 mRNA. Translation: BAF83354.1.
AK290707 mRNA. Translation: BAF83396.1.
AK075146 mRNA. Translation: BAC11433.1.
CH471125 Genomic DNA. Translation: EAW92588.1.
CH471125 Genomic DNA. Translation: EAW92590.1.
BC009689 mRNA. Translation: AAH09689.1.
RefSeqNP_036274.3. NM_012142.4.
UniGeneHs.36794.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AY5X-ray2.50A1-360[»]
ProteinModelPortalO95273.
SMRO95273. Positions 14-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117117. 10 interactions.
IntActO95273. 21 interactions.
MINTMINT-1411177.

PTM databases

PhosphoSiteO95273.

Proteomic databases

PaxDbO95273.
PRIDEO95273.

Protocols and materials databases

DNASU23582.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300213; ENSP00000300213; ENSG00000166946. [O95273-1]
ENST00000565296; ENSP00000455419; ENSG00000166946. [O95273-2]
ENST00000566515; ENSP00000456797; ENSG00000166946. [O95273-2]
GeneID23582.
KEGGhsa:23582.
UCSCuc001zqv.3. human. [O95273-1]
uc021sjs.1. human. [O95273-4]

Organism-specific databases

CTD23582.
GeneCardsGC15P043477.
HGNCHGNC:1587. CCNDBP1.
HPACAB020664.
HPA041065.
MIM607089. gene.
neXtProtNX_O95273.
PharmGKBPA26154.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG19167.
HOVERGENHBG107623.
InParanoidO95273.
OMACMNRIKE.
OrthoDBEOG70S75V.
PhylomeDBO95273.
TreeFamTF336444.

Gene expression databases

ArrayExpressO95273.
BgeeO95273.
GenevestigatorO95273.

Family and domain databases

InterProIPR026907. CCNDBP1.
[Graphical view]
PANTHERPTHR32435. PTHR32435. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCCNDBP1. human.
GeneWikiCCNDBP1.
GenomeRNAi23582.
NextBio46190.
PROO95273.
SOURCESearch...

Entry information

Entry nameCCDB1_HUMAN
AccessionPrimary (citable) accession number: O95273
Secondary accession number(s): A8K3Q0 expand/collapse secondary AC list , A8K3U2, Q6ZQN9, Q7Z519, Q8NBS7, Q8NBY2, Q9NS19, Q9NYH3, Q9UHX9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: April 16, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM