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Protein

Cyclin-D1-binding protein 1

Gene

CCNDBP1

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

Functioni

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.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-D1-binding protein 1
Alternative name(s):
Grap2 and cyclin-D-interacting protein
Human homolog of Maid
Gene namesi
Name:CCNDBP1
Synonyms:DIP1, GCIP, HHM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:1587. CCNDBP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26154.

Polymorphism and mutation databases

BioMutaiCCNDBP1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 360359Cyclin-D1-binding protein 1PRO_0000323372Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95273.
PaxDbiO95273.
PRIDEiO95273.

PTM databases

PhosphoSiteiO95273.

Expressioni

Tissue specificityi

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.5 Publications

Developmental stagei

Expression may increase during differentiation.1 Publication

Inductioni

Expression is induced by sodium butyrate, an inhibitor of colon cancer cell proliferation.1 Publication

Gene expression databases

BgeeiO95273.
ExpressionAtlasiO95273. baseline and differential.
GenevisibleiO95273. HS.

Organism-specific databases

HPAiCAB020664.
HPA041065.

Interactioni

Subunit structurei

Interacts with CCND1 and GRAP2. May also interact with COPS5, RPLP0, SIRT6, SYF2 and TCF3.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
B0FTY23EBI-748961,EBI-10175366
B2R4U63EBI-748961,EBI-10175477
F4ZW623EBI-748961,EBI-10177680
Q5XG853EBI-748961,EBI-10248413
Q8N9J23EBI-748961,EBI-10268244
Q96BA23EBI-748961,EBI-10282278
AMPD2Q014333EBI-748961,EBI-8796759
ARHGAP22Q7Z5H33EBI-748961,EBI-3866859
ATP4BP511643EBI-748961,EBI-3904463
C22orf23Q9BZE73EBI-748961,EBI-10303102
C6orf226Q5I0X43EBI-748961,EBI-10244057
CCDC108Q6ZU64-33EBI-748961,EBI-10255250
CCDC146Q8IYE0-23EBI-748961,EBI-10247802
CDK18Q070023EBI-748961,EBI-746238
CNNM3Q8NE013EBI-748961,EBI-741032
COPS5Q929055EBI-748961,EBI-594661
CUL5Q930343EBI-748961,EBI-1057139
DMRT3Q9NQL93EBI-748961,EBI-9679045
DOCK2Q926083EBI-748961,EBI-448771
FAM110AQ9BQ893EBI-748961,EBI-1752811
FAM64AQ9BSJ63EBI-748961,EBI-2568609
FAM74A6Q5TZK33EBI-748961,EBI-10247271
GSTK1Q9Y2Q33EBI-748961,EBI-1053767
ID2Q023634EBI-748961,EBI-713450
IMP3Q9NV315EBI-748961,EBI-747481
MAP2K2P365073EBI-748961,EBI-1056930
MOSP005403EBI-748961,EBI-1757866
MRPL15Q9P0154EBI-748961,EBI-2371967
NAIF1Q69YI73EBI-748961,EBI-10249231
NANOS2P603213EBI-748961,EBI-10216569
Neurod1Q608674EBI-748961,EBI-309315From a different organism.
PIAS2O759284EBI-748961,EBI-348555
PMP2P026893EBI-748961,EBI-10193858
PSMB10P403064EBI-748961,EBI-603329
RBP5P829803EBI-748961,EBI-3941274
RPL28P467794EBI-748961,EBI-366357
RPL39LQ96EH53EBI-748961,EBI-6658607
RPLP0P053883EBI-748961,EBI-354101
RPS28P628573EBI-748961,EBI-353027
RRADP550425EBI-748961,EBI-3911502
SPG7Q9UQ903EBI-748961,EBI-717201
SYF2O959263EBI-748961,EBI-2557644
TCF3P15923-13EBI-748961,EBI-769645
TEAD4D3DUQ63EBI-748961,EBI-10176734
THAP10Q9P2Z04EBI-748961,EBI-745404
THAP7Q9BT493EBI-748961,EBI-741350
TMEM120BA0PK003EBI-748961,EBI-10171534
TRAPPC5Q8IUR03EBI-748961,EBI-3246160
TTC23Q5W5X93EBI-748961,EBI-6447954
TYMSOSQ8TAI13EBI-748961,EBI-742060
ZBTB24O431673EBI-748961,EBI-744471
ZGPATQ8N5A54EBI-748961,EBI-3439227
ZNF124Q159733EBI-748961,EBI-2555767
ZNF136P527374EBI-748961,EBI-749129
ZNF169Q149293EBI-748961,EBI-10234472
ZNF20P170243EBI-748961,EBI-717634
ZNF230Q9UIE03EBI-748961,EBI-1105361
ZNF394Q53GI33EBI-748961,EBI-10211248
ZNF439Q8NDP43EBI-748961,EBI-747580
ZNF490Q9ULM23EBI-748961,EBI-1105370
ZNF555Q8NEP93EBI-748961,EBI-10270752
ZNF564Q8TBZ83EBI-748961,EBI-10273713
ZNF581Q9P0T43EBI-748961,EBI-745520
ZNF627Q7L9453EBI-748961,EBI-2797561
ZNF670Q9BS343EBI-748961,EBI-745276
ZNF697Q8N5083EBI-748961,EBI-10265733
ZNF707Q96C283EBI-748961,EBI-748111
ZSCAN26Q166703EBI-748961,EBI-3920053

Protein-protein interaction databases

BioGridi117117. 84 interactions.
IntActiO95273. 77 interactions.
MINTiMINT-1411177.
STRINGi9606.ENSP00000300213.

Structurei

Secondary structure

1
360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2913Combined sources
Helixi31 – 366Combined sources
Helixi49 – 7325Combined sources
Beta strandi76 – 783Combined sources
Helixi82 – 10322Combined sources
Helixi108 – 1103Combined sources
Helixi112 – 13726Combined sources
Helixi154 – 1607Combined sources
Turni161 – 1644Combined sources
Helixi169 – 19729Combined sources
Helixi235 – 26531Combined sources
Helixi271 – 29525Combined sources
Beta strandi296 – 2983Combined sources
Helixi301 – 32424Combined sources
Helixi335 – 35218Combined sources
Helixi353 – 3586Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AY5X-ray2.50A1-360[»]
ProteinModelPortaliO95273.
SMRiO95273. Positions 14-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 208207Required for interaction with CCND1Add
BLAST
Regioni2 – 190189Interaction with RPLP0Add
BLAST
Regioni2 – 184183Interaction with TCF3Add
BLAST
Regioni150 – 360211Interaction with TCF3Add
BLAST
Regioni240 – 360121Interaction with RPLP0Add
BLAST

Sequence similaritiesi

Belongs to the CCNDBP1 family.Curated

Phylogenomic databases

eggNOGiNOG19167.
GeneTreeiENSGT00390000018016.
HOVERGENiHBG107623.
InParanoidiO95273.
OMAiCMNRIKE.
OrthoDBiEOG70S75V.
PhylomeDBiO95273.
TreeFamiTF336444.

Family and domain databases

InterProiIPR026907. CCNDBP1.
[Graphical view]
PANTHERiPTHR15492. PTHR15492. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95273-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASATAPAAA VPTLASPLEQ LRHLAEELRL LLPRVRVGEA QETTEEFNRE
60 70 80 90 100
MFWRRLNEAA VTVSREATTL TIVFSQLPLP SPQETQKFCE QVHAAIKAFI
110 120 130 140 150
AVYYLLPKDQ GITLRKLVRG ATLDIVDGMA QLMEVLSVTP TQSPENNDLI
160 170 180 190 200
SYNSVWVACQ QMPQIPRDNK AAALLMLTKN VDFVKDAHEE MEQAVEECDP
210 220 230 240 250
YSGLLNDTEE NNSDNHNHED DVLGFPSNQD LYWSEDDQEL IIPCLALVRA
260 270 280 290 300
SKACLKKIRM LVAENGKKDQ VAQLDDIVDI SDEISPSVDD LALSIYPPMC
310 320 330 340 350
HLTVRINSAK LVSVLKKALE ITKASHVTPQ PEDSWIPLLI NAIDHCMNRI
360
KELTQSELEL
Length:360
Mass (Da):40,262
Last modified:March 18, 2008 - v2
Checksum:i40C7C3686632F6A7
GO
Isoform 2 (identifier: O95273-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     308-309: SA → EP
     310-360: Missing.

Note: No experimental confirmation available.
Show »
Length:309
Mass (Da):34,553
Checksum:iAD95CB0FFA840BED
GO
Isoform 3 (identifier: O95273-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: Missing.

Show »
Length:232
Mass (Da):26,038
Checksum:i358E6410BEF74DB4
GO
Isoform 4 (identifier: O95273-4) [UniParc]FASTAAdd to basket

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.
Show »
Length:204
Mass (Da):22,714
Checksum:iBA2C46B96005794A
GO

Sequence cautioni

The sequence AAD11777.1 differs from that shown. Reason: Frameshift at positions 8, 14 and 18. Curated
The sequence AAP97163.1 differs from that shown. Reason: Frameshift at positions 17 and 40. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401A → D in AAD11777 (PubMed:10854051).Curated
Sequence conflicti41 – 411Q → R in AAP97163 (Ref. 4) Curated
Sequence conflicti74 – 741F → S in BAC11433 (PubMed:16303743).Curated
Sequence conflicti211 – 2111N → S in BAC11433 (PubMed:16303743).Curated
Sequence conflicti235 – 2351E → G in BAF83396 (PubMed:14702039).Curated
Sequence conflicti267 – 2671K → R in BAC87645 (PubMed:14702039).Curated
Sequence conflicti274 – 2741L → M in AAD11777 (PubMed:10854051).Curated
Sequence conflicti274 – 2741L → M in AAF67182 (PubMed:10801854).Curated
Sequence conflicti310 – 3101K → R in BAC11530 (PubMed:14702039).Curated
Sequence conflicti334 – 3341S → I in BAF83354 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 128128Missing in isoform 3 and isoform 4. 2 PublicationsVSP_032012Add
BLAST
Alternative sequencei308 – 33326SAKLV…PQPED → VSTGFEGIATEQMGRISLIT SISCK in isoform 4. 1 PublicationVSP_032013Add
BLAST
Alternative sequencei308 – 3092SA → EP in isoform 2. 1 PublicationVSP_032014
Alternative sequencei310 – 36051Missing in isoform 2. 1 PublicationVSP_032015Add
BLAST
Alternative sequencei334 – 36027Missing in isoform 4. 1 PublicationVSP_032016Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10092.1. [O95273-1]
RefSeqiNP_036274.3. NM_012142.4. [O95273-1]
UniGeneiHs.36794.

Genome annotation databases

EnsembliENST00000300213; ENSP00000300213; ENSG00000166946.
ENST00000565296; ENSP00000455419; ENSG00000166946. [O95273-2]
ENST00000566515; ENSP00000456797; ENSG00000166946. [O95273-2]
GeneIDi23582.
KEGGihsa:23582.
UCSCiuc001zqv.3. human. [O95273-1]
uc021sjs.1. human. [O95273-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10092.1. [O95273-1]
RefSeqiNP_036274.3. NM_012142.4. [O95273-1]
UniGeneiHs.36794.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AY5X-ray2.50A1-360[»]
ProteinModelPortaliO95273.
SMRiO95273. Positions 14-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117117. 84 interactions.
IntActiO95273. 77 interactions.
MINTiMINT-1411177.
STRINGi9606.ENSP00000300213.

PTM databases

PhosphoSiteiO95273.

Polymorphism and mutation databases

BioMutaiCCNDBP1.

Proteomic databases

MaxQBiO95273.
PaxDbiO95273.
PRIDEiO95273.

Protocols and materials databases

DNASUi23582.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300213; ENSP00000300213; ENSG00000166946.
ENST00000565296; ENSP00000455419; ENSG00000166946. [O95273-2]
ENST00000566515; ENSP00000456797; ENSG00000166946. [O95273-2]
GeneIDi23582.
KEGGihsa:23582.
UCSCiuc001zqv.3. human. [O95273-1]
uc021sjs.1. human. [O95273-4]

Organism-specific databases

CTDi23582.
GeneCardsiGC15P043477.
HGNCiHGNC:1587. CCNDBP1.
HPAiCAB020664.
HPA041065.
MIMi607089. gene.
neXtProtiNX_O95273.
PharmGKBiPA26154.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG19167.
GeneTreeiENSGT00390000018016.
HOVERGENiHBG107623.
InParanoidiO95273.
OMAiCMNRIKE.
OrthoDBiEOG70S75V.
PhylomeDBiO95273.
TreeFamiTF336444.

Miscellaneous databases

ChiTaRSiCCNDBP1. human.
GeneWikiiCCNDBP1.
GenomeRNAii23582.
NextBioi46190.
PROiO95273.
SOURCEiSearch...

Gene expression databases

BgeeiO95273.
ExpressionAtlasiO95273. baseline and differential.
GenevisibleiO95273. HS.

Family and domain databases

InterProiIPR026907. CCNDBP1.
[Graphical view]
PANTHERiPTHR15492. PTHR15492. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCCDB1_HUMAN
AccessioniPrimary (citable) accession number: O95273
Secondary accession number(s): A8K3Q0
, A8K3U2, Q6ZQN9, Q7Z519, Q8NBS7, Q8NBY2, Q9NS19, Q9NYH3, Q9UHX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: July 22, 2015
This is version 94 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.