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Protein

E3 ubiquitin-protein ligase CCNB1IP1

Gene

CCNB1IP1

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

Functioni

Ubiquitin E3 ligase that acts as a limiting factor for crossing-over during meiosis: required during zygonema to limit the colocalization of RNF212 with MutS-gamma-associated recombination sites and thereby establish early differentiation of crossover and non-crossover sites. Later, it is directed by MutL-gamma to stably accumulate at designated crossover sites. Probably promotes the dissociation of RNF212 and MutS-gamma to allow the progression of recombination and the implementation of the final steps of crossing over (By similarity). Modulates cyclin-B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis.By similarity
E3 ubiquitin-protein ligase. Modulates cyclin B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis.

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri4 – 5148RING-type; atypicalAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. blastocyst formation Source: Ensembl
  2. chiasma assembly Source: UniProtKB
  3. protein ubiquitination Source: UniProtKB-UniPathway
  4. reciprocal meiotic recombination Source: UniProtKB
  5. spermatid development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Meiosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase CCNB1IP1 (EC:6.3.2.-)
Alternative name(s):
Cyclin-B1-interacting protein 1
Human enhancer of invasion 10
Gene namesi
Name:CCNB1IP1
Synonyms:C14orf18, HEI10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:19437. CCNB1IP1.

Subcellular locationi

  1. Nucleus
  2. Chromosome

  3. Note: Associates to the synaptonemal complex.

GO - Cellular componenti

  1. synaptonemal complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi28 – 281C → A: Abrogates induction of filamentous growth in yeast; when associated with A-30 and A-33. 1 Publication
Mutagenesisi30 – 301H → A: Abrogates induction of filamentous growth in yeast; when associated with A-28 and A-33. 1 Publication
Mutagenesisi33 – 331C → A: Abrogates induction of filamentous growth in yeast; when associated with A-28 and A-30. 1 Publication

Organism-specific databases

PharmGKBiPA134863884.

Polymorphism and mutation databases

BioMutaiCCNB1IP1.
DMDMi37078756.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277E3 ubiquitin-protein ligase CCNB1IP1PRO_0000055874Add
BLAST

Post-translational modificationi

Ubiquitinated; autoubiquitinated.1 Publication
Phosphorylated by CDK1 on serine or threonine residues (in vitro).1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9NPC3.
PRIDEiQ9NPC3.

PTM databases

PhosphoSiteiQ9NPC3.

Expressioni

Tissue specificityi

Highly expressed in heart. Detected at intermediate levels in liver and kidney, and at low levels in placenta, brain and lung.1 Publication

Gene expression databases

BgeeiQ9NPC3.
CleanExiHS_CCNB1IP1.
ExpressionAtlasiQ9NPC3. baseline and differential.
GenevestigatoriQ9NPC3.

Interactioni

Subunit structurei

Interacts with CCNB1, UBE2L3 and NF2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P629722EBI-745269,EBI-412964From a different organism.
CCNB1P146352EBI-745269,EBI-495332
EPM2AIP1Q7L7753EBI-745269,EBI-6255981
KEAP1Q141453EBI-745269,EBI-751001
KRT15P190123EBI-745269,EBI-739566
PRKAA2P546463EBI-745269,EBI-1383852

Protein-protein interaction databases

BioGridi121779. 12 interactions.
IntActiQ9NPC3. 8 interactions.
MINTiMINT-1450464.
STRINGi9606.ENSP00000337396.

Structurei

3D structure databases

ProteinModelPortaliQ9NPC3.
SMRiQ9NPC3. Positions 3-58.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili127 – 18256Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri4 – 5148RING-type; atypicalAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG27432.
GeneTreeiENSGT00390000002849.
HOGENOMiHOG000111677.
HOVERGENiHBG050962.
InParanoidiQ9NPC3.
KOiK10639.
OMAiIANHEGT.
OrthoDBiEOG76MK99.
PhylomeDBiQ9NPC3.
TreeFamiTF328863.

Family and domain databases

InterProiIPR001841. Znf_RING.
[Graphical view]
PfamiPF14634. zf-RING_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NPC3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLCEDMLLC NYRKCRIKLS GYAWVTACSH IFCDQHGSGE FSRSPAICPA
60 70 80 90 100
CNSTLSGKLD IVRTELSPSE EYKAMVLAGL RPEIVLDISS RALAFWTYQV
110 120 130 140 150
HQERLYQEYN FSKAEGHLKQ MEKIYTQQIQ SKDVELTSMK GEVTSMKKVL
160 170 180 190 200
EEYKKKFSDI SEKLMERNRQ YQKLQGLYDS LRLRNITIAN HEGTLEPSMI
210 220 230 240 250
AQSGVLGFPL GNNSKFPLDN TPVRNRGDGD GDFQFRPFFA GSPTAPEPSN
260 270
SFFSFVSPSR ELEQQQVSSR AFKVKRI
Length:277
Mass (Da):31,544
Last modified:October 1, 2000 - v1
Checksum:i885723B01A35225A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216381 mRNA. Translation: AAF36386.1.
AL161994 mRNA. Translation: CAB82326.1.
AK026233 mRNA. Translation: BAB15403.1.
BX161423 mRNA. Translation: CAD61896.1.
BX161424 mRNA. Translation: CAD61897.1.
BX247978 mRNA. Translation: CAD62312.1.
BC000369 mRNA. Translation: AAH00369.1.
BC001218 mRNA. Translation: AAH01218.1.
BC004435 mRNA. Translation: AAH04435.1.
CCDSiCCDS9547.1.
PIRiT47153.
RefSeqiNP_067001.3. NM_021178.4.
NP_878269.1. NM_182849.2.
NP_878272.1. NM_182852.3.
UniGeneiHs.107003.
Hs.741214.

Genome annotation databases

EnsembliENST00000353689; ENSP00000337396; ENSG00000100814.
ENST00000358932; ENSP00000351810; ENSG00000100814.
ENST00000398160; ENSP00000381226; ENSG00000100814.
ENST00000398163; ENSP00000381229; ENSG00000100814.
ENST00000398169; ENSP00000381235; ENSG00000100814.
ENST00000437553; ENSP00000409896; ENSG00000100814.
GeneIDi57820.
KEGGihsa:57820.
UCSCiuc001vwv.4. human.

Polymorphism and mutation databases

BioMutaiCCNB1IP1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216381 mRNA. Translation: AAF36386.1.
AL161994 mRNA. Translation: CAB82326.1.
AK026233 mRNA. Translation: BAB15403.1.
BX161423 mRNA. Translation: CAD61896.1.
BX161424 mRNA. Translation: CAD61897.1.
BX247978 mRNA. Translation: CAD62312.1.
BC000369 mRNA. Translation: AAH00369.1.
BC001218 mRNA. Translation: AAH01218.1.
BC004435 mRNA. Translation: AAH04435.1.
CCDSiCCDS9547.1.
PIRiT47153.
RefSeqiNP_067001.3. NM_021178.4.
NP_878269.1. NM_182849.2.
NP_878272.1. NM_182852.3.
UniGeneiHs.107003.
Hs.741214.

3D structure databases

ProteinModelPortaliQ9NPC3.
SMRiQ9NPC3. Positions 3-58.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121779. 12 interactions.
IntActiQ9NPC3. 8 interactions.
MINTiMINT-1450464.
STRINGi9606.ENSP00000337396.

PTM databases

PhosphoSiteiQ9NPC3.

Polymorphism and mutation databases

BioMutaiCCNB1IP1.
DMDMi37078756.

Proteomic databases

PaxDbiQ9NPC3.
PRIDEiQ9NPC3.

Protocols and materials databases

DNASUi57820.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353689; ENSP00000337396; ENSG00000100814.
ENST00000358932; ENSP00000351810; ENSG00000100814.
ENST00000398160; ENSP00000381226; ENSG00000100814.
ENST00000398163; ENSP00000381229; ENSG00000100814.
ENST00000398169; ENSP00000381235; ENSG00000100814.
ENST00000437553; ENSP00000409896; ENSG00000100814.
GeneIDi57820.
KEGGihsa:57820.
UCSCiuc001vwv.4. human.

Organism-specific databases

CTDi57820.
GeneCardsiGC14M020779.
HGNCiHGNC:19437. CCNB1IP1.
MIMi608249. gene.
neXtProtiNX_Q9NPC3.
PharmGKBiPA134863884.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG27432.
GeneTreeiENSGT00390000002849.
HOGENOMiHOG000111677.
HOVERGENiHBG050962.
InParanoidiQ9NPC3.
KOiK10639.
OMAiIANHEGT.
OrthoDBiEOG76MK99.
PhylomeDBiQ9NPC3.
TreeFamiTF328863.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiCCNB1IP1. human.
GeneWikiiCCNB1IP1.
GenomeRNAii57820.
NextBioi64776.
PROiQ9NPC3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NPC3.
CleanExiHS_CCNB1IP1.
ExpressionAtlasiQ9NPC3. baseline and differential.
GenevestigatoriQ9NPC3.

Family and domain databases

InterProiIPR001841. Znf_RING.
[Graphical view]
PfamiPF14634. zf-RING_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels."
    Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.
    Mol. Cell. Biol. 23:2109-2122(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-28; HIS-30 AND CYS-33, FUNCTION, INTERACTION WITH UBE2L3 AND CCNB1, UBIQUITINATION, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "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: Small intestine.
  4. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain and Placenta.
  5. "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: Lung and Muscle.
  6. "A functional association between merlin and HEI10, a cell cycle regulator."
    Gronholm M., Muranen T., Toby G.G., Utermark T., Hanemann C.O., Golemis E.A., Carpen O.
    Oncogene 25:4389-4398(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NF2.
  7. "HEI10 negatively regulates cell invasion by inhibiting cyclin B/Cdk1 and other promotility proteins."
    Singh M.K., Nicolas E., Gherraby W., Dadke D., Lessin S., Golemis E.A.
    Oncogene 26:4825-4832(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCIP1_HUMAN
AccessioniPrimary (citable) accession number: Q9NPC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: October 1, 2000
Last modified: April 29, 2015
This is version 124 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.