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E3 ubiquitin-protein ligase CCNB1IP1 (EC 2.3.2.27) (Cyclin-B1-interacting protein 1) (Human enhancer of invasion 10) (RING-type E3 ubiquitin transferase CCNB1IP1)

 CIP1_HUMAN              Reviewed;         277 AA.
Q9NPC3;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
18-JUL-2018, entry version 153.
RecName: Full=E3 ubiquitin-protein ligase CCNB1IP1;
EC=2.3.2.27 {ECO:0000269|PubMed:12612082};
AltName: Full=Cyclin-B1-interacting protein 1;
AltName: Full=Human enhancer of invasion 10;
AltName: Full=RING-type E3 ubiquitin transferase CCNB1IP1 {ECO:0000305};
Name=CCNB1IP1; Synonyms=C14orf18, HEI10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-28; HIS-30 AND CYS-33,
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3 AND CCNB1,
UBIQUITINATION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=12612082; DOI=10.1128/MCB.23.6.2109-2122.2003;
Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.;
"A novel RING finger protein, human enhancer of invasion 10, alters
mitotic progression through regulation of cyclin B levels.";
Mol. Cell. Biol. 23:2109-2122(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal brain, and Placenta;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH NF2.
PubMed=16532029; DOI=10.1038/sj.onc.1209475;
Gronholm M., Muranen T., Toby G.G., Utermark T., Hanemann C.O.,
Golemis E.A., Carpen O.;
"A functional association between merlin and HEI10, a cell cycle
regulator.";
Oncogene 25:4389-4398(2006).
[7]
FUNCTION.
PubMed=17297447; DOI=10.1038/sj.onc.1210282;
Singh M.K., Nicolas E., Gherraby W., Dadke D., Lessin S.,
Golemis E.A.;
"HEI10 negatively regulates cell invasion by inhibiting cyclin B/Cdk1
and other promotility proteins.";
Oncogene 26:4825-4832(2007).
-!- FUNCTION: 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. {ECO:0000250, ECO:0000269|PubMed:12612082,
ECO:0000269|PubMed:17297447}.
-!- FUNCTION: 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.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:12612082}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with CCNB1, UBE2L3 and NF2.
{ECO:0000269|PubMed:12612082, ECO:0000269|PubMed:16532029}.
-!- INTERACTION:
P62972:- (xeno); NbExp=2; IntAct=EBI-745269, EBI-412964;
P14635:CCNB1; NbExp=2; IntAct=EBI-745269, EBI-495332;
Q7L775:EPM2AIP1; NbExp=3; IntAct=EBI-745269, EBI-6255981;
Q14145:KEAP1; NbExp=3; IntAct=EBI-745269, EBI-751001;
P19012:KRT15; NbExp=3; IntAct=EBI-745269, EBI-739566;
P25375:PRD1 (xeno); NbExp=3; IntAct=EBI-745269, EBI-13932;
P54646:PRKAA2; NbExp=3; IntAct=EBI-745269, EBI-1383852;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates to the
synaptonemal complex.
-!- TISSUE SPECIFICITY: Highly expressed in heart. Detected at
intermediate levels in liver and kidney, and at low levels in
placenta, brain and lung. {ECO:0000269|PubMed:12612082}.
-!- PTM: Ubiquitinated; autoubiquitinated.
{ECO:0000269|PubMed:12612082}.
-!- PTM: Phosphorylated by CDK1 on serine or threonine residues (in
vitro). {ECO:0000269|PubMed:12612082}.
-----------------------------------------------------------------------
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EMBL; AF216381; AAF36386.1; -; mRNA.
EMBL; AL161994; CAB82326.1; -; mRNA.
EMBL; AK026233; BAB15403.1; -; mRNA.
EMBL; BX161423; CAD61896.1; -; mRNA.
EMBL; BX161424; CAD61897.1; -; mRNA.
EMBL; BX247978; CAD62312.1; -; mRNA.
EMBL; BC000369; AAH00369.1; -; mRNA.
EMBL; BC001218; AAH01218.1; -; mRNA.
EMBL; BC004435; AAH04435.1; -; mRNA.
CCDS; CCDS9547.1; -.
PIR; T47153; T47153.
RefSeq; NP_067001.3; NM_021178.4.
RefSeq; NP_878269.1; NM_182849.2.
RefSeq; NP_878272.1; NM_182852.3.
UniGene; Hs.107003; -.
UniGene; Hs.741214; -.
ProteinModelPortal; Q9NPC3; -.
SMR; Q9NPC3; -.
BioGrid; 121779; 13.
IntAct; Q9NPC3; 12.
STRING; 9606.ENSP00000337396; -.
iPTMnet; Q9NPC3; -.
PhosphoSitePlus; Q9NPC3; -.
BioMuta; CCNB1IP1; -.
DMDM; 37078756; -.
PaxDb; Q9NPC3; -.
PeptideAtlas; Q9NPC3; -.
PRIDE; Q9NPC3; -.
ProteomicsDB; 81965; -.
DNASU; 57820; -.
Ensembl; ENST00000353689; ENSP00000337396; ENSG00000100814.
Ensembl; ENST00000358932; ENSP00000351810; ENSG00000100814.
Ensembl; ENST00000398160; ENSP00000381226; ENSG00000100814.
Ensembl; ENST00000398163; ENSP00000381229; ENSG00000100814.
Ensembl; ENST00000398169; ENSP00000381235; ENSG00000100814.
Ensembl; ENST00000437553; ENSP00000409896; ENSG00000100814.
GeneID; 57820; -.
KEGG; hsa:57820; -.
UCSC; uc001vwv.5; human.
CTD; 57820; -.
EuPathDB; HostDB:ENSG00000100814.17; -.
GeneCards; CCNB1IP1; -.
HGNC; HGNC:19437; CCNB1IP1.
MIM; 608249; gene.
neXtProt; NX_Q9NPC3; -.
OpenTargets; ENSG00000100814; -.
PharmGKB; PA134863884; -.
eggNOG; ENOG410IE9K; Eukaryota.
eggNOG; ENOG410XTEP; LUCA.
GeneTree; ENSGT00390000002849; -.
HOGENOM; HOG000111677; -.
HOVERGEN; HBG050962; -.
InParanoid; Q9NPC3; -.
KO; K10639; -.
OMA; IANHEGT; -.
OrthoDB; EOG091G0RN7; -.
PhylomeDB; Q9NPC3; -.
TreeFam; TF328863; -.
UniPathway; UPA00143; -.
ChiTaRS; CCNB1IP1; human.
GeneWiki; CCNB1IP1; -.
GenomeRNAi; 57820; -.
PRO; PR:Q9NPC3; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100814; -.
CleanEx; HS_CCNB1IP1; -.
ExpressionAtlas; Q9NPC3; baseline and differential.
Genevisible; Q9NPC3; HS.
GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
GO; GO:0051026; P:chiasma assembly; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
GO; GO:0007131; P:reciprocal meiotic recombination; ISS:UniProtKB.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
InterPro; IPR001841; Znf_RING.
Pfam; PF14634; zf-RING_5; 1.
1: Evidence at protein level;
Chromosome; Coiled coil; Complete proteome; Meiosis; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 277 E3 ubiquitin-protein ligase CCNB1IP1.
/FTId=PRO_0000055874.
ZN_FING 4 51 RING-type; atypical.
COILED 127 182 {ECO:0000255}.
MUTAGEN 28 28 C->A: Abrogates induction of filamentous
growth in yeast; when associated with A-
30 and A-33.
{ECO:0000269|PubMed:12612082}.
MUTAGEN 30 30 H->A: Abrogates induction of filamentous
growth in yeast; when associated with A-
28 and A-33.
{ECO:0000269|PubMed:12612082}.
MUTAGEN 33 33 C->A: Abrogates induction of filamentous
growth in yeast; when associated with A-
28 and A-30.
{ECO:0000269|PubMed:12612082}.
SEQUENCE 277 AA; 31544 MW; 885723B01A35225A CRC64;
MSLCEDMLLC NYRKCRIKLS GYAWVTACSH IFCDQHGSGE FSRSPAICPA CNSTLSGKLD
IVRTELSPSE EYKAMVLAGL RPEIVLDISS RALAFWTYQV HQERLYQEYN FSKAEGHLKQ
MEKIYTQQIQ SKDVELTSMK GEVTSMKKVL EEYKKKFSDI SEKLMERNRQ YQKLQGLYDS
LRLRNITIAN HEGTLEPSMI AQSGVLGFPL GNNSKFPLDN TPVRNRGDGD GDFQFRPFFA
GSPTAPEPSN SFFSFVSPSR ELEQQQVSSR AFKVKRI


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