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CBLL2_HUMAN
ID   CBLL2_HUMAN             Reviewed;         425 AA.
AC   Q8N7E2; A0AV29; A0AV31; E3SBK4; Q6DJY9;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=E3 ubiquitin-protein ligase CBLL2 {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000269|PubMed:20657603};
DE   AltName: Full=Cbl proto-oncogene-like protein 2;
DE   AltName: Full=RING-type E3 ubiquitin transferase ZNF645;
DE   AltName: Full=Zinc finger protein 645;
DE   AltName: Full=c-Cbl-like protein 2;
GN   Name=CBLL2 {ECO:0000312|HGNC:HGNC:26371}; Synonyms=ZNF645;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   VARIANT GLU-166, AND CATALYTIC ACTIVITY.
RC   TISSUE=Testis;
RX   PubMed=20657603; DOI=10.1038/aja.2010.54;
RA   Liu Y.Q., Bai G., Zhang H., Su D., Tao D.C., Yang Y., Ma Y.X., Zhang S.Z.;
RT   "Human RING finger protein ZNF645 is a novel testis-specific E3 ubiquitin
RT   ligase.";
RL   Asian J. Androl. 12:658-666(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-166.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND DOMAIN HYB.
RX   PubMed=22252131; DOI=10.1038/emboj.2011.496;
RA   Mukherjee M., Chow S.Y., Yusoff P., Seetharaman J., Ng C., Sinniah S.,
RA   Koh X.W., Asgar N.F., Li D., Yim D., Jackson R.A., Yew J., Qian J., Iyu A.,
RA   Lim Y.P., Zhou X., Sze S.K., Guy G.R., Sivaraman J.;
RT   "Structure of a novel phosphotyrosine-binding domain in Hakai that targets
RT   E-cadherin.";
RL   EMBO J. 31:1308-1319(2012).
CC   -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of
CC       ubiquitin moieties onto substrate proteins (PubMed:20657603). May
CC       operate on tyrosine-phosphorylated SRC substrates (PubMed:22252131).
CC       {ECO:0000269|PubMed:20657603, ECO:0000269|PubMed:22252131}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000269|PubMed:20657603};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:20657603}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9JIY2}.
CC   -!- INTERACTION:
CC       Q8N7E2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12196065, EBI-3867333;
CC       Q8N7E2; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-12196065, EBI-10176379;
CC       Q8N7E2; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-12196065, EBI-2341787;
CC       Q8N7E2; P45984: MAPK9; NbExp=3; IntAct=EBI-12196065, EBI-713568;
CC       Q8N7E2; Q99750: MDFI; NbExp=3; IntAct=EBI-12196065, EBI-724076;
CC       Q8N7E2; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-12196065, EBI-10232538;
CC       Q8N7E2; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-12196065, EBI-740924;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20657603}.
CC       Note=Localized over the postacrosomal perinuclear theca region and the
CC       entire length of sperm tail. {ECO:0000269|PubMed:20657603}.
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in testis and sperm,
CC       including spermatocytes, round and elongated spermatids, and Leydig
CC       cells. {ECO:0000269|PubMed:20657603}.
CC   -!- DOMAIN: The HYB domain forms a phosphotyrosine-binding pocket upon
CC       dimerization, and mediates as well the recognition of its flanking
CC       acidic amino acids. {ECO:0000250|UniProtKB:Q9JIY2}.
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DR   EMBL; GQ355336; ADI56589.1; -; mRNA.
DR   EMBL; AK098601; BAC05348.1; -; mRNA.
DR   EMBL; BX293560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC074910; AAH74910.1; -; mRNA.
DR   EMBL; BC126190; AAI26191.1; -; mRNA.
DR   EMBL; BC126192; AAI26193.1; -; mRNA.
DR   CCDS; CCDS14205.1; -.
DR   RefSeq; NP_689790.1; NM_152577.3.
DR   AlphaFoldDB; Q8N7E2; -.
DR   SMR; Q8N7E2; -.
DR   BioGRID; 127688; 21.
DR   IntAct; Q8N7E2; 13.
DR   STRING; 9606.ENSP00000323348; -.
DR   iPTMnet; Q8N7E2; -.
DR   PhosphoSitePlus; Q8N7E2; -.
DR   BioMuta; ZNF645; -.
DR   DMDM; 74759980; -.
DR   PaxDb; Q8N7E2; -.
DR   PeptideAtlas; Q8N7E2; -.
DR   PRIDE; Q8N7E2; -.
DR   Antibodypedia; 399; 86 antibodies from 22 providers.
DR   DNASU; 158506; -.
DR   Ensembl; ENST00000323684.4; ENSP00000323348.2; ENSG00000175809.6.
DR   GeneID; 158506; -.
DR   KEGG; hsa:158506; -.
DR   MANE-Select; ENST00000323684.4; ENSP00000323348.2; NM_152577.4; NP_689790.1.
DR   UCSC; uc004dai.3; human.
DR   CTD; 158506; -.
DR   DisGeNET; 158506; -.
DR   GeneCards; CBLL2; -.
DR   HGNC; HGNC:26371; CBLL2.
DR   HPA; ENSG00000175809; Tissue enriched (testis).
DR   neXtProt; NX_Q8N7E2; -.
DR   OpenTargets; ENSG00000175809; -.
DR   PharmGKB; PA134934025; -.
DR   VEuPathDB; HostDB:ENSG00000175809; -.
DR   eggNOG; KOG2932; Eukaryota.
DR   GeneTree; ENSGT00510000047522; -.
DR   HOGENOM; CLU_031291_1_0_1; -.
DR   InParanoid; Q8N7E2; -.
DR   OMA; PIQWETV; -.
DR   OrthoDB; 765364at2759; -.
DR   PhylomeDB; Q8N7E2; -.
DR   TreeFam; TF332910; -.
DR   PathwayCommons; Q8N7E2; -.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q8N7E2; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 158506; 8 hits in 736 CRISPR screens.
DR   GenomeRNAi; 158506; -.
DR   Pharos; Q8N7E2; Tdark.
DR   PRO; PR:Q8N7E2; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q8N7E2; protein.
DR   Bgee; ENSG00000175809; Expressed in sperm and 14 other tissues.
DR   Genevisible; Q8N7E2; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0030155; P:regulation of cell adhesion; IBA:GO_Central.
DR   CDD; cd16508; RING-HC_HAKAI_like; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR040380; HAKAI-like_RING-HC.
DR   InterPro; IPR040383; HAKAI/CBLL2.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR041042; Znf_Hakai.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13480; PTHR13480; 1.
DR   Pfam; PF18408; zf_Hakai; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..425
FT                   /note="E3 ubiquitin-protein ligase CBLL2"
FT                   /id="PRO_0000056316"
FT   ZN_FING         57..97
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         112..138
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          96..154
FT                   /note="HYB domain"
FT   REGION          241..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..295
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         166
FT                   /note="D -> E (in dbSNP:rs5951426)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:20657603"
FT                   /id="VAR_030340"
FT   VARIANT         287
FT                   /note="S -> F (in dbSNP:rs12860105)"
FT                   /id="VAR_030341"
FT   CONFLICT        267
FT                   /note="P -> L (in Ref. 1; ADI56589)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        411
FT                   /note="H -> Q (in Ref. 1; ADI56589)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   425 AA;  48785 MW;  873C2802514CD9E5 CRC64;
     MNKMPAGEQE CEYNKEGKYY SKGVKLVRKK KKIPGYRWGD IKINIIGEKD DLPIHFCDKC
     DLPIKIYGRI IPCKHAFCYH CANLYDKVGY KVCPRCRYPV LRIEAHKRGS VFMCSIVQQC
     KRTYLSQKSL QAHIKRRHKR ARKQVTSASL EKVRPHIAPP QTEISDIPKR LQDRDHLSYI
     PPEQHTMVSL PSVQHMLQEQ HNQPHKDIQA PPPELSLSLP FPIQWETVSI FTRKHGNLTV
     DHIQNNSDSG AKKPTPPDYY PECQSQPAVS SPHHIIPQKQ HYAPPPSPSS PVNHQMPYPP
     QDVVTPNSVR SQVPALTTTY DPSSGYIIVK VPPDMNSPPL RAPQSQNGNP SASEFASHHY
     NLNILPQFTE NQETLSPQFT QTDAMDHRRW PAWKRLSPCP PTRSPPPSTL HGRSHHSHQR
     RHRRY
 
 
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