位置:首页 > 蛋白库 > HECD2_MOUSE
HECD2_MOUSE
ID   HECD2_MOUSE             Reviewed;         774 AA.
AC   Q8CDU6; E9QK99; Q8CBQ9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase HECTD2;
DE            EC=2.3.2.26 {ECO:0000250|UniProtKB:Q5U5R9};
DE   AltName: Full=HECT domain-containing protein 2;
DE   AltName: Full=HECT-type E3 ubiquitin transferase HECTD2;
GN   Name=Hectd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC       E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC       directly transfers the ubiquitin to targeted substrates.
CC       {ECO:0000250|UniProtKB:Q5U5R9}.
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=2.3.2.26; Evidence={ECO:0000250|UniProtKB:Q5U5R9};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q5U5R9}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29085.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK029549; BAC26510.1; -; mRNA.
DR   EMBL; AK035511; BAC29085.1; ALT_INIT; mRNA.
DR   EMBL; AC113514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC119947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS29773.1; -.
DR   RefSeq; NP_001156943.1; NM_001163471.1.
DR   RefSeq; NP_766225.2; NM_172637.3.
DR   AlphaFoldDB; Q8CDU6; -.
DR   SMR; Q8CDU6; -.
DR   BioGRID; 230470; 2.
DR   STRING; 10090.ENSMUSP00000128387; -.
DR   iPTMnet; Q8CDU6; -.
DR   PhosphoSitePlus; Q8CDU6; -.
DR   PaxDb; Q8CDU6; -.
DR   PRIDE; Q8CDU6; -.
DR   ProteomicsDB; 269555; -.
DR   Antibodypedia; 30347; 193 antibodies from 26 providers.
DR   DNASU; 226098; -.
DR   Ensembl; ENSMUST00000047247; ENSMUSP00000042646; ENSMUSG00000041180.
DR   GeneID; 226098; -.
DR   KEGG; mmu:226098; -.
DR   UCSC; uc008hho.2; mouse.
DR   CTD; 143279; -.
DR   MGI; MGI:2442663; Hectd2.
DR   VEuPathDB; HostDB:ENSMUSG00000041180; -.
DR   eggNOG; KOG0941; Eukaryota.
DR   GeneTree; ENSGT00940000157750; -.
DR   HOGENOM; CLU_002173_5_0_1; -.
DR   InParanoid; Q8CDU6; -.
DR   OrthoDB; 339404at2759; -.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 226098; 4 hits in 75 CRISPR screens.
DR   ChiTaRS; Hectd2; mouse.
DR   PRO; PR:Q8CDU6; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q8CDU6; protein.
DR   Bgee; ENSMUSG00000041180; Expressed in lateral septal nucleus and 207 other tissues.
DR   ExpressionAtlas; Q8CDU6; baseline and differential.
DR   Genevisible; Q8CDU6; MM.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   CDD; cd00078; HECTc; 1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..774
FT                   /note="Probable E3 ubiquitin-protein ligase HECTD2"
FT                   /id="PRO_0000240852"
FT   DOMAIN          435..774
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        742
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        315
FT                   /note="A -> G (in Ref. 1; BAC26510)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        754
FT                   /note="K -> R (in Ref. 1; BAC26510)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   774 AA;  87773 MW;  C7427B2D1C3E1957 CRC64;
     MSEAARDLSP GAPPAVAAAA PEERKGKEPE REKLPPIVTA GAAAGLDRGS KGQISTFSSF
     VSTVTQKKEA AENRSSPTHL ALPNIRNVRD LPPICLDVRQ KQRMSVEALP SEVKVPPLPE
     PSLPSQPKTV KDFEEDLEKA EATGNWKTVH AFYITAFDSF TELNTAFKKD ATASFNTIED
     SGLNANLVNA VFDALLNTPQ DIQKSVLKGI INSLLQEWKG PRTKDDLRAY FILLQNPQFN
     ITSTYVIYAH LLRQIATLVE ADHHFLVHWL KKLSQKKFKQ LVERLLQFVS LRLFPAKPEE
     FPPLTKCTWW IPSAAKVLAL LNTANNLVHP PLVPYTDFYN STLDHIDLME EYHTWQSFGN
     SHRFSFCQYP FVISIAAKKI IIQRDSEQQM ISIARQSLVD KVSRRQRPDM NMLFLNMKVR
     RTHLVSDSLD ELTRKRADLK KKLKVTFVGE AGLDMGGLTK EWFLLLIRQI FHPDYGMFTY
     HKDSHCHWFS SFKCDNYSEF RLVGILMGLA VYNSITLDIR FPPCCYKKLL SPPVVPSDQS
     TPVGICSVTI DDLCQVMPEL AHGLKELLSY EGNVEEDFYS TFQVFQEEFG VIKSYNLKPG
     GDKIPVTNQN RREYVQLYTD FLLNKSIYKQ FAAFYCGFHS VCASNALMLL RPEEVEILVC
     GSPELDMHAL QRSTQYDGYA KTDLTIRYFW DVVLGFPLEL QKKLLHFTTG SDRVPVGGMA
     DLNFKISKNE TSTNWLPVAH TCFNQLCLPP YKSKKDLKQK LIIGISNSEG FGLE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024