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