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Q7TMY8

- HUWE1_MOUSE

UniProt

Q7TMY8 - HUWE1_MOUSE

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Protein

E3 ubiquitin-protein ligase HUWE1

Gene
Huwe1, Kiaa0312, Ureb1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1. Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair. Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4. Binds to an upstream initiator-like sequence in the preprodynorphin gene By similarity. Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN. May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation By similarity.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei4344 – 43441Glycyl thioester intermediate By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. ligase activity Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. base-excision repair Source: UniProtKB
  2. cell differentiation Source: UniProtKB-KW
  3. histone ubiquitination Source: UniProtKB
  4. protein monoubiquitination Source: UniProtKB
  5. protein polyubiquitination Source: UniProtKB
  6. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Differentiation, DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase HUWE1 (EC:6.3.2.-)
Alternative name(s):
E3Histone
HECT, UBA and WWE domain-containing protein 1
Upstream regulatory element-binding protein 1
Short name:
URE-B1
Short name:
URE-binding protein 1
Gene namesi
Name:Huwe1
Synonyms:Kiaa0312, Ureb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1926884. Huwe1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Mainly expressed in the cytoplasm of most tissues, except in the nucleus of spermatogonia, primary spermatocytes and neuronal cells.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 43774377E3 ubiquitin-protein ligase HUWE1PRO_0000120341Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1084 – 10841Phosphoserine By similarity
Modified residuei1368 – 13681Phosphoserine By similarity
Modified residuei1370 – 13701Phosphoserine By similarity
Modified residuei1395 – 13951Phosphoserine1 Publication
Modified residuei1907 – 19071Phosphoserine2 Publications
Modified residuei2267 – 22671N6-acetyllysine1 Publication
Modified residuei2362 – 23621Phosphoserine By similarity
Modified residuei2365 – 23651Phosphoserine By similarity
Modified residuei2391 – 23911Phosphoserine By similarity
Modified residuei2595 – 25951Phosphoserine By similarity
Modified residuei2619 – 26191Phosphoserine By similarity
Modified residuei2751 – 27511Phosphothreonine By similarity
Modified residuei2887 – 28871Phosphoserine By similarity
Modified residuei2918 – 29181Phosphoserine By similarity
Modified residuei3116 – 31161Phosphoserine By similarity
Modified residuei3127 – 31271Phosphoserine By similarity
Modified residuei3663 – 36631Phosphoserine By similarity
Modified residuei3753 – 37531Phosphoserine By similarity
Modified residuei3758 – 37581Phosphoserine By similarity
Modified residuei3761 – 37611Phosphoserine By similarity
Modified residuei3810 – 38101Phosphoserine1 Publication
Modified residuei3818 – 38181Phosphoserine By similarity
Modified residuei3922 – 39221Phosphoserine By similarity
Modified residuei3927 – 39271Phosphothreonine By similarity
Modified residuei3930 – 39301Phosphothreonine By similarity

Post-translational modificationi

Phosphorylated on tyrosine; phosphorylation is probably required for its ability to inhibit TP53 transactivation By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7TMY8.
PaxDbiQ7TMY8.
PRIDEiQ7TMY8.

PTM databases

PhosphoSiteiQ7TMY8.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Developmental stagei

Expression increases during neuronal differentiation such that the cortical plate contains the highest level.1 Publication

Gene expression databases

ArrayExpressiQ7TMY8.
BgeeiQ7TMY8.
CleanExiMM_HUWE1.
GenevestigatoriQ7TMY8.

Interactioni

Subunit structurei

Interacts with isoform p19ARF of CDKN2A which strongly inhibits HUWE1 ubiquitin ligase activity By similarity. Interacts with MYCN, POLB and CDC6 By similarity.

Protein-protein interaction databases

BioGridi208493. 9 interactions.
IntActiQ7TMY8. 3 interactions.
MINTiMINT-4139570.
STRINGi10090.ENSMUSP00000026292.

Structurei

3D structure databases

ProteinModelPortaliQ7TMY8.
SMRiQ7TMY8. Positions 1310-1356, 4003-4369.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1316 – 135540UBAAdd
BLAST
Repeati1370 – 138920UIMAdd
BLAST
Domaini1603 – 168078WWEAdd
BLAST
Domaini4041 – 4377337HECTAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2295 – 2469175Glu-richAdd
BLAST
Compositional biasi2427 – 249064Asp-richAdd
BLAST
Compositional biasi3484 – 355269Thr-richAdd
BLAST

Domaini

The HECT domain mediates inhibition of the transcriptional activity of p53 By similarity.

Sequence similaritiesi

Contains 1 UBA domain.
Contains 1 WWE domain.

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00750000117291.
HOVERGENiHBG080254.
KOiK10592.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR025527. DUF4414.
IPR010309. E3_Ub_ligase_DUF908.
IPR010314. E3_Ub_ligase_DUF913.
IPR000569. HECT.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR004170. WWE-dom.
[Graphical view]
PfamiPF14377. DUF4414. 1 hit.
PF06012. DUF908. 1 hit.
PF06025. DUF913. 1 hit.
PF00632. HECT. 1 hit.
PF00627. UBA. 1 hit.
PF02825. WWE. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF48371. SSF48371. 3 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS50030. UBA. 1 hit.
PS50918. WWE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7TMY8-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MKVDRTKLKK TPTEAPADCR ALIDKLKVCN DEQLLLELQQ IKTWNIGKCE     50
LYHWVDLLDR FDGILADAGQ TVENMSWMLV CDRPEKEQLK MLLLAVLNFT 100
ALLIEYSFSR HLYSSIEHLT TLLASSDMQV VLAVLNLLYV FSKRSNYITR 150
LGSDKRTPLL TRLQHLAESW GGKENGFGLA ECCRDLQMLK YPPSATTLHF 200
EFYADPGAEV KIEKRTTSNT LHYIHIEQLD KISESPSEIM ESLTKMYSIP 250
KDKQMLLFTH IRLAHGFSNH RKRLQAVQAR LHAISILVYS NALQESANSI 300
LYNGLIEELV DVLQITDKQL MEIKAASLRT LTSIVHLERT PKLSSIIDCT 350
GTASYHGFLP VLVRNCIQAM IDPSMDPYPH QFATALFSFL YHLASYDAGG 400
EALVSCGMME ALLKVIKFLG DEQDQITFVT RAVRVVDLIT NLDMAAFQSH 450
SGLSIFIYRL EHEVDLCRKE CPFVIKPKIQ RPSTTQEGEE METDMDGVQC 500
IPQRAALLKS MLNFLKKAIQ DPAFSDGIRH VMDGSLPTSL KHIISNAEYY 550
GPSLFLLATE VVTVFVFQEP SLLSSLQDNG LTDVMLHALL IKDVPATREV 600
LGSLPNVFSA LCLNARGLQS FVQCQPFERL FKVLLSPDYL PAMRRRRSSD 650
PLGDTASNLG SAVDELMRHQ PTLKTDATTA IIKLLEEICN LGRDPKYICQ 700
KPSIQKADGT ATAPPPRSNH AAEEASSEDE EEEEVQAMQS FNSAQQNETE 750
PNQQVVGTEE RIPIPLMDYI LNVMKFVESI LSNNTTDDHC QEFVNQKGLL 800
PLVTILGLPN LPIDFPTSAA CQAVAGVCKS ILTLSHEPKV LQEGLLQLDL 850
ILSSLEPLHR PIESPGGSVL LRELACAGNV ADATLSAQAT PLLHALTAAH 900
AYIMMFVHTC RVGQSEIRSI SVNQWGSQLG LSVLSKLSQL YCSLVWESTV 950
LLSLCTPNSL PSGCEFGQAD MQKLVPKDEK AGTTQGGKRS DGEQDGTAGS 1000
MDASAQGLLE GIELDGDTLA PMETDEPSSS DSKGKSKITP AMAARIKQIK 1050
PLLSASSRLG RALAELFGLL VKLCVGSPVR QRRSHHAAST TTAPTPAARS 1100
TASALTKLLT KGLSWQPPPY TPTPRFRLTF FICSVGFTSP MLFDERKYPY 1150
HLMLQKFLCS GGHNALFETF NWALSMGGKV PVSEGLEHSD LPDGTGEFLD 1200
AWLMLVEKMV NPTTVLESPH SLPAKLPGGV QSFPQFSALR FLVVTQKAAF 1250
TCIKNLWNRK PLKVYGGRMA ESMLAILCHI LRGEPVIRER LSKEKEGSRG 1300
EEEAGQEEGG SRREPQVNQQ QLQQLMDMGF TREHAMEALL NTSTMEQATE 1350
YLLTHPPPII GGVVRDLSMS EEDQMMRAIA MSLGQDIPMD QRAESPEEVA 1400
CRKEEEERKA REKQEEEEAK CLEKFQDADP LEQDELHTFT DTMLPGCFHL 1450
LDELPDTVYR VCDLIMTAIK RNGADYRDMI LKQVVNQVWE AADVLIKAAL 1500
PLTTSDTKTV SEWISQMATL PQASNLATRI LLLTLLFEEL KLPCAWVVES 1550
SGILNVLIKL LEVVQPCLQA AKEQKEVQTP KWITPVLLLI DFYEKTAISS 1600
KRRAQMTKYL QSNSNNWRWF DDRSGRWCSY SASNNSTIDS AWKSGETSVR 1650
FTAGRRRYTV QFTTMVQVNE ETGNRRPVML TLLRVPRLSK NSKSSNGQEL 1700
EKTLEESKET DIKHKENKGN DIPLALESTN TEKEASLDET KIGEILIQGL 1750
TEDMVTVLIR ACVSMLGVPV DPDTLHATLR LCLRLTRDHK YAMMFAELKS 1800
TRMILNLTQS SGFNGFTPLV TLLLRHIIED PCTLRHTMEK VVRSAATSGA 1850
GSTTSGVVSG SLGSREINYI LRVLGPAACR NPDIFTEVAN CCIRIALPAP 1900
RGSGTASDDE FENLRIKGPN AVQLVKTTPL KPSSLPVIPD TIKEVIYDML 1950
NALAAYHAPE EADKSDPKPG GTTQEVGQLL QDMGDDVYQQ YRSLTRQSSD 2000
FDTQSGFSLN SQVFAADGAP AETSTTGTSQ GEASTPEETR EGKKDKEGDR 2050
TSEEGKQKSK GSKPLMPTST ILRLLAELVR SYVGIATLIA NYSYTVGQSE 2100
LIKEDCSVLA FVLDHLLPHT QNAEDKDTPA LARLFLASLA AAGSGTDAQV 2150
ALVNEVKAAL GRALAMAEST EKHARLQAVM CIISTIMESC PSTSSFYSSA 2200
TAKTQHNGMN NIIRLFLKKG LVNDLARVPH SLDLSSPNMA NTVNAALKPL 2250
ETLSRIVNQP SSLFGSKSAS SKNKSEQDAQ GASQDSSSHQ QDPGEPGEAE 2300
VQEEDHDVTQ TEVADGDIMD GEAETDSVVI AGQPEVLSSQ EMQVENELED 2350
LIDELLERDG GSGNSTIIVS RSGEDESQED VLMDEAPSNL SQASTLQANR 2400
EDSMNILDPE DEEEHTQEED SSGSNEDEDD SQDEEEEEEE DEEDDQEDDE 2450
GEEGDEDDDD DGSEMELDED YPDMNASPLV RFERFDREDD LIIEFDNMFS 2500
SATDIPPSPG NIPTTHPLMV RHADHSSLTL GSGSSTTRLT QGIGRSQRTL 2550
RQLTANTGHT IHVHYPGNRQ PNPPLILQRL LGPSAAADIL QLSSSLPLQS 2600
RGRARLLVGN DDVHIIARSD DELLDDFFHD QSTATSQAGT LSSIPTALTR 2650
WTEECKVLDA ESMHDCVSVV KVPIVNHLEF LRDEELEERR EKRRKQLAEE 2700
ETKIIDKGKE DKENRDQSAQ CTVTKTNDST EQNVSDGTPM PDSYPTTPSS 2750
TDAPTSESKE TLGTLQPSQQ QPALPPPPSL GEIPQELQSP AEEVANSTQL 2800
LMPIELEELG PTRPSGEAET TQMELSPAPT ITSLSPERAE DSDALTAVSS 2850
QLEGSPMDTS SLASCTLEEA VGDTPAAGSS EQPTAGSSTP GDAPSVVAEV 2900
QGRPDVSRES NQPPEDSSPP ASSESSSTRD SAVAISGADS RGILEEPLPS 2950
TSSEEEDPLA GISLPEGVDP SFLAALPDDI RREVLQNQLG IRPPTRSAPS 3000
SNSSAPAVVG NPGVTEVSPE FLAALPPAIQ EEVLAQQRAE QQRRELAQNA 3050
SSDTPMDPVT FIQTLPSDLR RSVLEDMEDS VLAVMPPDIA AEAQALRREQ 3100
EARQRQLMHE RLFGHSSTSA LSAILRSPAF TSRLSGNRGV QYTRLAVQRG 3150
GTFQMGGSSS HNRPSGSNVD TLLRLRGRLL LDHEALSCLL VLLFVDEPKL 3200
NTSRLHRVLR NLCYHAQTRH WVIRSLLSIL QRSSESELCI ETPKLSTSEE 3250
RGKKSSKSCA SSSHENRPLD LLHKMESKSS NQLSWLSVSM DAALGCRTNI 3300
FQIQRSGGRK HTEKHASSGS TVHIHPQAAP VVCRHVLDTL IQLAKVFPSH 3350
FTQQRTKETN CESDRERGSK QACSPCSSQS SSSGICTDFW DLLVKLDNMN 3400
VSRKGKNSVK SVPVSSGGEG ETSPHSLEAS PLGQLMNMLS HPVIRRSSLL 3450
TEKLLRLLSL ISIALPENKV SEVQTNSSNS GSSTAATSNT STTTTTTTTA 3500
TAPTPTPPAA TTPVTSAPAL VAATAISTIT VAASTTVTTP TTATTTVSTS 3550
TTKGSKSPAK VGEGGSGIDF KMVSSGLTEN QLQLSVEVLT SHSCSEEGLE 3600
DAANVLLQLS RGDSGTRDTV LKLLLNGARH LGYTLCKQIG TLLAELREYN 3650
LEQQRRAQCE TLSPDGLPEE QPQTTKLKGK MQSRFDMAEN VVIVASQKRP 3700
LGGRELQLPS MSMLTSKTST QKFFLRVLQV IIQLRDDTRR ANKKAKQTGR 3750
LGSSGLGSAS SIQAAVRQLE AEADAIIQMV REGQRARRQQ QAATSESSNQ 3800
SETSVRREES PMDVDQPSPS AQDTQSIVIS DGTPQGEKEK EEKPPELPLL 3850
SEQLSLDELW DMLGECLKEL EESHDQHAVL VLQPAVEAFF LVHATERESK 3900
PPVRDTRESQ LAHIKDEPPP LSPAPLTPAT PSSLDPFFSR EPSSMHISSS 3950
LPPDTQKFLR FAETHRTVLN QILRQSTTHL ADGPFAVLVD YIRVLDFDVK 4000
RKYFRQELER LDEGLRKEDM AVHVRRDHVF EDSYRELHRK SPEEMKNRLY 4050
IVFEGEEGQD AGGLLREWYM IISREMFNPM YALFRTSPGD RVTYTINPSS 4100
HCNPNHLSYF KFVGRIVAKA VYDNRLLECY FTRSFYKHIL GKSVRYTDME 4150
SEDYHFYQGL VYLLENDVST LGYDLTFSTE VQEFGVCEVR DLKPNGANIL 4200
VTEENKKEYV HLVCQMRMTG AIRKQLAAFL EGFYEIIPKR LISIFTEQEL 4250
ELLISGLPTI DIDDLKSNTE YHKYQSNSIQ IQWFWRALRS FDQADRAKFL 4300
QFVTGTSKVP LQGFAALEGM NGIQKFQIHR DDRSTDRLPS AHTCFNQLDL 4350
PAYESFEKLR HMLLLAIQEC SEGFGLA 4377
Length:4,377
Mass (Da):482,635
Last modified:July 27, 2011 - v5
Checksum:i22700C859CD9AF83
GO
Isoform 2 (identifier: Q7TMY8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3347-3364: FPSHFTQQRTKETNCESD → RSLKESLTPGFFGHQHLG
     3365-4377: Missing.

Note: No experimental confirmation available.

Show »
Length:3,364
Mass (Da):369,701
Checksum:iBD5116429BF0E509
GO
Isoform 3 (identifier: Q7TMY8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3780-3794: Missing.

Note: No experimental confirmation available.

Show »
Length:4,362
Mass (Da):480,898
Checksum:i0D640BFE13725964
GO
Isoform 4 (identifier: Q7TMY8-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3795-3832: SESSNQSETS...DTQSIVISDG → VSMMPVAPHS...LVCFCITFAK
     3833-4377: Missing.

Note: No experimental confirmation available.

Show »
Length:3,832
Mass (Da):419,496
Checksum:iC8B75208FD6CB0EC
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3347 – 336418FPSHF…NCESD → RSLKESLTPGFFGHQHLG in isoform 2. VSP_011147Add
BLAST
Alternative sequencei3365 – 43771013Missing in isoform 2. VSP_011148Add
BLAST
Alternative sequencei3780 – 379415Missing in isoform 3. VSP_011149Add
BLAST
Alternative sequencei3795 – 383238SESSN…VISDG → VSMMPVAPHSFLYPPSCTMS SVGVHCPYLVCFCITFAK in isoform 4. VSP_011150Add
BLAST
Alternative sequencei3833 – 4377545Missing in isoform 4. VSP_011151Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531K → R in AAX24124. 1 Publication
Sequence conflicti253 – 2531K → R in AAV90839. 1 Publication
Sequence conflicti1728 – 17281S → I in AAV90839. 1 Publication
Sequence conflicti1728 – 17281S → I in BAC41411. 1 Publication
Sequence conflicti2032 – 20321E → EG in AAV90839. 1 Publication
Sequence conflicti2032 – 20321E → EG in BAC41411. 1 Publication
Sequence conflicti2032 – 20321E → EG in AAH70444. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY772010 mRNA. Translation: AAV90839.3.
AY929611 mRNA. Translation: AAX24124.1.
BX571795, AL672180, AL954855 Genomic DNA. Translation: CAM13774.1.
AL954855, AL672180, BX571795 Genomic DNA. Translation: CAM17616.1.
AL672180, AL954855, BX571795 Genomic DNA. Translation: CAM23826.1.
AB093227 mRNA. Translation: BAC41411.2.
BC011391 mRNA. Translation: AAH11391.1.
BC017642 mRNA. Translation: AAH17642.2.
BC054372 mRNA. Translation: AAH54372.1.
BC070444 mRNA. Translation: AAH70444.1.
AK083499 mRNA. Translation: BAC38936.1.
AB025966 mRNA. Translation: BAA84697.1.
RefSeqiNP_067498.4. NM_021523.4.
UniGeneiMm.27372.
Mm.488413.

Genome annotation databases

EnsembliENSMUST00000112622; ENSMUSP00000108241; ENSMUSG00000025261. [Q7TMY8-1]
GeneIDi59026.
KEGGimmu:59026.
UCSCiuc009upq.2. mouse. [Q7TMY8-1]
uc009upr.1. mouse. [Q7TMY8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY772010 mRNA. Translation: AAV90839.3 .
AY929611 mRNA. Translation: AAX24124.1 .
BX571795 , AL672180 , AL954855 Genomic DNA. Translation: CAM13774.1 .
AL954855 , AL672180 , BX571795 Genomic DNA. Translation: CAM17616.1 .
AL672180 , AL954855 , BX571795 Genomic DNA. Translation: CAM23826.1 .
AB093227 mRNA. Translation: BAC41411.2 .
BC011391 mRNA. Translation: AAH11391.1 .
BC017642 mRNA. Translation: AAH17642.2 .
BC054372 mRNA. Translation: AAH54372.1 .
BC070444 mRNA. Translation: AAH70444.1 .
AK083499 mRNA. Translation: BAC38936.1 .
AB025966 mRNA. Translation: BAA84697.1 .
RefSeqi NP_067498.4. NM_021523.4.
UniGenei Mm.27372.
Mm.488413.

3D structure databases

ProteinModelPortali Q7TMY8.
SMRi Q7TMY8. Positions 1310-1356, 4003-4369.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208493. 9 interactions.
IntActi Q7TMY8. 3 interactions.
MINTi MINT-4139570.
STRINGi 10090.ENSMUSP00000026292.

PTM databases

PhosphoSitei Q7TMY8.

Proteomic databases

MaxQBi Q7TMY8.
PaxDbi Q7TMY8.
PRIDEi Q7TMY8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000112622 ; ENSMUSP00000108241 ; ENSMUSG00000025261 . [Q7TMY8-1 ]
GeneIDi 59026.
KEGGi mmu:59026.
UCSCi uc009upq.2. mouse. [Q7TMY8-1 ]
uc009upr.1. mouse. [Q7TMY8-2 ]

Organism-specific databases

CTDi 10075.
MGIi MGI:1926884. Huwe1.
Rougei Search...

Phylogenomic databases

eggNOGi COG5021.
GeneTreei ENSGT00750000117291.
HOVERGENi HBG080254.
KOi K10592.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSi HUWE1. mouse.
NextBioi 314602.
PROi Q7TMY8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q7TMY8.
Bgeei Q7TMY8.
CleanExi MM_HUWE1.
Genevestigatori Q7TMY8.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR025527. DUF4414.
IPR010309. E3_Ub_ligase_DUF908.
IPR010314. E3_Ub_ligase_DUF913.
IPR000569. HECT.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR004170. WWE-dom.
[Graphical view ]
Pfami PF14377. DUF4414. 1 hit.
PF06012. DUF908. 1 hit.
PF06025. DUF913. 1 hit.
PF00632. HECT. 1 hit.
PF00627. UBA. 1 hit.
PF02825. WWE. 1 hit.
[Graphical view ]
SMARTi SM00119. HECTc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF48371. SSF48371. 3 hits.
SSF56204. SSF56204. 1 hit.
PROSITEi PS50237. HECT. 1 hit.
PS50030. UBA. 1 hit.
PS50918. WWE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor."
    Chen D., Kon N., Li M., Zhang W., Qin J., Gu W.
    Cell 121:1071-1083(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  2. Chen D., Kon N., Li M., Zhang W., Qin J., Gu W.
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 253; 1728; 2009-2010; 2032 AND 3034-3035.
  3. "Characterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones."
    Liu Z., Oughtred R., Wing S.S.
    Mol. Cell. Biol. 25:2819-2831(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Strain: C57BL/6J.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
    DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1445-4377 (ISOFORM 1).
    Tissue: Embryonic intestine.
  6. Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
    Tissue: Brain.
  7. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1627-1655; 3127-3133 AND 3245-3253, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  8. "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] OF 1630-4377 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3283-4377 (ISOFORM 3).
    Strain: C57BL/6 and FVB/N-3.
    Tissue: Brain, Eye and Mammary gland.
  9. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3421-4377 (ISOFORM 4).
    Strain: C57BL/6J.
  10. "Mouse homolog to KIAA0312."
    Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4005-4377 (ISOFORMS 1/3).
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  12. "Regulated expression of the ubiquitin protein ligase, E3(Histone)/LASU1/Mule/ARF-BP1/HUWE1, during spermatogenesis."
    Liu Z., Miao D., Xia Q., Hermo L., Wing S.S.
    Dev. Dyn. 236:2889-2898(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1395; SER-1907 AND SER-3810, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "The HECT-domain ubiquitin ligase Huwe1 controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein."
    Zhao X., Heng J.I.-T., Guardavaccaro D., Jiang R., Pagano M., Guillemot F., Iavarone A., Lasorella A.
    Nat. Cell Biol. 10:643-653(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  15. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1907, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  16. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHUWE1_MOUSE
AccessioniPrimary (citable) accession number: Q7TMY8
Secondary accession number(s): A2AFQ1
, Q4G2Z1, Q5BMM7, Q6NS61, Q8BNJ7, Q8CFH2, Q8VD14, Q921M5, Q9R0P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 102 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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