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Q7Z6Z7

- HUWE1_HUMAN

UniProt

Q7Z6Z7 - HUWE1_HUMAN

Protein

E3 ubiquitin-protein ligase HUWE1

Gene

HUWE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (30 Aug 2005)
      Previous versions | rss
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    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. 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.7 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei4341 – 43411Glycyl thioester intermediate

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. ligase activity Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. 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

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Differentiation, DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase HUWE1 (EC:6.3.2.-)
    Alternative name(s):
    ARF-binding protein 1
    Short name:
    ARF-BP1
    HECT, UBA and WWE domain-containing protein 1
    Homologous to E6AP carboxyl terminus homologous protein 9
    Short name:
    HectH9
    Large structure of UREB1
    Short name:
    LASU1
    Mcl-1 ubiquitin ligase E3
    Short name:
    Mule
    Upstream regulatory element-binding protein 1
    Short name:
    URE-B1
    Short name:
    URE-binding protein 1
    Gene namesi
    Name:HUWE1
    Synonyms:KIAA0312, KIAA1578, UREB1
    ORF Names:HSPC272
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:30892. HUWE1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Mainly expressed in the cytoplasm of most tissues, except in the nucleus of spermatogonia, primary spermatocytes and neuronal cells By similarity. Predominantly cytosolic or perinuclear in some colorectal carcinoma cells.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, X-linked, syndromic, Turner type (MRXST) [MIM:300706]: A syndrome characterized by the association of mental retardation with macrocephaly and variable contractures.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Mental retardation, X-linked 17 (MRX17) [MIM:300705]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.1 Publication
    Note: The gene represented in this entry is involved in disease pathogenesis. A chromosomal microduplication involving HSD17B10 and HUWE1 has been found in patients with mental retardation.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4268 – 42681Y → S: Loss of activity. 1 Publication
    Mutagenesisi4341 – 43411C → A or D: Loss of activity. 4 Publications

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi300705. phenotype.
    300706. phenotype.
    Orphaneti85328. intellectual disability, X-linked, Turner type.
    PharmGKBiPA128394567.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 43744374E3 ubiquitin-protein ligase HUWE1PRO_0000120340Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1084 – 10841Phosphoserine3 Publications
    Modified residuei1368 – 13681Phosphoserine2 Publications
    Modified residuei1370 – 13701Phosphoserine1 Publication
    Modified residuei1395 – 13951Phosphoserine3 Publications
    Modified residuei1722 – 17221Phosphothreonine1 Publication
    Modified residuei1907 – 19071Phosphoserine5 Publications
    Modified residuei2267 – 22671N6-acetyllysineBy similarity
    Modified residuei2362 – 23621Phosphoserine7 Publications
    Modified residuei2365 – 23651Phosphoserine3 Publications
    Modified residuei2391 – 23911Phosphoserine1 Publication
    Modified residuei2595 – 25951Phosphoserine2 Publications
    Modified residuei2619 – 26191Phosphoserine1 Publication
    Modified residuei2751 – 27511Phosphothreonine1 Publication
    Modified residuei2887 – 28871Phosphoserine3 Publications
    Modified residuei2918 – 29181Phosphoserine1 Publication
    Modified residuei3116 – 31161Phosphoserine1 Publication
    Modified residuei3127 – 31271Phosphoserine1 Publication
    Modified residuei3662 – 36621Phosphoserine2 Publications
    Modified residuei3752 – 37521Phosphoserine1 Publication
    Modified residuei3757 – 37571Phosphoserine2 Publications
    Modified residuei3760 – 37601Phosphoserine1 Publication
    Modified residuei3808 – 38081Phosphoserine1 Publication
    Modified residuei3816 – 38161Phosphoserine1 Publication
    Modified residuei3919 – 39191Phosphoserine3 Publications
    Modified residuei3924 – 39241Phosphothreonine2 Publications
    Modified residuei3927 – 39271Phosphothreonine1 Publication

    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

    MaxQBiQ7Z6Z7.
    PaxDbiQ7Z6Z7.
    PRIDEiQ7Z6Z7.

    PTM databases

    PhosphoSiteiQ7Z6Z7.

    Expressioni

    Tissue specificityi

    Weakly expressed in heart, brain and placenta but not in other tissues. Expressed in a number of cell lines, predominantly in those from colorectal carcinomas.1 Publication

    Gene expression databases

    ArrayExpressiQ7Z6Z7.
    BgeeiQ7Z6Z7.
    GenevestigatoriQ7Z6Z7.

    Organism-specific databases

    HPAiCAB022718.
    HPA002548.

    Interactioni

    Subunit structurei

    Interacts with isoform p14ARF of CDKN2A which strongly inhibits HUWE1 ubiquitin ligase activity. Interacts with MYCN, POLB and CDC6.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDKN2AQ8N7264EBI-625934,EBI-625922
    TP53P046373EBI-625934,EBI-366083
    USP4Q131074EBI-625934,EBI-723290

    Protein-protein interaction databases

    BioGridi115385. 70 interactions.
    DIPiDIP-34362N.
    IntActiQ7Z6Z7. 25 interactions.
    MINTiMINT-1576525.

    Structurei

    Secondary structure

    1
    4374
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1319 – 132911
    Helixi1332 – 134110
    Helixi1345 – 13539
    Helixi3994 – 400815
    Turni4009 – 40113
    Beta strandi4016 – 40216
    Helixi4023 – 40253
    Helixi4026 – 40349
    Helixi4041 – 40433
    Beta strandi4044 – 40507
    Helixi4061 – 407212
    Helixi4076 – 40783
    Beta strandi4080 – 40834
    Turni4085 – 40873
    Beta strandi4088 – 40936
    Helixi4095 – 40995
    Helixi4103 – 412018
    Helixi4130 – 41378
    Helixi4143 – 41453
    Helixi4146 – 41494
    Helixi4151 – 416212
    Helixi4165 – 41673
    Beta strandi4168 – 41703
    Beta strandi4172 – 41754
    Turni4176 – 41783
    Beta strandi4181 – 41833
    Helixi4186 – 41894
    Beta strandi4193 – 41975
    Turni4200 – 42023
    Helixi4203 – 421513
    Helixi4217 – 42193
    Helixi4220 – 423314
    Helixi4236 – 42394
    Helixi4244 – 42529
    Helixi4259 – 42646
    Beta strandi4266 – 42716
    Helixi4276 – 428712
    Helixi4290 – 430112
    Beta strandi4302 – 43043
    Helixi4311 – 43133
    Beta strandi4317 – 43204
    Beta strandi4323 – 43286
    Beta strandi4337 – 43393
    Helixi4340 – 43423
    Beta strandi4344 – 43485
    Helixi4353 – 436513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EKKNMR-A1317-1356[»]
    3G1NX-ray2.60A/B4005-4374[»]
    3H1DX-ray1.89A3993-4374[»]
    ProteinModelPortaliQ7Z6Z7.
    SMRiQ7Z6Z7. Positions 1310-1356, 4000-4366.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7Z6Z7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1316 – 135540UBAPROSITE-ProRule annotationAdd
    BLAST
    Repeati1370 – 138920UIMAdd
    BLAST
    Domaini1603 – 168078WWEPROSITE-ProRule annotationAdd
    BLAST
    Domaini4038 – 4374337HECTPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2295 – 2469175Glu-richAdd
    BLAST
    Compositional biasi2427 – 249064Asp-richAdd
    BLAST
    Compositional biasi3483 – 355068Thr-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the UPL family. TOM1/PTR1 subfamily.Curated
    Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
    Contains 1 UBA domain.PROSITE-ProRule annotation
    Contains 1 WWE domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5021.
    HOVERGENiHBG080254.
    KOiK10592.
    OMAiGMTQEVG.
    PhylomeDBiQ7Z6Z7.
    TreeFamiTF323417.

    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z6Z7-1) [UniParc]FASTAAdd to Basket

    Also known as: LASU1, Large structure of UREB1

    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 CDRPEREQLK MLLLAVLNFT 100
    ALLIEYSFSR HLYSSIEHLT TLLASSDMQV VLAVLNLLYV FSKRSNYITR 150
    LGSDKRTPLL TRLQHLAESW GGKENGFGLA ECCRDLHMMK 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 RPNTTQEGEE 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 FNSTQQNETE 750
    PNQQVVGTEE RIPIPLMDYI LNVMKFVESI LSNNTTDDHC QEFVNQKGLL 800
    PLVTILGLPN LPIDFPTSAA CQAVAGVCKS ILTLSHEPKV LQEGLLQLDS 850
    ILSSLEPLHR PIESPGGSVL LRELACAGNV ADATLSAQAT PLLHALTAAH 900
    AYIMMFVHTC RVGQSEIRSI SVNQWGSQLG LSVLSKLSQL YCSLVWESTV 950
    LLSLCTPNSL PSGCEFGQAD MQKLVPKDEK AGTTQGGKRS DGEQDGAAGS 1000
    MDASTQGLLE GIGLDGDTLA PMETDEPTAS DSKGKSKITP AMAARIKQIK 1050
    PLLSASSRLG RALAELFGLL VKLCVGSPVR QRRSHHAAST TTAPTPAARS 1100
    TASALTKLLT KGLSWQPPPY TPTPRFRLTF FICSVGFTSP MLFDERKYPY 1150
    HLMLQKFLCS GGHNALFETF NWALSMGGKV PVSEGLEHSD LPDGTGEFLD 1200
    AWLMLVEKMV NPTTVLESPH SLPAKLPGGV QNFPQFSALR FLVVTQKAAF 1250
    TCIKNLWNRK PLKVYGGRMA ESMLAILCHI LRGEPVIRER LSKEKEGSRG 1300
    EEDTGQEEGG SRREPQVNQQ QLQQLMDMGF TREHAMEALL NTSTMEQATE 1350
    YLLTHPPPIM 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 TLLRVPRLNK NSKNSNGQEL 1700
    EKTLEESKEM DIKRKENKGN DTPLALESTN TEKETSLEET KIGEILIQGL 1750
    TEDMVTVLIR ACVSMLGVPV DPDTLHATLR LCLRLTRDHK YAMMFAELKS 1800
    TRMILNLTQS SGFNGFTPLV TLLLRHIIED PCTLRHTMEK VVRSAATSGA 1850
    GSTTSGVVSG SLGSREINYI LRVLGPAACR NPDIFTEVAN CCIRIALPAP 1900
    RGSGTASDDE FENLRIKGPN AVQLVKTTPL KPSPLPVIPD TIKEVIYDML 1950
    NALAAYHAPE EADKSDPKPG VMTQEVGQLL QDMGDDVYQQ YRSLTRQSSD 2000
    FDTQSGFSIN SQVFAADGAS TETSASGTSQ GEASTPEESR DGKKDKEGDR 2050
    ASEEGKQKGK 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 GASQDSSSNQ 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 KVSIVNHLEF LRDEELEERR EKRRKQLAEE 2700
    ETKITDKGKE DKENRDQSAQ CTASKSNDST EQNLSDGTPM PDSYPTTPSS 2750
    TDAATSESKE TLGTLQSSQQ QPTLPTPPAL GEVPQELQSP AGEGGSSTQL 2800
    LMPVEPEELG PTRPSGEAET TQMELSPAPT ITSLSPERAE DSDALTAVSS 2850
    QLEGSPMDTS SLASCTLEEA VGDTSAAGSS EQPRAGSSTP GDAPPAVAEV 2900
    QGRSDGSGES AQPPEDSSPP ASSESSSTRD SAVAISGADS RGILEEPLPS 2950
    TSSEEEDPLA GISLPEGVDP SFLAALPDDI RREVLQNQLG IRPPTRTAPS 3000
    TNSSAPAVVG 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 ETPKLTTSEE 3250
    KGKKSSKSCG SSSHENRPLD LLHKMESKSS NQLSWLSVSM DAALGCRTNI 3300
    FQIQRSGGRK HTEKHASGGS TVHIHPQAAP VVCRHVLDTL IQLAKVFPSH 3350
    FTQQRTKETN CESDRERGNK ACSPCSSQSS SSGICTDFWD LLVKLDNMNV 3400
    SRKGKNSVKS VPVSAGGEGE TSPYSLEASP LGQLMNMLSH PVIRRSSLLT 3450
    EKLLRLLSLI SIALPENKVS EAQANSGSGA SSTTTATSTT STTTTTAAST 3500
    TPTPPTAPTP VTSAPALVAA TAISTIVVAA STTVTTPTTA TTTVSISPTT 3550
    KGSKSPAKVS DGGSSSTDFK MVSSGLTENQ LQLSVEVLTS HSCSEEGLED 3600
    AANVLLQLSR GDSGTRDTVL KLLLNGARHL GYTLCKQIGT LLAELREYNL 3650
    EQQRRAQCET LSPDGLPEEQ PQTTKLKGKM QSRFDMAENV VIVASQKRPL 3700
    GGRELQLPSM SMLTSKTSTQ KFFLRVLQVI IQLRDDTRRA NKKAKQTGRL 3750
    GSSGLGSASS IQAAVRQLEA EADAIIQMVR EGQRARRQQQ AATSESSQSE 3800
    ASVRREESPM DVDQPSPSAQ DTQSIASDGT PQGEKEKEER PPELPLLSEQ 3850
    LSLDELWDML GECLKELEES HDQHAVLVLQ PAVEAFFLVH ATERESKPPV 3900
    RDTRESQLAH IKDEPPPLSP APLTPATPSS LDPFFSREPS SMHISSSLPP 3950
    DTQKFLRFAE THRTVLNQIL RQSTTHLADG PFAVLVDYIR VLDFDVKRKY 4000
    FRQELERLDE GLRKEDMAVH VRRDHVFEDS YRELHRKSPE EMKNRLYIVF 4050
    EGEEGQDAGG LLREWYMIIS REMFNPMYAL FRTSPGDRVT YTINPSSHCN 4100
    PNHLSYFKFV GRIVAKAVYD NRLLECYFTR SFYKHILGKS VRYTDMESED 4150
    YHFYQGLVYL LENDVSTLGY DLTFSTEVQE FGVCEVRDLK PNGANILVTE 4200
    ENKKEYVHLV CQMRMTGAIR KQLAAFLEGF YEIIPKRLIS IFTEQELELL 4250
    ISGLPTIDID DLKSNTEYHK YQSNSIQIQW FWRALRSFDQ ADRAKFLQFV 4300
    TGTSKVPLQG FAALEGMNGI QKFQIHRDDR STDRLPSAHT CFNQLDLPAY 4350
    ESFEKLRHML LLAIQECSEG FGLA 4374
    Length:4,374
    Mass (Da):481,891
    Last modified:August 30, 2005 - v3
    Checksum:iFA9D3A7712F6393B
    GO
    Isoform 2 (identifier: Q7Z6Z7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         3016-3031: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:4,358
    Mass (Da):480,198
    Checksum:iD30775B19F710F6F
    GO
    Isoform 3 (identifier: Q7Z6Z7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         982-990: Missing.

    Show »
    Length:4,365
    Mass (Da):481,018
    Checksum:iE8A8FFC3C7EB9B24
    GO

    Sequence cautioni

    The sequence BAB13404.1 differs from that shown. Reason: Chimeric cDNA, contains the C-terminal part of ATP5I.
    The sequence AAF28950.1 differs from that shown. Reason: Frameshift at position 4356.
    The sequence BAC06833.1 differs from that shown. Reason: Frameshift at positions 982 and 1055.
    The sequence AAC62492.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAF28950.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1111 – 11111K → N in BAC06833. 1 PublicationCurated
    Sequence conflicti1124 – 11241P → L in AAV90838. (PubMed:15989956)Curated
    Sequence conflicti1124 – 11241P → L in BAC06833. 1 PublicationCurated
    Sequence conflicti1190 – 11901D → H in BAC06833. 1 PublicationCurated
    Sequence conflicti1962 – 19621Missing in BAA20771. (PubMed:9205841)Curated
    Sequence conflicti2525 – 25251H → Y in BAC06833. 1 PublicationCurated
    Sequence conflicti2525 – 25251H → Y in AAF28950. (PubMed:11042152)Curated
    Sequence conflicti4022 – 40221R → L in AAH02602. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti483 – 4831N → S.
    Corresponds to variant rs41307640 [ dbSNP | Ensembl ].
    VAR_061986
    Natural varianti2981 – 29811R → H in MRXS-Turner. 1 Publication
    VAR_045670
    Natural varianti4013 – 40131R → W in MRXS-Turner. 1 Publication
    VAR_045671
    Natural varianti4187 – 41871R → C in MRXS-Turner. 1 Publication
    VAR_045672

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei982 – 9909Missing in isoform 3. 1 PublicationVSP_015272
    Alternative sequencei3016 – 303116Missing in isoform 2. 1 PublicationVSP_011146Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY772009 mRNA. Translation: AAV90838.1.
    DQ097177 mRNA. Translation: AAY98258.1.
    AY929612 mRNA. Translation: AAX24125.1.
    AL592046, Z94044, Z97054 Genomic DNA. Translation: CAI39580.1.
    Z94044, AL592046, Z97054 Genomic DNA. Translation: CAI42354.1.
    Z97054, AL592046, Z94044 Genomic DNA. Translation: CAI42654.1.
    AB071605 mRNA. Translation: BAC06833.1. Frameshift.
    AB002310 mRNA. Translation: BAA20771.3.
    AB046798 mRNA. Translation: BAB13404.1. Sequence problems.
    AF161390 mRNA. Translation: AAF28950.1. Sequence problems.
    BC002602 mRNA. Translation: AAH02602.2.
    BC063505 mRNA. Translation: AAH63505.1.
    AF057569 mRNA. Translation: AAC62492.1. Different initiation.
    CR456813 mRNA. Translation: CAG33094.1.
    AL162050 mRNA. Translation: CAB82393.1.
    CCDSiCCDS35301.1. [Q7Z6Z7-1]
    PIRiT47165.
    RefSeqiNP_113584.3. NM_031407.6. [Q7Z6Z7-1]
    XP_005262022.1. XM_005261965.2. [Q7Z6Z7-1]
    XP_005262023.1. XM_005261966.2. [Q7Z6Z7-1]
    XP_005262024.1. XM_005261967.2. [Q7Z6Z7-1]
    UniGeneiHs.136905.

    Genome annotation databases

    EnsembliENST00000262854; ENSP00000262854; ENSG00000086758. [Q7Z6Z7-1]
    ENST00000342160; ENSP00000340648; ENSG00000086758. [Q7Z6Z7-1]
    GeneIDi10075.
    KEGGihsa:10075.
    UCSCiuc004dsn.4. human. [Q7Z6Z7-2]
    uc004dsp.4. human. [Q7Z6Z7-1]

    Polymorphism databases

    DMDMi73915353.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY772009 mRNA. Translation: AAV90838.1 .
    DQ097177 mRNA. Translation: AAY98258.1 .
    AY929612 mRNA. Translation: AAX24125.1 .
    AL592046 , Z94044 , Z97054 Genomic DNA. Translation: CAI39580.1 .
    Z94044 , AL592046 , Z97054 Genomic DNA. Translation: CAI42354.1 .
    Z97054 , AL592046 , Z94044 Genomic DNA. Translation: CAI42654.1 .
    AB071605 mRNA. Translation: BAC06833.1 . Frameshift.
    AB002310 mRNA. Translation: BAA20771.3 .
    AB046798 mRNA. Translation: BAB13404.1 . Sequence problems.
    AF161390 mRNA. Translation: AAF28950.1 . Sequence problems.
    BC002602 mRNA. Translation: AAH02602.2 .
    BC063505 mRNA. Translation: AAH63505.1 .
    AF057569 mRNA. Translation: AAC62492.1 . Different initiation.
    CR456813 mRNA. Translation: CAG33094.1 .
    AL162050 mRNA. Translation: CAB82393.1 .
    CCDSi CCDS35301.1. [Q7Z6Z7-1 ]
    PIRi T47165.
    RefSeqi NP_113584.3. NM_031407.6. [Q7Z6Z7-1 ]
    XP_005262022.1. XM_005261965.2. [Q7Z6Z7-1 ]
    XP_005262023.1. XM_005261966.2. [Q7Z6Z7-1 ]
    XP_005262024.1. XM_005261967.2. [Q7Z6Z7-1 ]
    UniGenei Hs.136905.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EKK NMR - A 1317-1356 [» ]
    3G1N X-ray 2.60 A/B 4005-4374 [» ]
    3H1D X-ray 1.89 A 3993-4374 [» ]
    ProteinModelPortali Q7Z6Z7.
    SMRi Q7Z6Z7. Positions 1310-1356, 4000-4366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115385. 70 interactions.
    DIPi DIP-34362N.
    IntActi Q7Z6Z7. 25 interactions.
    MINTi MINT-1576525.

    PTM databases

    PhosphoSitei Q7Z6Z7.

    Polymorphism databases

    DMDMi 73915353.

    Proteomic databases

    MaxQBi Q7Z6Z7.
    PaxDbi Q7Z6Z7.
    PRIDEi Q7Z6Z7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262854 ; ENSP00000262854 ; ENSG00000086758 . [Q7Z6Z7-1 ]
    ENST00000342160 ; ENSP00000340648 ; ENSG00000086758 . [Q7Z6Z7-1 ]
    GeneIDi 10075.
    KEGGi hsa:10075.
    UCSCi uc004dsn.4. human. [Q7Z6Z7-2 ]
    uc004dsp.4. human. [Q7Z6Z7-1 ]

    Organism-specific databases

    CTDi 10075.
    GeneCardsi GC0XM053575.
    HGNCi HGNC:30892. HUWE1.
    HPAi CAB022718.
    HPA002548.
    MIMi 300697. gene.
    300705. phenotype.
    300706. phenotype.
    neXtProti NX_Q7Z6Z7.
    Orphaneti 85328. intellectual disability, X-linked, Turner type.
    PharmGKBi PA128394567.
    HUGEi Search...
    Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5021.
    HOVERGENi HBG080254.
    KOi K10592.
    OMAi GMTQEVG.
    PhylomeDBi Q7Z6Z7.
    TreeFami TF323417.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi HUWE1. human.
    EvolutionaryTracei Q7Z6Z7.
    GeneWikii HUWE1.
    GenomeRNAii 10075.
    NextBioi 38085.
    PROi Q7Z6Z7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z6Z7.
    Bgeei Q7Z6Z7.
    Genevestigatori Q7Z6Z7.

    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

    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), FUNCTION, INTERACTION WITH CDKN2A, MUTAGENESIS OF CYS-4341.
    2. "Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis."
      Zhong Q., Gao W., Du F., Wang X.
      Cell 121:1085-1095(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF CYS-4341.
    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.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Homo sapiens LASU1 (large structure of UREB1) mRNA, complete cds."
      Miyazaki K., Okamoto Y., Sakamoto M., Kato C., Ozaki T., Watanabe K., Nakagawara A.
      Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 959-4374 (ISOFORM 3).
      Tissue: Brain.
    6. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1166-4374 (ISOFORM 2).
      Tissue: Brain.
    7. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 2310.
    8. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
      DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1246-2418.
      Tissue: Brain.
    9. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2451-4374.
      Tissue: Umbilical cord blood.
    10. "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 3953-4374.
      Tissue: Ovary and Placenta.
    11. Kim J.W., Lee Y., Hong Y.M., Hong M., Choe I.S.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4029-4374.
    12. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4067-4374.
    13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4320-4374.
      Tissue: Melanoma.
    14. "Over-expression of human UREB1 in colorectal cancer: HECT domain of human UREB1 inhibits the activity of tumor suppressor p53 protein."
      Yoon S.Y., Lee Y., Kim J.H., Chung A.-S., Joo J.H., Kim C.-N., Kim N.-S., Choe I.S., Kim J.W.
      Biochem. Biophys. Res. Commun. 326:7-17(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-4268 AND CYS-4341.
    15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1395; SER-1907; SER-2362; SER-2887 AND SER-2918, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Cdc6 stability is regulated by the Huwe1 ubiquitin ligase after DNA damage."
      Hall J.R., Kow E., Nevis K.R., Lu C.K., Luce K.S., Zhong Q., Cook J.G.
      Mol. Biol. Cell 18:3340-3350(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDC6.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    19. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    21. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "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, INTERACTION WITH MYCN, MUTAGENESIS OF CYS-4341.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1368; SER-1907; SER-2362; SER-2365; SER-2887; SER-3662; SER-3919; THR-3924 AND THR-3927, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH POLB.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1370; SER-1395; SER-1907; SER-2362; SER-2391; SER-2595; SER-2619; THR-2751; SER-2887; SER-3116; SER-3752; SER-3757; SER-3808; SER-3816; SER-3919 AND THR-3924, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    28. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1368; SER-1395; THR-1722; SER-1907; SER-2362; SER-2365; SER-2595; SER-3127; SER-3662; SER-3757; SER-3760 AND SER-3919, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1907; SER-2362 AND SER-2365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Solution structure of RSGI RUH-074, a human UBA domain."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1317-1356.
    32. "Hect domain of human huwe1/mule."
      Structural genomics consortium (SGC)
      Submitted (MAY-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 4005-4374.
    33. Cited for: VARIANTS MRXS-TURNER HIS-2981; TRP-4013 AND CYS-4187, INVOLVEMENT IN MRX17.

    Entry informationi

    Entry nameiHUWE1_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z6Z7
    Secondary accession number(s): O15029
    , Q4G2Z2, Q5H961, Q6P4D0, Q8NG67, Q9BUI0, Q9HCJ4, Q9NSL6, Q9P0A9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3