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Q7Z6Z7

- HUWE1_HUMAN

UniProt

Q7Z6Z7 - HUWE1_HUMAN

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Protein
E3 ubiquitin-protein ligase HUWE1
Gene
HUWE1, KIAA0312, KIAA1578, UREB1, HSPC272
Organism
Homo sapiens (Human)
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. 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
Complete GO annotation...

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_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. Nucleus
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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. nucleus Source: UniProtKB
Complete GO annotation...

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.
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.1 Publication

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 HUWE1
PRO_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-acetyllysine By 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. 68 interactions.
DIPiDIP-34362N.
IntActiQ7Z6Z7. 25 interactions.
MINTiMINT-1576525.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ7Z6Z7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1316 – 135540UBA
Add
BLAST
Repeati1370 – 138920UIM
Add
BLAST
Domaini1603 – 168078WWE
Add
BLAST
Domaini4038 – 4374337HECT
Add
BLAST

Compositional bias

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

Domaini

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

Sequence similaritiesi

Contains 1 UBA domain.
Contains 1 WWE domain.

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.

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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.

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.
VSP_015272
Alternative sequencei3016 – 303116Missing in isoform 2.
VSP_011146Add
BLAST

Sequence conflict

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

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...

Protein-protein interaction databases

BioGridi 115385. 68 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

« 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), 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: September 3, 2014
This is version 126 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

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