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UniProtKB - Q7Z6Z7 (HUWE1_HUMAN)

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Protein

E3 ubiquitin-protein ligase HUWE1

Gene

HUWE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Mediates polyubiquitination of isoform 2 of PA2G4.8 Publications

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei4341Glycyl thioester intermediate1

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: GO_Central
  • ubiquitin-protein transferase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  • base-excision repair Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • histone ubiquitination Source: UniProtKB
  • neutrophil degranulation Source: Reactome
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • protein monoubiquitination Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: GO_Central
Complete GO annotation...

Keywordsi

Molecular functionDNA-binding, Transferase
Biological processDifferentiation, DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase HUWE1 (EC:2.3.2.26)
Alternative name(s):
ARF-binding protein 1
Short name:
ARF-BP1
HECT, UBA and WWE domain-containing protein 1
HECT-type E3 ubiquitin transferase HUWE1
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:30892. HUWE1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: HPA
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • ficolin-1-rich granule lumen Source: Reactome
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • secretory granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked, syndromic, Turner type (MRXST)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by the association of mental retardation with macrocephaly and variable contractures.
See also OMIM:300706
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0456702981R → H in MRXST. 1 PublicationCorresponds to variant dbSNP:rs121918526Ensembl.1
Natural variantiVAR_0456714013R → W in MRXST. 1 PublicationCorresponds to variant dbSNP:rs121918525Ensembl.1
Natural variantiVAR_0456724187R → C in MRXST. 1 PublicationCorresponds to variant dbSNP:rs121918527Ensembl.1
Mental retardation, X-linked 17 (MRX17)1 Publication
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.
Disease descriptionA 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.
See also OMIM:300705

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4268Y → S: Loss of activity. 1 Publication1
Mutagenesisi4341C → A or D: Loss of activity. 4 Publications1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi10075.
MalaCardsiHUWE1.
MIMi300705. phenotype.
300706. phenotype.
OpenTargetsiENSG00000086758.
Orphaneti85328. X-linked intellectual disability, Turner type.
PharmGKBiPA128394567.

Polymorphism and mutation databases

BioMutaiHUWE1.
DMDMi73915353.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001203401 – 4374E3 ubiquitin-protein ligase HUWE1Add BLAST4374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei648PhosphoserineBy similarity1
Modified residuei649PhosphoserineBy similarity1
Modified residuei740PhosphoserineCombined sources1
Modified residuei1084PhosphoserineCombined sources1
Modified residuei1368PhosphoserineCombined sources1
Modified residuei1370PhosphoserineCombined sources1
Modified residuei1382PhosphoserineCombined sources1
Modified residuei1395PhosphoserineCombined sources1
Modified residuei1722PhosphothreonineCombined sources1
Modified residuei1907PhosphoserineCombined sources1
Modified residuei2035PhosphothreonineCombined sources1
Modified residuei2266PhosphoserineCombined sources1
Modified residuei2267N6-acetyllysineBy similarity1
Modified residuei2362PhosphoserineCombined sources1
Modified residuei2365PhosphoserineCombined sources1
Modified residuei2391PhosphoserineCombined sources1
Modified residuei2527PhosphoserineCombined sources1
Modified residuei2532PhosphoserineCombined sources1
Modified residuei2535PhosphoserineCombined sources1
Modified residuei2554PhosphothreonineCombined sources1
Modified residuei2584PhosphoserineCombined sources1
Modified residuei2595PhosphoserineCombined sources1
Modified residuei2619PhosphoserineCombined sources1
Modified residuei2751PhosphothreonineCombined sources1
Modified residuei2826PhosphoserineCombined sources1
Modified residuei2833PhosphoserineCombined sources1
Modified residuei2835PhosphoserineCombined sources1
Modified residuei2861PhosphoserineCombined sources1
Modified residuei2887PhosphoserineCombined sources1
Modified residuei2888PhosphoserineCombined sources1
Modified residuei2889PhosphothreonineCombined sources1
Modified residuei2918PhosphoserineCombined sources1
Modified residuei3116PhosphoserineCombined sources1
Modified residuei3117PhosphoserineCombined sources1
Modified residuei3122PhosphoserineCombined sources1
Modified residuei3127PhosphoserineCombined sources1
Modified residuei3135PhosphoserineCombined sources1
Modified residuei3149Omega-N-methylarginineBy similarity1
Modified residuei3555PhosphoserineCombined sources1
Modified residuei3662PhosphoserineCombined sources1
Modified residuei3752PhosphoserineCombined sources1
Modified residuei3757PhosphoserineCombined sources1
Modified residuei3759PhosphoserineCombined sources1
Modified residuei3760PhosphoserineCombined sources1
Modified residuei3808PhosphoserineCombined sources1
Modified residuei3816PhosphoserineCombined sources1
Modified residuei3827PhosphoserineCombined sources1
Modified residuei3830PhosphothreonineCombined sources1
Modified residuei3906PhosphoserineCombined sources1
Modified residuei3919PhosphoserineCombined sources1
Modified residuei3924PhosphothreonineCombined sources1
Modified residuei3927PhosphothreonineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ7Z6Z7.
MaxQBiQ7Z6Z7.
PaxDbiQ7Z6Z7.
PeptideAtlasiQ7Z6Z7.
PRIDEiQ7Z6Z7.

PTM databases

iPTMnetiQ7Z6Z7.
PhosphoSitePlusiQ7Z6Z7.

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

BgeeiENSG00000086758.
ExpressionAtlasiQ7Z6Z7. baseline and differential.
GenevisibleiQ7Z6Z7. HS.

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. Interacts with isoform 2 of PA2G4.5 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi115385. 469 interactors.
DIPiDIP-34362N.
IntActiQ7Z6Z7. 79 interactors.
MINTiMINT-1576525.
STRINGi9606.ENSP00000262854.

Structurei

Secondary structure

14374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1319 – 1329Combined sources11
Helixi1332 – 1341Combined sources10
Helixi1345 – 1353Combined sources9
Helixi1976 – 1991Combined sources16
Helixi2958 – 2960Combined sources3
Helixi2970 – 2975Combined sources6
Helixi2978 – 2988Combined sources11
Helixi3952 – 3972Combined sources21
Turni3977 – 3979Combined sources3
Helixi3983 – 3991Combined sources9
Helixi3994 – 4008Combined sources15
Turni4009 – 4011Combined sources3
Beta strandi4016 – 4021Combined sources6
Helixi4023 – 4025Combined sources3
Helixi4026 – 4034Combined sources9
Helixi4041 – 4043Combined sources3
Beta strandi4044 – 4050Combined sources7
Helixi4061 – 4072Combined sources12
Helixi4076 – 4078Combined sources3
Beta strandi4080 – 4083Combined sources4
Turni4085 – 4087Combined sources3
Beta strandi4088 – 4093Combined sources6
Helixi4095 – 4099Combined sources5
Helixi4103 – 4120Combined sources18
Helixi4130 – 4137Combined sources8
Helixi4143 – 4145Combined sources3
Helixi4146 – 4149Combined sources4
Helixi4151 – 4162Combined sources12
Helixi4165 – 4167Combined sources3
Beta strandi4168 – 4170Combined sources3
Beta strandi4172 – 4175Combined sources4
Turni4176 – 4178Combined sources3
Beta strandi4181 – 4183Combined sources3
Helixi4186 – 4189Combined sources4
Beta strandi4193 – 4197Combined sources5
Turni4200 – 4202Combined sources3
Helixi4203 – 4215Combined sources13
Helixi4217 – 4219Combined sources3
Helixi4220 – 4233Combined sources14
Helixi4236 – 4239Combined sources4
Helixi4244 – 4252Combined sources9
Helixi4259 – 4264Combined sources6
Beta strandi4266 – 4271Combined sources6
Helixi4276 – 4287Combined sources12
Helixi4290 – 4301Combined sources12
Beta strandi4302 – 4304Combined sources3
Helixi4311 – 4313Combined sources3
Beta strandi4317 – 4320Combined sources4
Beta strandi4323 – 4328Combined sources6
Beta strandi4337 – 4339Combined sources3
Helixi4340 – 4342Combined sources3
Beta strandi4344 – 4348Combined sources5
Helixi4353 – 4365Combined sources13
Beta strandi4370 – 4372Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EKKNMR-A1317-1356[»]
2MULNMR-A2951-3003[»]
3G1NX-ray2.60A/B4005-4374[»]
3H1DX-ray1.89A3993-4374[»]
5C6HX-ray2.05B/D/F/H/J/L/N/P/R/T/V/X1969-1994[»]
5LP8X-ray2.70A/B3951-4374[»]
ProteinModelPortaliQ7Z6Z7.
SMRiQ7Z6Z7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7Z6Z7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1316 – 1355UBAPROSITE-ProRule annotationAdd BLAST40
Domaini1370 – 1389UIMCuratedAdd BLAST20
Domaini1603 – 1680WWEPROSITE-ProRule annotationAdd BLAST78
Domaini4038 – 4374HECTPROSITE-ProRule annotationAdd BLAST337

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2295 – 2469Glu-richAdd BLAST175
Compositional biasi2427 – 2490Asp-richAdd BLAST64
Compositional biasi3483 – 3550Thr-richAdd BLAST68

Domaini

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

Sequence similaritiesi

Belongs to the UPL family. TOM1/PTR1 subfamily.Curated

Phylogenomic databases

eggNOGiKOG0939. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00850000132302.
HOVERGENiHBG080254.
InParanoidiQ7Z6Z7.
KOiK10592.
OMAiGDLYHWI.
OrthoDBiEOG091G01V1.
PhylomeDBiQ7Z6Z7.
TreeFamiTF323417.

Family and domain databases

CDDicd00078. HECTc. 1 hit.
Gene3Di1.25.10.10. 1 hit.
InterProiView protein in InterPro
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR025527. DUF4414.
IPR010309. E3_Ub_ligase_DUF908.
IPR010314. E3_Ub_ligase_DUF913.
IPR000569. HECT_dom.
IPR015940. UBA.
IPR009060. UBA-like.
IPR004170. WWE-dom.
PfamiView protein in Pfam
PF14377. DUF4414. 1 hit.
PF06012. DUF908. 1 hit.
PF06025. DUF913. 1 hit.
PF00632. HECT. 1 hit.
PF00627. UBA. 1 hit.
PF02825. WWE. 1 hit.
SMARTiView protein in SMART
SM00119. HECTc. 1 hit.
SM00165. UBA. 1 hit.
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF48371. SSF48371. 3 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiView protein in PROSITE
PS50237. HECT. 1 hit.
PS50030. UBA. 1 hit.
PS50918. WWE. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MKVDRTKLKK TPTEAPADCR ALIDKLKVCN DEQLLLELQQ IKTWNIGKCE 
        60         70         80         90        100
LYHWVDLLDR FDGILADAGQ TVENMSWMLV CDRPEREQLK MLLLAVLNFT 
       110        120        130        140        150
ALLIEYSFSR HLYSSIEHLT TLLASSDMQV VLAVLNLLYV FSKRSNYITR 
       160        170        180        190        200
LGSDKRTPLL TRLQHLAESW GGKENGFGLA ECCRDLHMMK YPPSATTLHF 
       210        220        230        240        250
EFYADPGAEV KIEKRTTSNT LHYIHIEQLD KISESPSEIM ESLTKMYSIP 
       260        270        280        290        300
KDKQMLLFTH IRLAHGFSNH RKRLQAVQAR LHAISILVYS NALQESANSI 
       310        320        330        340        350
LYNGLIEELV DVLQITDKQL MEIKAASLRT LTSIVHLERT PKLSSIIDCT 
       360        370        380        390        400
GTASYHGFLP VLVRNCIQAM IDPSMDPYPH QFATALFSFL YHLASYDAGG 
       410        420        430        440        450
EALVSCGMME ALLKVIKFLG DEQDQITFVT RAVRVVDLIT NLDMAAFQSH 
       460        470        480        490        500
SGLSIFIYRL EHEVDLCRKE CPFVIKPKIQ RPNTTQEGEE METDMDGVQC 
       510        520        530        540        550
IPQRAALLKS MLNFLKKAIQ DPAFSDGIRH VMDGSLPTSL KHIISNAEYY 
       560        570        580        590        600
GPSLFLLATE VVTVFVFQEP SLLSSLQDNG LTDVMLHALL IKDVPATREV 
       610        620        630        640        650
LGSLPNVFSA LCLNARGLQS FVQCQPFERL FKVLLSPDYL PAMRRRRSSD 
       660        670        680        690        700
PLGDTASNLG SAVDELMRHQ PTLKTDATTA IIKLLEEICN LGRDPKYICQ 
       710        720        730        740        750
KPSIQKADGT ATAPPPRSNH AAEEASSEDE EEEEVQAMQS FNSTQQNETE 
       760        770        780        790        800
PNQQVVGTEE RIPIPLMDYI LNVMKFVESI LSNNTTDDHC QEFVNQKGLL 
       810        820        830        840        850
PLVTILGLPN LPIDFPTSAA CQAVAGVCKS ILTLSHEPKV LQEGLLQLDS 
       860        870        880        890        900
ILSSLEPLHR PIESPGGSVL LRELACAGNV ADATLSAQAT PLLHALTAAH 
       910        920        930        940        950
AYIMMFVHTC RVGQSEIRSI SVNQWGSQLG LSVLSKLSQL YCSLVWESTV 
       960        970        980        990       1000
LLSLCTPNSL PSGCEFGQAD MQKLVPKDEK AGTTQGGKRS DGEQDGAAGS 
      1010       1020       1030       1040       1050
MDASTQGLLE GIGLDGDTLA PMETDEPTAS DSKGKSKITP AMAARIKQIK 
      1060       1070       1080       1090       1100
PLLSASSRLG RALAELFGLL VKLCVGSPVR QRRSHHAAST TTAPTPAARS 
      1110       1120       1130       1140       1150
TASALTKLLT KGLSWQPPPY TPTPRFRLTF FICSVGFTSP MLFDERKYPY 
      1160       1170       1180       1190       1200
HLMLQKFLCS GGHNALFETF NWALSMGGKV PVSEGLEHSD LPDGTGEFLD 
      1210       1220       1230       1240       1250
AWLMLVEKMV NPTTVLESPH SLPAKLPGGV QNFPQFSALR FLVVTQKAAF 
      1260       1270       1280       1290       1300
TCIKNLWNRK PLKVYGGRMA ESMLAILCHI LRGEPVIRER LSKEKEGSRG 
      1310       1320       1330       1340       1350
EEDTGQEEGG SRREPQVNQQ QLQQLMDMGF TREHAMEALL NTSTMEQATE 
      1360       1370       1380       1390       1400
YLLTHPPPIM GGVVRDLSMS EEDQMMRAIA MSLGQDIPMD QRAESPEEVA 
      1410       1420       1430       1440       1450
CRKEEEERKA REKQEEEEAK CLEKFQDADP LEQDELHTFT DTMLPGCFHL 
      1460       1470       1480       1490       1500
LDELPDTVYR VCDLIMTAIK RNGADYRDMI LKQVVNQVWE AADVLIKAAL 
      1510       1520       1530       1540       1550
PLTTSDTKTV SEWISQMATL PQASNLATRI LLLTLLFEEL KLPCAWVVES 
      1560       1570       1580       1590       1600
SGILNVLIKL LEVVQPCLQA AKEQKEVQTP KWITPVLLLI DFYEKTAISS 
      1610       1620       1630       1640       1650
KRRAQMTKYL QSNSNNWRWF DDRSGRWCSY SASNNSTIDS AWKSGETSVR 
      1660       1670       1680       1690       1700
FTAGRRRYTV QFTTMVQVNE ETGNRRPVML TLLRVPRLNK NSKNSNGQEL 
      1710       1720       1730       1740       1750
EKTLEESKEM DIKRKENKGN DTPLALESTN TEKETSLEET KIGEILIQGL 
      1760       1770       1780       1790       1800
TEDMVTVLIR ACVSMLGVPV DPDTLHATLR LCLRLTRDHK YAMMFAELKS 
      1810       1820       1830       1840       1850
TRMILNLTQS SGFNGFTPLV TLLLRHIIED PCTLRHTMEK VVRSAATSGA 
      1860       1870       1880       1890       1900
GSTTSGVVSG SLGSREINYI LRVLGPAACR NPDIFTEVAN CCIRIALPAP 
      1910       1920       1930       1940       1950
RGSGTASDDE FENLRIKGPN AVQLVKTTPL KPSPLPVIPD TIKEVIYDML 
      1960       1970       1980       1990       2000
NALAAYHAPE EADKSDPKPG VMTQEVGQLL QDMGDDVYQQ YRSLTRQSSD 
      2010       2020       2030       2040       2050
FDTQSGFSIN SQVFAADGAS TETSASGTSQ GEASTPEESR DGKKDKEGDR 
      2060       2070       2080       2090       2100
ASEEGKQKGK GSKPLMPTST ILRLLAELVR SYVGIATLIA NYSYTVGQSE 
      2110       2120       2130       2140       2150
LIKEDCSVLA FVLDHLLPHT QNAEDKDTPA LARLFLASLA AAGSGTDAQV 
      2160       2170       2180       2190       2200
ALVNEVKAAL GRALAMAEST EKHARLQAVM CIISTIMESC PSTSSFYSSA 
      2210       2220       2230       2240       2250
TAKTQHNGMN NIIRLFLKKG LVNDLARVPH SLDLSSPNMA NTVNAALKPL 
      2260       2270       2280       2290       2300
ETLSRIVNQP SSLFGSKSAS SKNKSEQDAQ GASQDSSSNQ QDPGEPGEAE 
      2310       2320       2330       2340       2350
VQEEDHDVTQ TEVADGDIMD GEAETDSVVI AGQPEVLSSQ EMQVENELED 
      2360       2370       2380       2390       2400
LIDELLERDG GSGNSTIIVS RSGEDESQED VLMDEAPSNL SQASTLQANR 
      2410       2420       2430       2440       2450
EDSMNILDPE DEEEHTQEED SSGSNEDEDD SQDEEEEEEE DEEDDQEDDE 
      2460       2470       2480       2490       2500
GEEGDEDDDD DGSEMELDED YPDMNASPLV RFERFDREDD LIIEFDNMFS 
      2510       2520       2530       2540       2550
SATDIPPSPG NIPTTHPLMV RHADHSSLTL GSGSSTTRLT QGIGRSQRTL 
      2560       2570       2580       2590       2600
RQLTANTGHT IHVHYPGNRQ PNPPLILQRL LGPSAAADIL QLSSSLPLQS 
      2610       2620       2630       2640       2650
RGRARLLVGN DDVHIIARSD DELLDDFFHD QSTATSQAGT LSSIPTALTR 
      2660       2670       2680       2690       2700
WTEECKVLDA ESMHDCVSVV KVSIVNHLEF LRDEELEERR EKRRKQLAEE 
      2710       2720       2730       2740       2750
ETKITDKGKE DKENRDQSAQ CTASKSNDST EQNLSDGTPM PDSYPTTPSS 
      2760       2770       2780       2790       2800
TDAATSESKE TLGTLQSSQQ QPTLPTPPAL GEVPQELQSP AGEGGSSTQL 
      2810       2820       2830       2840       2850
LMPVEPEELG PTRPSGEAET TQMELSPAPT ITSLSPERAE DSDALTAVSS 
      2860       2870       2880       2890       2900
QLEGSPMDTS SLASCTLEEA VGDTSAAGSS EQPRAGSSTP GDAPPAVAEV 
      2910       2920       2930       2940       2950
QGRSDGSGES AQPPEDSSPP ASSESSSTRD SAVAISGADS RGILEEPLPS 
      2960       2970       2980       2990       3000
TSSEEEDPLA GISLPEGVDP SFLAALPDDI RREVLQNQLG IRPPTRTAPS 
      3010       3020       3030       3040       3050
TNSSAPAVVG NPGVTEVSPE FLAALPPAIQ EEVLAQQRAE QQRRELAQNA 
      3060       3070       3080       3090       3100
SSDTPMDPVT FIQTLPSDLR RSVLEDMEDS VLAVMPPDIA AEAQALRREQ 
      3110       3120       3130       3140       3150
EARQRQLMHE RLFGHSSTSA LSAILRSPAF TSRLSGNRGV QYTRLAVQRG 
      3160       3170       3180       3190       3200
GTFQMGGSSS HNRPSGSNVD TLLRLRGRLL LDHEALSCLL VLLFVDEPKL 
      3210       3220       3230       3240       3250
NTSRLHRVLR NLCYHAQTRH WVIRSLLSIL QRSSESELCI ETPKLTTSEE 
      3260       3270       3280       3290       3300
KGKKSSKSCG SSSHENRPLD LLHKMESKSS NQLSWLSVSM DAALGCRTNI 
      3310       3320       3330       3340       3350
FQIQRSGGRK HTEKHASGGS TVHIHPQAAP VVCRHVLDTL IQLAKVFPSH 
      3360       3370       3380       3390       3400
FTQQRTKETN CESDRERGNK ACSPCSSQSS SSGICTDFWD LLVKLDNMNV 
      3410       3420       3430       3440       3450
SRKGKNSVKS VPVSAGGEGE TSPYSLEASP LGQLMNMLSH PVIRRSSLLT 
      3460       3470       3480       3490       3500
EKLLRLLSLI SIALPENKVS EAQANSGSGA SSTTTATSTT STTTTTAAST 
      3510       3520       3530       3540       3550
TPTPPTAPTP VTSAPALVAA TAISTIVVAA STTVTTPTTA TTTVSISPTT 
      3560       3570       3580       3590       3600
KGSKSPAKVS DGGSSSTDFK MVSSGLTENQ LQLSVEVLTS HSCSEEGLED 
      3610       3620       3630       3640       3650
AANVLLQLSR GDSGTRDTVL KLLLNGARHL GYTLCKQIGT LLAELREYNL 
      3660       3670       3680       3690       3700
EQQRRAQCET LSPDGLPEEQ PQTTKLKGKM QSRFDMAENV VIVASQKRPL 
      3710       3720       3730       3740       3750
GGRELQLPSM SMLTSKTSTQ KFFLRVLQVI IQLRDDTRRA NKKAKQTGRL 
      3760       3770       3780       3790       3800
GSSGLGSASS IQAAVRQLEA EADAIIQMVR EGQRARRQQQ AATSESSQSE 
      3810       3820       3830       3840       3850
ASVRREESPM DVDQPSPSAQ DTQSIASDGT PQGEKEKEER PPELPLLSEQ 
      3860       3870       3880       3890       3900
LSLDELWDML GECLKELEES HDQHAVLVLQ PAVEAFFLVH ATERESKPPV 
      3910       3920       3930       3940       3950
RDTRESQLAH IKDEPPPLSP APLTPATPSS LDPFFSREPS SMHISSSLPP 
      3960       3970       3980       3990       4000
DTQKFLRFAE THRTVLNQIL RQSTTHLADG PFAVLVDYIR VLDFDVKRKY 
      4010       4020       4030       4040       4050
FRQELERLDE GLRKEDMAVH VRRDHVFEDS YRELHRKSPE EMKNRLYIVF 
      4060       4070       4080       4090       4100
EGEEGQDAGG LLREWYMIIS REMFNPMYAL FRTSPGDRVT YTINPSSHCN 
      4110       4120       4130       4140       4150
PNHLSYFKFV GRIVAKAVYD NRLLECYFTR SFYKHILGKS VRYTDMESED 
      4160       4170       4180       4190       4200
YHFYQGLVYL LENDVSTLGY DLTFSTEVQE FGVCEVRDLK PNGANILVTE 
      4210       4220       4230       4240       4250
ENKKEYVHLV CQMRMTGAIR KQLAAFLEGF YEIIPKRLIS IFTEQELELL 
      4260       4270       4280       4290       4300
ISGLPTIDID DLKSNTEYHK YQSNSIQIQW FWRALRSFDQ ADRAKFLQFV 
      4310       4320       4330       4340       4350
TGTSKVPLQG FAALEGMNGI QKFQIHRDDR STDRLPSAHT CFNQLDLPAY 
      4360       4370 
ESFEKLRHML LLAIQECSEG FGLA
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 AAC62492 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF28950 differs from that shown. Reason: Frameshift at position 4356.Curated
The sequence AAF28950 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB13404 differs from that shown. Chimeric cDNA, contains the C-terminal part of ATP5I.Curated
The sequence BAC06833 differs from that shown. Reason: Frameshift at positions 982 and 1055.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1111K → N in BAC06833 (Ref. 5) Curated1
Sequence conflicti1124P → L in AAV90838 (PubMed:15989956).Curated1
Sequence conflicti1124P → L in BAC06833 (Ref. 5) Curated1
Sequence conflicti1190D → H in BAC06833 (Ref. 5) Curated1
Sequence conflicti1962Missing in BAA20771 (PubMed:9205841).Curated1
Sequence conflicti2525H → Y in BAC06833 (Ref. 5) Curated1
Sequence conflicti2525H → Y in AAF28950 (PubMed:11042152).Curated1
Sequence conflicti4022R → L in AAH02602 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_061986483N → S. Corresponds to variant dbSNP:rs41307640Ensembl.1
Natural variantiVAR_076253950V → D Found in patients with autism spectrum disorders; unknown pathological significance. 1 Publication1
Natural variantiVAR_0456702981R → H in MRXST. 1 PublicationCorresponds to variant dbSNP:rs121918526Ensembl.1
Natural variantiVAR_0456714013R → W in MRXST. 1 PublicationCorresponds to variant dbSNP:rs121918525Ensembl.1
Natural variantiVAR_0456724187R → C in MRXST. 1 PublicationCorresponds to variant dbSNP:rs121918527Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_015272982 – 990Missing in isoform 3. 1 Publication9
Alternative sequenceiVSP_0111463016 – 3031Missing in isoform 2. 1 PublicationAdd BLAST16

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005261965.3. [Q7Z6Z7-1]
UniGeneiHs.136905.

Genome annotation databases

EnsembliENST00000262854; ENSP00000262854; ENSG00000086758. [Q7Z6Z7-1]
ENST00000342160; ENSP00000340648; ENSG00000086758. [Q7Z6Z7-1]
ENST00000612484; ENSP00000479451; ENSG00000086758. [Q7Z6Z7-3]
GeneIDi10075.
KEGGihsa:10075.
UCSCiuc033eew.2. human. [Q7Z6Z7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiHUWE1_HUMAN
AccessioniPrimary (citable) accession number: Q7Z6Z7
Secondary accession number(s): O15029
, Q4G2Z2, Q5H961, Q6P4D0, Q8NG67, Q9BUI0, Q9HCJ4, Q9NSL6, Q9P0A9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: August 30, 2005
Last modified: July 5, 2017
This is version 159 of the entry and version 3 of the sequence. See 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