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Q7Z6Z7 (HUWE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:HUWE1
Synonyms:KIAA0312, KIAA1578, UREB1
ORF Names:HSPC272
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4374 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.3 Ref.14 Ref.17 Ref.22 Ref.25

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with isoform p14ARFof CDKN2A which strongly inhibits HUWE1 ubiquitin ligase activity. Interacts with MYCN, POLB and CDC6. Ref.1 Ref.17 Ref.22 Ref.25

Subcellular location

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. Ref.25

Tissue specificity

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. Ref.14

Domain

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

Post-translational modification

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

Involvement in disease

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. Ref.33

Sequence similarities

Belongs to the UPL family. TOM1/PTR1 subfamily.

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.

Contains 1 UBA domain.

Contains 1 UIM (ubiquitin-interacting motif) repeat.

Contains 1 WWE domain.

Sequence caution

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.

The sequence AAF28950.1 differs from that shown. Reason: Frameshift at position 4356.

The sequence BAB13404.1 differs from that shown. Reason: Chimeric cDNA, contains the C-terminal part of ATP5I.

The sequence BAC06833.1 differs from that shown. Reason: Frameshift at positions 982 and 1055.

Ontologies

Keywords
   Biological processDifferentiation
DNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Mental retardation
   LigandDNA-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbase-excision repair

Inferred from mutant phenotype Ref.25. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

histone ubiquitination

Inferred from direct assay Ref.3. Source: UniProtKB

protein monoubiquitination

Inferred from direct assay Ref.25. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay Ref.2. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.25. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.2Ref.25. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z6Z7-1)

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.
Isoform 2 (identifier: Q7Z6Z7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     3016-3031: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q7Z6Z7-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 43744374E3 ubiquitin-protein ligase HUWE1
PRO_0000120340

Regions

Domain1316 – 135540UBA
Repeat1370 – 138920UIM
Domain1603 – 168078WWE
Domain4038 – 4374337HECT
Compositional bias2295 – 2469175Glu-rich
Compositional bias2427 – 249064Asp-rich
Compositional bias3483 – 355068Thr-rich

Sites

Active site43411Glycyl thioester intermediate

Amino acid modifications

Modified residue10841Phosphoserine Ref.19 Ref.28 Ref.30
Modified residue13681Phosphoserine Ref.23 Ref.28
Modified residue13701Phosphoserine Ref.27
Modified residue13951Phosphoserine Ref.16 Ref.27 Ref.28
Modified residue17221Phosphothreonine Ref.28
Modified residue19071Phosphoserine Ref.16 Ref.23 Ref.27 Ref.28 Ref.30
Modified residue22671N6-acetyllysine By similarity
Modified residue23621Phosphoserine Ref.15 Ref.16 Ref.21 Ref.23 Ref.27 Ref.28 Ref.30
Modified residue23651Phosphoserine Ref.23 Ref.28 Ref.30
Modified residue23911Phosphoserine Ref.27
Modified residue25951Phosphoserine Ref.27 Ref.28
Modified residue26191Phosphoserine Ref.27
Modified residue27511Phosphothreonine Ref.27
Modified residue28871Phosphoserine Ref.16 Ref.23 Ref.27
Modified residue29181Phosphoserine Ref.16
Modified residue31161Phosphoserine Ref.27
Modified residue31271Phosphoserine Ref.28
Modified residue36621Phosphoserine Ref.23 Ref.28
Modified residue37521Phosphoserine Ref.27
Modified residue37571Phosphoserine Ref.27 Ref.28
Modified residue37601Phosphoserine Ref.28
Modified residue38081Phosphoserine Ref.27
Modified residue38161Phosphoserine Ref.27
Modified residue39191Phosphoserine Ref.23 Ref.27 Ref.28
Modified residue39241Phosphothreonine Ref.23 Ref.27
Modified residue39271Phosphothreonine Ref.23

Natural variations

Alternative sequence982 – 9909Missing in isoform 3.
VSP_015272
Alternative sequence3016 – 303116Missing in isoform 2.
VSP_011146
Natural variant4831N → S.
Corresponds to variant rs41307640 [ dbSNP | Ensembl ].
VAR_061986
Natural variant29811R → H in MRXS-Turner. Ref.33
VAR_045670
Natural variant40131R → W in MRXS-Turner. Ref.33
VAR_045671
Natural variant41871R → C in MRXS-Turner. Ref.33
VAR_045672

Experimental info

Mutagenesis42681Y → S: Loss of activity. Ref.14
Mutagenesis43411C → A or D: Loss of activity. Ref.1 Ref.2 Ref.14 Ref.22
Sequence conflict11111K → N in BAC06833. Ref.5
Sequence conflict11241P → L in AAV90838. Ref.1
Sequence conflict11241P → L in BAC06833. Ref.5
Sequence conflict11901D → H in BAC06833. Ref.5
Sequence conflict19621Missing in BAA20771. Ref.6
Sequence conflict25251H → Y in BAC06833. Ref.5
Sequence conflict25251H → Y in AAF28950. Ref.9
Sequence conflict40221R → L in AAH02602. Ref.10

Secondary structure

.................................................................................. 4374
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LASU1) (Large structure of UREB1) [UniParc].

Last modified August 30, 2005. Version 3.
Checksum: FA9D3A7712F6393B

FASTA4,374481,891
        10         20         30         40         50         60 
MKVDRTKLKK TPTEAPADCR ALIDKLKVCN DEQLLLELQQ IKTWNIGKCE LYHWVDLLDR 

        70         80         90        100        110        120 
FDGILADAGQ TVENMSWMLV CDRPEREQLK MLLLAVLNFT ALLIEYSFSR HLYSSIEHLT 

       130        140        150        160        170        180 
TLLASSDMQV VLAVLNLLYV FSKRSNYITR LGSDKRTPLL TRLQHLAESW GGKENGFGLA 

       190        200        210        220        230        240 
ECCRDLHMMK YPPSATTLHF EFYADPGAEV KIEKRTTSNT LHYIHIEQLD KISESPSEIM 

       250        260        270        280        290        300 
ESLTKMYSIP KDKQMLLFTH IRLAHGFSNH RKRLQAVQAR LHAISILVYS NALQESANSI 

       310        320        330        340        350        360 
LYNGLIEELV DVLQITDKQL MEIKAASLRT LTSIVHLERT PKLSSIIDCT GTASYHGFLP 

       370        380        390        400        410        420 
VLVRNCIQAM IDPSMDPYPH QFATALFSFL YHLASYDAGG EALVSCGMME ALLKVIKFLG 

       430        440        450        460        470        480 
DEQDQITFVT RAVRVVDLIT NLDMAAFQSH SGLSIFIYRL EHEVDLCRKE CPFVIKPKIQ 

       490        500        510        520        530        540 
RPNTTQEGEE METDMDGVQC IPQRAALLKS MLNFLKKAIQ DPAFSDGIRH VMDGSLPTSL 

       550        560        570        580        590        600 
KHIISNAEYY GPSLFLLATE VVTVFVFQEP SLLSSLQDNG LTDVMLHALL IKDVPATREV 

       610        620        630        640        650        660 
LGSLPNVFSA LCLNARGLQS FVQCQPFERL FKVLLSPDYL PAMRRRRSSD PLGDTASNLG 

       670        680        690        700        710        720 
SAVDELMRHQ PTLKTDATTA IIKLLEEICN LGRDPKYICQ KPSIQKADGT ATAPPPRSNH 

       730        740        750        760        770        780 
AAEEASSEDE EEEEVQAMQS FNSTQQNETE PNQQVVGTEE RIPIPLMDYI LNVMKFVESI 

       790        800        810        820        830        840 
LSNNTTDDHC QEFVNQKGLL PLVTILGLPN LPIDFPTSAA CQAVAGVCKS ILTLSHEPKV 

       850        860        870        880        890        900 
LQEGLLQLDS ILSSLEPLHR PIESPGGSVL LRELACAGNV ADATLSAQAT PLLHALTAAH 

       910        920        930        940        950        960 
AYIMMFVHTC RVGQSEIRSI SVNQWGSQLG LSVLSKLSQL YCSLVWESTV LLSLCTPNSL 

       970        980        990       1000       1010       1020 
PSGCEFGQAD MQKLVPKDEK AGTTQGGKRS DGEQDGAAGS MDASTQGLLE GIGLDGDTLA 

      1030       1040       1050       1060       1070       1080 
PMETDEPTAS DSKGKSKITP AMAARIKQIK PLLSASSRLG RALAELFGLL VKLCVGSPVR 

      1090       1100       1110       1120       1130       1140 
QRRSHHAAST TTAPTPAARS TASALTKLLT KGLSWQPPPY TPTPRFRLTF FICSVGFTSP 

      1150       1160       1170       1180       1190       1200 
MLFDERKYPY HLMLQKFLCS GGHNALFETF NWALSMGGKV PVSEGLEHSD LPDGTGEFLD 

      1210       1220       1230       1240       1250       1260 
AWLMLVEKMV NPTTVLESPH SLPAKLPGGV QNFPQFSALR FLVVTQKAAF TCIKNLWNRK 

      1270       1280       1290       1300       1310       1320 
PLKVYGGRMA ESMLAILCHI LRGEPVIRER LSKEKEGSRG EEDTGQEEGG SRREPQVNQQ 

      1330       1340       1350       1360       1370       1380 
QLQQLMDMGF TREHAMEALL NTSTMEQATE YLLTHPPPIM GGVVRDLSMS EEDQMMRAIA 

      1390       1400       1410       1420       1430       1440 
MSLGQDIPMD QRAESPEEVA CRKEEEERKA REKQEEEEAK CLEKFQDADP LEQDELHTFT 

      1450       1460       1470       1480       1490       1500 
DTMLPGCFHL LDELPDTVYR VCDLIMTAIK RNGADYRDMI LKQVVNQVWE AADVLIKAAL 

      1510       1520       1530       1540       1550       1560 
PLTTSDTKTV SEWISQMATL PQASNLATRI LLLTLLFEEL KLPCAWVVES SGILNVLIKL 

      1570       1580       1590       1600       1610       1620 
LEVVQPCLQA AKEQKEVQTP KWITPVLLLI DFYEKTAISS KRRAQMTKYL QSNSNNWRWF 

      1630       1640       1650       1660       1670       1680 
DDRSGRWCSY SASNNSTIDS AWKSGETSVR FTAGRRRYTV QFTTMVQVNE ETGNRRPVML 

      1690       1700       1710       1720       1730       1740 
TLLRVPRLNK NSKNSNGQEL EKTLEESKEM DIKRKENKGN DTPLALESTN TEKETSLEET 

      1750       1760       1770       1780       1790       1800 
KIGEILIQGL TEDMVTVLIR ACVSMLGVPV DPDTLHATLR LCLRLTRDHK YAMMFAELKS 

      1810       1820       1830       1840       1850       1860 
TRMILNLTQS SGFNGFTPLV TLLLRHIIED PCTLRHTMEK VVRSAATSGA GSTTSGVVSG 

      1870       1880       1890       1900       1910       1920 
SLGSREINYI LRVLGPAACR NPDIFTEVAN CCIRIALPAP RGSGTASDDE FENLRIKGPN 

      1930       1940       1950       1960       1970       1980 
AVQLVKTTPL KPSPLPVIPD TIKEVIYDML NALAAYHAPE EADKSDPKPG VMTQEVGQLL 

      1990       2000       2010       2020       2030       2040 
QDMGDDVYQQ YRSLTRQSSD FDTQSGFSIN SQVFAADGAS TETSASGTSQ GEASTPEESR 

      2050       2060       2070       2080       2090       2100 
DGKKDKEGDR ASEEGKQKGK GSKPLMPTST ILRLLAELVR SYVGIATLIA NYSYTVGQSE 

      2110       2120       2130       2140       2150       2160 
LIKEDCSVLA FVLDHLLPHT QNAEDKDTPA LARLFLASLA AAGSGTDAQV ALVNEVKAAL 

      2170       2180       2190       2200       2210       2220 
GRALAMAEST EKHARLQAVM CIISTIMESC PSTSSFYSSA TAKTQHNGMN NIIRLFLKKG 

      2230       2240       2250       2260       2270       2280 
LVNDLARVPH SLDLSSPNMA NTVNAALKPL ETLSRIVNQP SSLFGSKSAS SKNKSEQDAQ 

      2290       2300       2310       2320       2330       2340 
GASQDSSSNQ QDPGEPGEAE VQEEDHDVTQ TEVADGDIMD GEAETDSVVI AGQPEVLSSQ 

      2350       2360       2370       2380       2390       2400 
EMQVENELED LIDELLERDG GSGNSTIIVS RSGEDESQED VLMDEAPSNL SQASTLQANR 

      2410       2420       2430       2440       2450       2460 
EDSMNILDPE DEEEHTQEED SSGSNEDEDD SQDEEEEEEE DEEDDQEDDE GEEGDEDDDD 

      2470       2480       2490       2500       2510       2520 
DGSEMELDED YPDMNASPLV RFERFDREDD LIIEFDNMFS SATDIPPSPG NIPTTHPLMV 

      2530       2540       2550       2560       2570       2580 
RHADHSSLTL GSGSSTTRLT QGIGRSQRTL RQLTANTGHT IHVHYPGNRQ PNPPLILQRL 

      2590       2600       2610       2620       2630       2640 
LGPSAAADIL QLSSSLPLQS RGRARLLVGN DDVHIIARSD DELLDDFFHD QSTATSQAGT 

      2650       2660       2670       2680       2690       2700 
LSSIPTALTR WTEECKVLDA ESMHDCVSVV KVSIVNHLEF LRDEELEERR EKRRKQLAEE 

      2710       2720       2730       2740       2750       2760 
ETKITDKGKE DKENRDQSAQ CTASKSNDST EQNLSDGTPM PDSYPTTPSS TDAATSESKE 

      2770       2780       2790       2800       2810       2820 
TLGTLQSSQQ QPTLPTPPAL GEVPQELQSP AGEGGSSTQL LMPVEPEELG PTRPSGEAET 

      2830       2840       2850       2860       2870       2880 
TQMELSPAPT ITSLSPERAE DSDALTAVSS QLEGSPMDTS SLASCTLEEA VGDTSAAGSS 

      2890       2900       2910       2920       2930       2940 
EQPRAGSSTP GDAPPAVAEV QGRSDGSGES AQPPEDSSPP ASSESSSTRD SAVAISGADS 

      2950       2960       2970       2980       2990       3000 
RGILEEPLPS TSSEEEDPLA GISLPEGVDP SFLAALPDDI RREVLQNQLG IRPPTRTAPS 

      3010       3020       3030       3040       3050       3060 
TNSSAPAVVG NPGVTEVSPE FLAALPPAIQ EEVLAQQRAE QQRRELAQNA SSDTPMDPVT 

      3070       3080       3090       3100       3110       3120 
FIQTLPSDLR RSVLEDMEDS VLAVMPPDIA AEAQALRREQ EARQRQLMHE RLFGHSSTSA 

      3130       3140       3150       3160       3170       3180 
LSAILRSPAF TSRLSGNRGV QYTRLAVQRG GTFQMGGSSS HNRPSGSNVD TLLRLRGRLL 

      3190       3200       3210       3220       3230       3240 
LDHEALSCLL VLLFVDEPKL NTSRLHRVLR NLCYHAQTRH WVIRSLLSIL QRSSESELCI 

      3250       3260       3270       3280       3290       3300 
ETPKLTTSEE KGKKSSKSCG SSSHENRPLD LLHKMESKSS NQLSWLSVSM DAALGCRTNI 

      3310       3320       3330       3340       3350       3360 
FQIQRSGGRK HTEKHASGGS TVHIHPQAAP VVCRHVLDTL IQLAKVFPSH FTQQRTKETN 

      3370       3380       3390       3400       3410       3420 
CESDRERGNK ACSPCSSQSS SSGICTDFWD LLVKLDNMNV SRKGKNSVKS VPVSAGGEGE 

      3430       3440       3450       3460       3470       3480 
TSPYSLEASP LGQLMNMLSH PVIRRSSLLT EKLLRLLSLI SIALPENKVS EAQANSGSGA 

      3490       3500       3510       3520       3530       3540 
SSTTTATSTT STTTTTAAST TPTPPTAPTP VTSAPALVAA TAISTIVVAA STTVTTPTTA 

      3550       3560       3570       3580       3590       3600 
TTTVSISPTT KGSKSPAKVS DGGSSSTDFK MVSSGLTENQ LQLSVEVLTS HSCSEEGLED 

      3610       3620       3630       3640       3650       3660 
AANVLLQLSR GDSGTRDTVL KLLLNGARHL GYTLCKQIGT LLAELREYNL EQQRRAQCET 

      3670       3680       3690       3700       3710       3720 
LSPDGLPEEQ PQTTKLKGKM QSRFDMAENV VIVASQKRPL GGRELQLPSM SMLTSKTSTQ 

      3730       3740       3750       3760       3770       3780 
KFFLRVLQVI IQLRDDTRRA NKKAKQTGRL GSSGLGSASS IQAAVRQLEA EADAIIQMVR 

      3790       3800       3810       3820       3830       3840 
EGQRARRQQQ AATSESSQSE ASVRREESPM DVDQPSPSAQ DTQSIASDGT PQGEKEKEER 

      3850       3860       3870       3880       3890       3900 
PPELPLLSEQ LSLDELWDML GECLKELEES HDQHAVLVLQ PAVEAFFLVH ATERESKPPV 

      3910       3920       3930       3940       3950       3960 
RDTRESQLAH IKDEPPPLSP APLTPATPSS LDPFFSREPS SMHISSSLPP DTQKFLRFAE 

      3970       3980       3990       4000       4010       4020 
THRTVLNQIL RQSTTHLADG PFAVLVDYIR VLDFDVKRKY FRQELERLDE GLRKEDMAVH 

      4030       4040       4050       4060       4070       4080 
VRRDHVFEDS YRELHRKSPE EMKNRLYIVF EGEEGQDAGG LLREWYMIIS REMFNPMYAL 

      4090       4100       4110       4120       4130       4140 
FRTSPGDRVT YTINPSSHCN PNHLSYFKFV GRIVAKAVYD NRLLECYFTR SFYKHILGKS 

      4150       4160       4170       4180       4190       4200 
VRYTDMESED YHFYQGLVYL LENDVSTLGY DLTFSTEVQE FGVCEVRDLK PNGANILVTE 

      4210       4220       4230       4240       4250       4260 
ENKKEYVHLV CQMRMTGAIR KQLAAFLEGF YEIIPKRLIS IFTEQELELL ISGLPTIDID 

      4270       4280       4290       4300       4310       4320 
DLKSNTEYHK YQSNSIQIQW FWRALRSFDQ ADRAKFLQFV TGTSKVPLQG FAALEGMNGI 

      4330       4340       4350       4360       4370 
QKFQIHRDDR STDRLPSAHT CFNQLDLPAY ESFEKLRHML LLAIQECSEG FGLA 

« Hide

Isoform 2 [UniParc].

Checksum: D30775B19F710F6F
Show »

FASTA4,358480,198
Isoform 3 [UniParc].

Checksum: E8A8FFC3C7EB9B24
Show »

FASTA4,365481,018

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Ubiquitin ligase ARF-BP1/Mule modulates base excision repair."
Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J., Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G., Dianov G.L.
EMBO J. 28:3207-3215(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH POLB.
[26]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Submicroscopic duplications of the hydroxysteroid dehydrogenase HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with mental retardation."
Froyen G., Corbett M., Vandewalle J., Jarvela I., Lawrence O., Meldrum C., Bauters M., Govaerts K., Vandeleur L., Van Esch H., Chelly J., Sanlaville D., van Bokhoven H., Ropers H.-H., Laumonnier F., Ranieri E., Schwartz C.E., Abidi F. expand/collapse author list , Tarpey P.S., Futreal P.A., Whibley A., Raymond F.L., Stratton M.R., Fryns J.-P., Scott R., Peippo M., Sipponen M., Partington M., Mowat D., Field M., Hackett A., Marynen P., Turner G., Gecz J.
Am. J. Hum. Genet. 82:432-443(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MRXS-TURNER HIS-2981; TRP-4013 AND CYS-4187, INVOLVEMENT IN MRX17.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT47165.
RefSeqNP_113584.3. NM_031407.6.
XP_005262022.1. XM_005261965.2.
XP_005262023.1. XM_005261966.2.
XP_005262024.1. XM_005261967.2.
UniGeneHs.136905.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EKKNMR-A1317-1356[»]
3G1NX-ray2.60A/B4005-4374[»]
3H1DX-ray1.89A3993-4374[»]
ProteinModelPortalQ7Z6Z7.
SMRQ7Z6Z7. Positions 1310-1356, 4000-4366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115385. 65 interactions.
DIPDIP-34362N.
IntActQ7Z6Z7. 25 interactions.
MINTMINT-1576525.

PTM databases

PhosphoSiteQ7Z6Z7.

Polymorphism databases

DMDM73915353.

Proteomic databases

PaxDbQ7Z6Z7.
PRIDEQ7Z6Z7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262854; ENSP00000262854; ENSG00000086758. [Q7Z6Z7-1]
ENST00000342160; ENSP00000340648; ENSG00000086758. [Q7Z6Z7-1]
GeneID10075.
KEGGhsa:10075.
UCSCuc004dsn.4. human. [Q7Z6Z7-2]
uc004dsp.4. human. [Q7Z6Z7-1]

Organism-specific databases

CTD10075.
GeneCardsGC0XM053575.
HGNCHGNC:30892. HUWE1.
HPACAB022718.
HPA002548.
MIM300697. gene.
300705. phenotype.
300706. phenotype.
neXtProtNX_Q7Z6Z7.
Orphanet85328. Intellectual deficit, X-linked, Turner type.
PharmGKBPA128394567.
HUGESearch...
Search...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5021.
HOVERGENHBG080254.
KOK10592.
OMAGMTQEVG.
PhylomeDBQ7Z6Z7.
TreeFamTF323417.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ7Z6Z7.
BgeeQ7Z6Z7.
GenevestigatorQ7Z6Z7.

Family and domain databases

InterProIPR016024. 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]
PfamPF14377. 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]
SMARTSM00119. HECTc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF48371. SSF48371. 3 hits.
SSF56204. SSF56204. 1 hit.
PROSITEPS50237. HECT. 1 hit.
PS50030. UBA. 1 hit.
PS50918. WWE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHUWE1. human.
EvolutionaryTraceQ7Z6Z7.
GeneWikiHUWE1.
GenomeRNAi10075.
NextBio38085.
PROQ7Z6Z7.
SOURCESearch...

Entry information

Entry nameHUWE1_HUMAN
AccessionPrimary (citable) accession number: Q7Z6Z7
Secondary accession number(s): O15029 expand/collapse secondary AC list , Q4G2Z2, Q5H961, Q6P4D0, Q8NG67, Q9BUI0, Q9HCJ4, Q9NSL6, Q9P0A9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM