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Q7Z6Z7

- HUWE1_HUMAN

UniProt

Q7Z6Z7 - HUWE1_HUMAN

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Protein

E3 ubiquitin-protein ligase HUWE1

Gene

HUWE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Differentiation, DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:30892. HUWE1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. membrane Source: UniProtKB
  4. nucleus Source: UniProtKB
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.1 Publication
Note: The gene represented in this entry is involved in disease pathogenesis. A chromosomal microduplication involving HSD17B10 and HUWE1 has been found in patients with mental retardation.

Mutagenesis

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

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7Z6Z7.
PaxDbiQ7Z6Z7.
PRIDEiQ7Z6Z7.

PTM databases

PhosphoSiteiQ7Z6Z7.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ7Z6Z7.
ExpressionAtlasiQ7Z6Z7. baseline and differential.
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. 75 interactions.
DIPiDIP-34362N.
IntActiQ7Z6Z7. 25 interactions.
MINTiMINT-1576525.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7Z6Z7.

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00760000118966.
HOVERGENiHBG080254.
InParanoidiQ7Z6Z7.
KOiK10592.
OMAiGMTQEVG.
PhylomeDBiQ7Z6Z7.
TreeFamiTF323417.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

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

Also known as: LASU1, Large structure of UREB1

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

« Hide

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

Experimental Info

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

Natural variant

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

Alternative sequence

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

Sequence databases

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

Genome annotation databases

EnsembliENST00000262854; ENSP00000262854; ENSG00000086758. [Q7Z6Z7-1]
ENST00000342160; ENSP00000340648; ENSG00000086758. [Q7Z6Z7-1]
ENST00000612484; ENSP00000479451; ENSG00000086758. [Q7Z6Z7-3]
GeneIDi10075.
KEGGihsa:10075.
UCSCiuc004dsn.4. human. [Q7Z6Z7-2]
uc004dsp.4. human. [Q7Z6Z7-1]

Polymorphism databases

DMDMi73915353.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

BioGridi 115385. 75 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 ]
ENST00000612484 ; ENSP00000479451 ; ENSG00000086758 . [Q7Z6Z7-3 ]
GeneIDi 10075.
KEGGi hsa:10075.
UCSCi uc004dsn.4. human. [Q7Z6Z7-2 ]
uc004dsp.4. human. [Q7Z6Z7-1 ]

Organism-specific databases

CTDi 10075.
GeneCardsi GC0XM053559.
HGNCi HGNC:30892. HUWE1.
HPAi CAB022718.
HPA002548.
MIMi 300697. gene.
300705. phenotype.
300706. phenotype.
neXtProti NX_Q7Z6Z7.
Orphaneti 85328. X-linked intellectual disability, Turner type.
PharmGKBi PA128394567.
HUGEi Search...
Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5021.
GeneTreei ENSGT00760000118966.
HOVERGENi HBG080254.
InParanoidi Q7Z6Z7.
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

Bgeei Q7Z6Z7.
ExpressionAtlasi Q7Z6Z7. baseline and differential.
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: October 29, 2014
This is version 128 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