Reviewed, UniProtKB/Swiss-Prot O95714 (HERC2_HUMAN)

Names and origin

Protein names

Recommended name:
    Probable E3 ubiquitin-protein ligase HERC2
    EC=6.3.2.-
Alternative name(s):
    HECT domain and RCC1-like domain-containing protein 2

Gene names

Name:

HERC2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	4834 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates By similarity.
Pathway	Protein modification; protein ubiquitination.
Polymorphism	Genetic variations in HERC2 are associated with skin/hair/eye pigmentation variability type 1 (SHEP1) [MIM:227220]; also known as skin/hair/eye pigmentation type 1, blue/nonblue eyes or skin/hair/eye pigmentation type 1, blue/brown eyes or skin/hair/eye pigmentation type 1, blond/brown hair or eye color, brown/blue or eye color, blue/nonblue or eye color type 3 (EYCL3) or brown eye color type 2 (BEY2) or hair color type 3 (HCL3). Hair, eye and skin pigmentation are among the most visible examples of human phenotypic variation, with a broad normal range that is subject to substantial geographic stratification. In the case of skin, individuals tend to have lighter pigmentation with increasing distance from the equator. By contrast, the majority of variation in human eye and hair color is found among individuals of European ancestry, with most other human populations fixed for brown eyes and black hair.
Sequence similarities	Contains 1 cytochrome b5 heme-binding domain. Contains 1 DOC domain. Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. Contains 1 MIB/HERC2 domain. Contains 19 RCC1 repeats. Contains 6 WD repeats. Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Domain	Coiled coil Repeat WD repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	intracellular protein transport Ref.1 Non-traceable author statement. Source: UniProtKB modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein ubiquitination Inferred from electronic annotation. Source: InterPro regulation of mitotic metaphase/anaphase transition Inferred from electronic annotation. Source: InterPro
Cellular component	anaphase-promoting complex Inferred from electronic annotation. Source: InterPro
Molecular function	guanyl-nucleotide exchange factor activity Ref.1 Non-traceable author statement. Source: UniProtKB heme binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from electronic annotation. Source: InterPro ubiquitin-protein ligase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 4834	4834	Probable E3 ubiquitin-protein ligase HERC2		PRO_0000229739
Regions
	Repeat	2 – 46	45	WD 1
	Repeat	286 – 327	42	WD 2
	Repeat	490 – 529	40	WD 3
	Repeat	513 – 568	56	RCC1 1
	Repeat	569 – 620	52	RCC1 2
	Repeat	623 – 674	52	RCC1 3
	Repeat	675 – 726	52	RCC1 4
	Repeat	704 – 743	40	WD 4
	Repeat	728 – 778	51	RCC1 5
	Domain	1207 – 1283	77	Cytochrome b5 heme-binding
	Domain	1859 – 1932	74	MIB/HERC2
	Domain	2759 – 2936	178	DOC
	Repeat	2958 – 3009	52	RCC1 6
	Repeat	3010 – 3064	55	RCC1 7
	Repeat	3065 – 3116	52	RCC1 8
	Repeat	3118 – 3168	51	RCC1 9
	Repeat	3171 – 3222	52	RCC1 10
	Repeat	3224 – 3274	51	RCC1 11
	Repeat	3275 – 3326	52	RCC1 12
	Repeat	3926 – 3967	42	WD 5
	Repeat	3951 – 4002	52	RCC1 13
	Repeat	4004 – 4056	53	RCC1 14
	Repeat	4058 – 4108	51	RCC1 15
	Repeat	4110 – 4162	53	RCC1 16
	Repeat	4164 – 4214	51	RCC1 17
	Repeat	4216 – 4266	51	RCC1 18
	Repeat	4241 – 4283	43	WD 6
	Repeat	4268 – 4318	51	RCC1 19
	Domain	4457 – 4794	338	HECT
	Zinc finger	2702 – 2749	48	ZZ-type
	Coiled coil	948 – 980	33	Potential
Sites
	Active site	4762	1	Glycyl thioester intermediate By similarity
Amino acid modifications
	Modified residue	1577	1	Phosphoserine Ref.3
	Modified residue	1588	1	Phosphoserine Ref.3
	Modified residue	2928	1	Phosphoserine Ref.3 Ref.7 Ref.8
	Modified residue	4810	1	Phosphoserine Ref.8
	Modified residue	4811	1	Phosphoserine Ref.8
	Modified residue	4814	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	2881	1	Y → C Ref.2
	Sequence conflict	3070	1	S → W Ref.2
	Sequence conflict	3346	1	P → R Ref.2
	Sequence conflict	3583 – 3584	2	VA → MP Ref.2
	Sequence conflict	3597	1	D → N Ref.2
	Sequence conflict	3808	1	F → S Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O95714-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 02BA6F4D6471F6D9	FASTA	4,834	527,472
	10 20 30 40 50 60 MPSESFCLAA QARLDSKWLK TDIQLAFTRD GLCGLWNEMV KDGEIVYTGT ESTQNGELPP 70 80 90 100 110 120 RKDDSVEPSG TKKEDLNDKE KKDEEETPAP IYRAKSILDS WVWGKQPDVN ELKECLSVLV 130 140 150 160 170 180 KEQQALAVQS ATTTLSALRL KQRLVILERY FIALNRTVFQ ENVKVKWKSS GISLPPVDKK 190 200 210 220 230 240 SSRPAGKGVE GLARVGSRAA LSFAFAFLRR AWRSGEDADL CSELLQESLD ALRALPEASL 250 260 270 280 290 300 FDESTVSSVW LEVVERATRF LRSVVTGDVH GTPATKGPGS IPLQDQHLAL AILLELAVQR 310 320 330 340 350 360 GTLSQMLSAI LLLLQLWDSG AQETDNERSA QGTSAPLLPL LQRFQSIICR KDAPHSEGDM 370 380 390 400 410 420 HLLSGPLSPN ESFLRYLTLP QDNELAIDLR QTAVVVMAHL DRLATPCMPP LCSSPTSHKG 430 440 450 460 470 480 SLQEVIGWGL IGWKYYANVI GPIQCEGLAN LGVTQIACAE KRFLILSRNG RVYTQAYNSD 490 500 510 520 530 540 TLAPQLVQGL ASRNIVKIAA HSDGHHYLAL AATGEVYSWG CGDGGRLGHG DTVPLEEPKV 550 560 570 580 590 600 ISAFSGKQAG KHVVHIACGS TYSAAITAEG ELYTWGRGNY GRLGHGSSED EAIPMLVAGL 610 620 630 640 650 660 KGLKVIDVAC GSGDAQTLAV TENGQVWSWG DGDYGKLGRG GSDGCKTPKL IEKLQDLDVV 670 680 690 700 710 720 KVRCGSQFSI ALTKDGQVYS WGKGDNQRLG HGTEEHVRYP KLLEGLQGKK VIDVAAGSTH 730 740 750 760 770 780 CLALTEDSEV HSWGSNDQCQ HFDTLRVTKP EPAALPGLDT KHIVGIACGP AQSFAWSSCS 790 800 810 820 830 840 EWSIGLRVPF VVDICSMTFE QLDLLLRQVS EGMDGSADWP PPQEKECVAV ATLNLLRLQL 850 860 870 880 890 900 HAAISHQVDP EFLGLGLGSI LLNSLKQTVV TLASSAGVLS TVQSAAQAVL QSGWSVLLPT 910 920 930 940 950 960 AEERARALSA LLPCAVSGNE VNISPGRRFM IDLLVGSLMA DGGLESALHA AITAEIQDIE 970 980 990 1000 1010 1020 AKKEAQKEKE IDEQEANAST FHRSRTPLDK DLINTGICES SGKQCLPLVQ LIQQLLRNIA 1030 1040 1050 1060 1070 1080 SQTVARLKDV ARRISSCLDF EQHSRERSAS LDWLLRFQRL LISKLYPGES IGQTSDISSP 1090 1100 1110 1120 1130 1140 ELMGVGSLLK KYTALLCTHI GDILPVAASI ASTSWRHFAE VAYIVEGDFT GVLLPELVVS 1150 1160 1170 1180 1190 1200 IVLLLSKNAD LMQEAGAVPL LGGLLEHLDR FNHLAPGKER DDHEELAWPG IMESFFTGQN 1210 1220 1230 1240 1250 1260 CRNNEEVTLI RKADLENHNK DGGFWTVIDG KVYDIKDFQT QSLTGNSILA QFAGEDPVVA 1270 1280 1290 1300 1310 1320 LEAALQFEDT RESMHAFCVG QYLEPDQEIV TIPDLGSLSS PLIDTERNLG LLLGLHASYL 1330 1340 1350 1360 1370 1380 AMSTPLSPVE IECAKWLQSS IFSGGLQTSQ IHYRYNEEKD EDHCSSPGGT PASKSRLCSH 1390 1400 1410 1420 1430 1440 RRALGDHSQA FLQAIADNNI QDHNVKDFLC QIERYCRQCH LTTPIMFPPE HPVEEVGRLL 1450 1460 1470 1480 1490 1500 LCCLLKHEDL GHVALSLVHA GALGIEQVKH RTLPKSVVDV CRVVYQAKCS LIKTHQEQGR 1510 1520 1530 1540 1550 1560 SYKEVCAPVI ERLRFLFNEL RPAVCNDLSI MSKFKLLSSL PRWRRIAQKI IRERRKKRVP 1570 1580 1590 1600 1610 1620 KKPESMDDEE KIGNEESDLE EACILPHSPI NVDKRPIAIK SPKDKWQPLL STVTGVHKYK 1630 1640 1650 1660 1670 1680 WLKQNVQGLY PQSPLLSTIA EFALKEEPVD VEKMRKCLLK QLERAEVRLE GIDTILKLAS 1690 1700 1710 1720 1730 1740 KNFLLPSVQY AMFCGWQRLI PEGIDIGEPL TDCLKDVDLI PPFNRMLLEV TFGKLYAWAV 1750 1760 1770 1780 1790 1800 QNIRNVLMDA SATFKELGIQ PVPLQTITNE NPSGPSLGTI PQARFLLVML SMLTLQHGAN 1810 1820 1830 1840 1850 1860 NLDLLLNSGM LALTQTALRL IGPSCDNVEE DMNASAQGAS ATVLEETRKE TAPVQLPVSG 1870 1880 1890 1900 1910 1920 PELAAMMKIG TRVMRGVDWK WGDQDGPPPG LGRVIGELGE DGWIRVQWDT GSTNSYRMGK 1930 1940 1950 1960 1970 1980 EGKYDLKLAE LPAAAQPSAE DSDTEDDSEA EQTERNIHPT AMMFTSTINL LQTLCLSAGV 1990 2000 2010 2020 2030 2040 HAEIMQSEAT KTLCGLLRML VESGTTDKTS SPNRLVYREQ HRSWCTLGFV RSIALTPQVC 2050 2060 2070 2080 2090 2100 GALSSPQWIT LLMKVVEGHA PFTATSLQRQ ILAVHLLQAV LPSWDKTERA RDMKCLVEKL 2110 2120 2130 2140 2150 2160 FDFLGSLLTT CSSDVPLLRE STLRRRRVRP QASLTATHSS TLAEEVVALL RTLHSLTQWN 2170 2180 2190 2200 2210 2220 GLINKYINSQ LRSITHSFVG RPSEGAQLED YFPDSENPEV GGLMAVLAVI GGIDGRLRLG 2230 2240 2250 2260 2270 2280 GQVMHDEFGE GTVTRITPKG KITVQFSDMR TCRVCPLNQL KPLPAVAFNV NNLPFTEPML 2290 2300 2310 2320 2330 2340 SVWAQLVNLA GSKLEKHKIK KSTKQAFAGQ VDLDLLRCQQ LKLYILKAGR ALLSHQDKLR 2350 2360 2370 2380 2390 2400 QILSQPAVQE TGTVHTDDGA VVSPDLGDMS PEGPQPPMIL LQQLLASATQ PSPVKAIFDK 2410 2420 2430 2440 2450 2460 QELEAAALAV CQCLAVESTH PSSPGFEDCS SSEATTPVAV QHIHPARVKR RKQSPVPALP 2470 2480 2490 2500 2510 2520 IVVQLMEMGF SRRNIEFALK SLTGASGNAS SLPGVEALVG WLLDHSDIQV TELSDADTVS 2530 2540 2550 2560 2570 2580 DEYSDEEVVE DVDDAAYSMS TGAVVTESQT YKKRADFLSN DDYAVYVREN IQVGMMVRCC 2590 2600 2610 2620 2630 2640 RAYEEVCEGD VGKVIKLDRD GLHDLNVQCD WQQKGGTYWV RYIHVELIGY PPPSSSSHIK 2650 2660 2670 2680 2690 2700 IGDKVRVKAS VTTPKYKWGS VTHQSVGVVK AFSANGKDII VDFPQQSHWT GLLSEMELVP 2710 2720 2730 2740 2750 2760 SIHPGVTCDG CQMFPINGSR FKCRNCDDFD FCETCFKTKK HNTRHTFGRI NEPGQSAVFC 2770 2780 2790 2800 2810 2820 GRSGKQLKRC HSSQPGMLLD SWSRMVKSLN VSSSVNQASR LIDGSEPCWQ SSGSQGKHWI 2830 2840 2850 2860 2870 2880 RLEIFPDVLV HRLKMIVDPA DSSYMPSLVV VSGGNSLNNL IELKTININP SDTTVPLLND 2890 2900 2910 2920 2930 2940 YTEYHRYIEI AIKQCRSSGI DCKIHGLILL GRIRAEEEDL AAVPFLASDN EEEEDEKGNS 2950 2960 2970 2980 2990 3000 GSLIRKKAAG LESAATIRTK VFVWGLNDKD QLGGLKGSKI KVPSFSETLS ALNVVQVAGG 3010 3020 3030 3040 3050 3060 SKSLFAVTVE GKVYACGEAT NGRLGLGISS GTVPIPRQIT ALSSYVVKKV AVHSGGRHAT 3070 3080 3090 3100 3110 3120 ALTVDGKVFS WGEGDDGKLG HFSRMNCDKP RLIEALKTKR IRDIACGSSH SAALTSSGEL 3130 3140 3150 3160 3170 3180 YTWGLGEYGR LGHGDNTTQL KPKMVKVLLG HRVIQVACGS RDAQTLALTD EGLVFSWGDG 3190 3200 3210 3220 3230 3240 DFGKLGRGGS EGCNIPQNIE RLNGQGVCQI ECGAQFSLAL TKSGVVWTWG KGDYFRLGHG 3250 3260 3270 3280 3290 3300 SDVHVRKPQV VEGLRGKKIV HVAVGALHCL AVTDSGQVYA WGDNDHGQQG NGTTTVNRKP 3310 3320 3330 3340 3350 3360 TLVQGLEGQK ITRVACGSSH SVAWTTVDVA TPSVHEPVLF QTARDPLGAS YLGVPSDADS 3370 3380 3390 3400 3410 3420 SAASNKISGA SNSKPNRPSL AKILLSLDGN LAKQQALSHI LTALQIMYAR DAVVGALMPA 3430 3440 3450 3460 3470 3480 AMIAPVECPS FSSAAPSDAS AMASPMNGEE CMLAVDIEDR LSPNPWQEKR EIVSSEDAVT 3490 3500 3510 3520 3530 3540 PSAVTPSAPS ASARPFIPVT DDLGAASIIA ETMTKTKEDV ESQNKAAGPE PQALDEFTSL 3550 3560 3570 3580 3590 3600 LIADDTRVVV DLLKLSVCSR AGDRGRDVLS AVLSGMGTAY PQVADMLLEL CVTELEDVAT 3610 3620 3630 3640 3650 3660 DSQSGRLSSQ PVVVESSHPY TDDTSTSGTV KIPGAEGLRV EFDRQCSTER RHDPLTVMDG 3670 3680 3690 3700 3710 3720 VNRIVSVRSG REWSDWSSEL RIPGDELKWK FISDGSVNGW GWRFTVYPIM PAAGPKELLS 3730 3740 3750 3760 3770 3780 DRCVLSCPSM DLVTCLLDFR LNLASNRSIV PRLAASLAAC AQLSALAASH RMWALQRLRK 3790 3800 3810 3820 3830 3840 LLTTEFGQSI NINRLLGEND GETRALSFTG SALAALVKGL PEALQRQFEY EDPIVRGGKQ 3850 3860 3870 3880 3890 3900 LLHSPFFKVL VALACDLELD TLPCCAETHK WAWFRRYCMA SRVAVALDKR TPLPRLFLDE 3910 3920 3930 3940 3950 3960 VAKKIRELMA DSENMDVLHE SHDIFKREQD EQLVQWMNRR PDDWTLSAGG SGTIYGWGHN 3970 3980 3990 4000 4010 4020 HRGQLGGIEG AKVKVPTPCE ALATLRPVQL IGGEQTLFAV TADGKLYATG YGAGGRLGIG 4030 4040 4050 4060 4070 4080 GTESVSTPTL LESIQHVFIK KVAVNSGGKH CLALSSEGEV YSWGEAEDGK LGHGNRSPCD 4090 4100 4110 4120 4130 4140 RPRVIESLRG IEVVDVAAGG AHSACVTAAG DLYTWGKGRY GRLGHSDSED QLKPKLVEAL 4150 4160 4170 4180 4190 4200 QGHRVVDIAC GSGDAQTLCL TDDDTVWSWG DGDYGKLGRG GSDGCKVPMK IDSLTGLGVV 4210 4220 4230 4240 4250 4260 KVECGSQFSV ALTKSGAVYT WGKGDYHRLG HGSDDHVRRP RQVQGLQGKK VIAIATGSLH 4270 4280 4290 4300 4310 4320 CVCCTEDGEV YTWGDNDEGQ LGDGTTNAIQ RPRLVAALQG KKVNRVACGS AHTLAWSTSK 4330 4340 4350 4360 4370 4380 PASAGKLPAQ VPMEYNHLQE IPIIALRNRL LLLHHLSELF CPCIPMFDLE GSLDETGLGP 4390 4400 4410 4420 4430 4440 SVGFDTLRGI LISQGKEAAF RKVVQATMVR DRQHGPVVEL NRIQVKRSRS KGGLAGPDGT 4450 4460 4470 4480 4490 4500 KSVFGQMCAK MSSFGPDSLL LPHRVWKVKF VGESVDDCGG GYSESIAEIC EELQNGLTPL 4510 4520 4530 4540 4550 4560 LIVTPNGRDE SGANRDCYLL SPAARAPVHS SMFRFLGVLL GIAIRTGSPL SLNLAEPVWK 4570 4580 4590 4600 4610 4620 QLAGMSLTIA DLSEVDKDFI PGLMYIRDNE ATSEEFEAMS LPFTVPSASG QDIQLSSKHT 4630 4640 4650 4660 4670 4680 HITLDNRAEY VRLAINYRLH EFDEQVAAVR EGMARVVPVP LLSLFTGYEL ETMVCGSPDI 4690 4700 4710 4720 4730 4740 PLHLLKSVAT YKGIEPSASL IQWFWEVMES FSNTERSLFL RFVWGRTRLP RTIADFRGRD 4750 4760 4770 4780 4790 4800 FVIQVLDKYN PPDHFLPESY TCFFLLKLPR YSCKQVLEEK LKYAIHFCKS IDTDDYARIA 4810 4820 4830 LTGEPAADDS SDDSDNEDVD SFASDSTQDY LTGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ancestral gene for transcribed, low-copy repeats in the Prader-Willi/Angelman region encodes a large protein implicated in protein trafficking, which is deficient in mice with neuromuscular and spermiogenic abnormalities." Ji Y., Walkowicz M.J., Buiting K., Johnson D.K., Tarvin R.E., Rinchik E.M., Horsthemke B., Stubbs L., Nicholls R.D. Hum. Mol. Genet. 8:533-542(1999) [PubMed: 9949213] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure of the highly conserved HERC2 gene and of multiple partially duplicated paralogs in human." Ji Y., Rebert N.A., Joslin J.M., Higgins M.J., Schultz R.A., Nicholls R.D. Genome Res. 10:319-329(2000) [PubMed: 10720573] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2818-2895; 2909-2957; 2963-3290; 3317-3363; 3389-3430; 3458-3495; 3512-3527; 3533-3633; 3635-3821; 3826-4084; 4097-4505 AND 4529-4834, GENE STRUCTURE.
[3]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1577; SER-1588 AND SER-2928, MASS SPECTROMETRY. Tissue: Epithelium.
[4]	"Three genome-wide association studies and a linkage analysis identify HERC2 as a human iris color gene." Kayser M., Liu F., Janssens A.C.J.W., Rivadeneira F., Lao O., van Duijn K., Vermeulen M., Arp P., Jhamai M.M., van Ijcken W.F.J., den Dunnen J.T., Heath S., Zelenika D., Despriet D.D.G., Klaver C.C.W., Vingerling J.R., de Jong P.T.V.M., Hofman A. , Aulchenko Y.S., Uitterlinden A.G., Oostra B.A., van Duijn C.M. Am. J. Hum. Genet. 82:411-423(2008) [PubMed: 18252221] [Abstract] Cited for: INVOLVEMENT IN SHEP1.
[5]	"A single SNP in an evolutionary conserved region within intron 86 of the HERC2 gene determines human blue-brown eye color." Sturm R.A., Duffy D.L., Zhao Z.Z., Leite F.P.M., Stark M.S., Hayward N.K., Martin N.G., Montgomery G.W. Am. J. Hum. Genet. 82:424-431(2008) [PubMed: 18252222] [Abstract] Cited for: INVOLVEMENT IN SHEP1.
[6]	"Blue eye color in humans may be caused by a perfectly associated founder mutation in a regulatory element located within the HERC2 gene inhibiting OCA2 expression." Eiberg H., Troelsen J., Nielsen M., Mikkelsen A., Mengel-From J., Kjaer K.W., Hansen L. Hum. Genet. 123:177-187(2008) [PubMed: 18172690] [Abstract] Cited for: INVOLVEMENT IN SHEP1.
[7]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2928, MASS SPECTROMETRY.
[8]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2928; SER-4810; SER-4811 AND SER-4814, MASS SPECTROMETRY.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF071172 mRNA. Translation: AAD08657.1.
AF224243, AF224242 Genomic DNA. Translation: AAO27473.1.
AF224245, AF224244 Genomic DNA. Translation: AAO27474.1.
AF224249 , AF224246, AF224247, AF224248 Genomic DNA. Translation: AAO27475.1.
AF224251, AF224250 Genomic DNA. Translation: AAO27476.1.
AF224255, AF224254 Genomic DNA. Translation: AAO27479.1.
AF224252 Genomic DNA. Translation: AAO27477.1.
AF224253 Genomic DNA. Translation: AAO27478.1.
AF224257, AF224256 Genomic DNA. Translation: AAO27480.1.
AF225401, AF225400 Genomic DNA. Translation: AAO27481.1.
AF225404, AF225402, AF225403 Genomic DNA. Translation: AAO27482.1.
AF225407, AF225405, AF225406 Genomic DNA. Translation: AAO27483.1.
AF225409, AF225408 Genomic DNA. Translation: AAO27484.1.

IPI

IPI00005826.

RefSeq

NP_004658.3.

UniGene

Hs.434890
Hs.610412

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KEO	NMR	-	A	1203-1296	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O95714. 1 interaction.

PTM databases

PhosphoSite

O95714.

Proteomic databases

PRIDE

O95714.

Genome annotation databases

Ensembl

ENSG00000128731. Homo sapiens. [Contig view]

GeneID

8924.

KEGG

hsa:8924.

Organism-specific databases

GeneCards

GC15M026029.

H-InvDB

HIX0038976.
HIX0059549.
HIX0059593.

HGNC

HGNC:4868. HERC2.

HPA

CAB017188.

MIM

227220. phenotype.
605837. gene.

PharmGKB

PA29243.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O95714.

Gene expression databases

ArrayExpress

O95714.

Bgee

O95714.

GermOnline

ENSG00000128731. Homo sapiens.

Family and domain databases

InterPro

IPR004939. APC10.
IPR006624. Beta-propeller_rpt_TECPR.
IPR001199. Cyt_B5.
IPR018506. Cyt_B5_heme-BS.
IPR000569. HECT.
IPR010606. MIB_HERC2.
IPR000408. Reg_chr_condens.
IPR009091. Reg_csome_cond/b-lactamase_inh.
IPR019775. WD40_repeat_CS.
IPR000433. Znf_ZZ.
[Graphical view]

Gene3D

G3DSA:3.10.120.10. Cyt_B5. 1 hit.
G3DSA:2.130.10.30. Reg_csome_cond/b-lactamase_inh. 3 hits.

Pfam

PF00173. Cyt-b5. 1 hit.
PF00632. HECT. 1 hit.
PF06701. MIB_HERC2. 1 hit.
PF00415. RCC1. 16 hits.
PF00569. ZZ. 1 hit.
[Graphical view]

PRINTS

PR00633. RCCNDNSATION.

ProDom

PD000612. Cyt_B5. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00119. HECTc. 1 hit.
SM00706. TECPR. 5 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]

PROSITE

PS00191. CYTOCHROME_B5_1. False negative.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51284. DOC. 1 hit.
PS50237. HECT. 1 hit.
PS51416. MIB_HERC2. 1 hit.
PS00625. RCC1_1. False negative.
PS00626. RCC1_2. 1 hit.
PS50012. RCC1_3. 18 hits.
PS00678. WD_REPEATS_1. False negative.
PS50082. WD_REPEATS_2. False negative.
PS50294. WD_REPEATS_REGION. False negative.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

33552.

SOURCE

Search...

Entry information

Entry name

HERC2_HUMAN

Accession

Primary (citable) accession number: O95714
Secondary accession number(s): Q86SV7 , Q86SV8, Q86SV9, Q86YY3, Q86YY4, Q86YY5, Q86YY6, Q86YY7, Q86YY8, Q86YY9, Q86YZ0, Q86YZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)