Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O95714

- HERC2_HUMAN

UniProt

O95714 - HERC2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

E3 ubiquitin-protein ligase HERC2

Gene

HERC2

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

Functioni

E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity.3 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei4762 – 47621Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2702 – 274948ZZ-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activity Source: UniProtKB
  2. heme binding Source: InterPro
  3. ligase activity Source: UniProtKB-KW
  4. SUMO binding Source: UniProtKB
  5. ubiquitin protein ligase binding Source: UniProtKB
  6. ubiquitin-protein transferase activity Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. DNA repair Source: UniProtKB
  3. intracellular protein transport Source: UniProtKB
  4. positive regulation of GTPase activity Source: GOC
  5. protein ubiquitination Source: UniProtKB
  6. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
  7. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase HERC2 (EC:6.3.2.-)
Alternative name(s):
HECT domain and RCC1-like domain-containing protein 2
Gene namesi
Name:HERC2Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:4868. HERC2.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Nucleus
Note: Recruited to sites of DNA damage in response to ionizing radiation (IR) via its interaction with RNF8. May loose association with centrosomes during mitosis.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. membrane Source: UniProtKB
  4. mitochondrial inner membrane Source: Ensembl
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal recessive 38 (MRT38) [MIM:615516]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT38 is characterized by global developmental delay affecting motor, speech, adaptive, and social development. Patients manifest autistic features, aggression, self-injury, impulsivity, and distractibility.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti594 – 5941P → L in MRT38; less stable than wild-type; diffuse cytosolic localization with the formation of abnormal aggregates. 1 Publication
VAR_069282

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2708 – 27081C → S: Abolishes binding to SUMO; when associated with S-2711. 1 Publication
Mutagenesisi2711 – 27111C → S: Abolishes binding to SUMO; when associated with S-2708. 1 Publication
Mutagenesisi4827 – 48271T → A: Prevents HERC2 C-terminal fragment binding to endogenous RNF8. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi227220. phenotype.
615516. phenotype.
Orphaneti329195. Developmental delay with autism spectrum disorder and gait instability.
PharmGKBiPA29243.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 48344834E3 ubiquitin-protein ligase HERC2PRO_0000229739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei647 – 6471Phosphothreonine1 Publication
Modified residuei1577 – 15771PhosphoserineBy similarity
Modified residuei1944 – 19441Phosphothreonine1 Publication
Modified residuei2454 – 24541Phosphoserine3 Publications
Modified residuei2928 – 29281Phosphoserine4 Publications
Modified residuei4810 – 48101Phosphoserine1 Publication
Modified residuei4811 – 48111Phosphoserine1 Publication
Modified residuei4814 – 48141Phosphoserine1 Publication
Modified residuei4827 – 48271Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylation at Thr-4827 is required for interaction with RNF8.6 Publications
Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks (DSBs), promoting the interaction with RNF8.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO95714.
PaxDbiO95714.
PRIDEiO95714.

PTM databases

PhosphoSiteiO95714.

Expressioni

Gene expression databases

BgeeiO95714.
ExpressionAtlasiO95714. baseline and differential.
GenevestigatoriO95714.

Organism-specific databases

HPAiCAB017188.
HPA048389.

Interactioni

Subunit structurei

Interacts (when phosphorylated at Thr-4827 and sumoylated) with RNF8 (via FHA domain); this interaction increases after ionizing radiation (IR) treatment. Interacts with XPA. Interacts with NEURL4. Via its interaction with NEURL4, may indirectly interact with CCP110 and CEP97.4 Publications

Protein-protein interaction databases

BioGridi114438. 65 interactions.
DIPiDIP-37632N.
IntActiO95714. 14 interactions.
MINTiMINT-8415335.

Structurei

Secondary structure

1
4834
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi425 – 4306
Helixi446 – 4494
Beta strandi453 – 4586
Beta strandi460 – 4678
Beta strandi472 – 4765
Beta strandi495 – 4995
Beta strandi505 – 5117
Beta strandi516 – 5205
Helixi523 – 5253
Beta strandi528 – 5314
Beta strandi535 – 5406
Helixi542 – 5443
Helixi549 – 5513
Beta strandi552 – 5587
Beta strandi560 – 5678
Beta strandi572 – 5765
Helixi579 – 5813
Beta strandi585 – 5873
Beta strandi591 – 5966
Helixi598 – 6003
Beta strandi605 – 6106
Beta strandi616 – 6216
Beta strandi626 – 6305
Helixi633 – 6353
Beta strandi638 – 6425
Beta strandi645 – 6506
Helixi652 – 6543
Beta strandi659 – 6657
Beta strandi668 – 6736
Beta strandi678 – 6825
Helixi685 – 6873
Beta strandi691 – 6933
Beta strandi697 – 7026
Helixi704 – 7063
Beta strandi711 – 7166
Beta strandi718 – 7258
Beta strandi730 – 7356
Beta strandi746 – 7549
Beta strandi763 – 7686
Beta strandi770 – 7778
Turni781 – 7833
Helixi1212 – 122110
Beta strandi1225 – 12284
Beta strandi1231 – 12344
Helixi1235 – 12428
Helixi1250 – 12523
Helixi1257 – 126610
Helixi1270 – 12734
Helixi1274 – 12774
Beta strandi1278 – 12825
Helixi1285 – 12884
Beta strandi3954 – 39596
Beta strandi3971 – 39788
Helixi3980 – 39845
Beta strandi3987 – 39937
Beta strandi3996 – 40016
Beta strandi4006 – 40105
Helixi4013 – 40153
Beta strandi4018 – 40225
Beta strandi4025 – 40306
Helixi4032 – 40343
Beta strandi4039 – 40435
Beta strandi4049 – 40557
Beta strandi4060 – 40645
Helixi4067 – 40693
Beta strandi4073 – 40753
Beta strandi4079 – 40846
Helixi4086 – 40883
Beta strandi4093 – 40986
Beta strandi4100 – 41078
Beta strandi4112 – 41165
Helixi4119 – 41213
Beta strandi4125 – 41273
Beta strandi4131 – 41366
Helixi4138 – 41403
Beta strandi4145 – 41506
Beta strandi4156 – 41616
Turni4162 – 41643
Beta strandi4165 – 41706
Helixi4173 – 41753
Beta strandi4178 – 41814
Beta strandi4185 – 41906
Helixi4192 – 41943
Beta strandi4199 – 42057
Beta strandi4208 – 42136
Beta strandi4218 – 42225
Helixi4225 – 42273
Beta strandi4231 – 42333
Beta strandi4237 – 42426
Helixi4244 – 42463
Beta strandi4251 – 42566
Beta strandi4258 – 42658
Beta strandi4270 – 42745
Beta strandi4283 – 42853
Beta strandi4289 – 42946
Helixi4296 – 42983
Beta strandi4305 – 43095
Beta strandi4312 – 43165

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KEONMR-A1203-1296[»]
3KCIX-ray1.80A3951-4321[»]
4L1MX-ray2.60A/B/C417-790[»]
ProteinModelPortaliO95714.
SMRiO95714. Positions 422-779, 1205-1296, 1867-1929, 3953-4318.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95714.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati415 – 46147RCC1 1-11 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati462 – 51251RCC1 1-21 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati513 – 56856RCC1 1-31 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati569 – 62052RCC1 1-41 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati623 – 67452RCC1 1-51 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati675 – 72652RCC1 1-61 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati728 – 77851RCC1 1-71 PublicationPROSITE-ProRule annotationAdd
BLAST
Domaini1207 – 128377Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1859 – 193274MIB/HERC2PROSITE-ProRule annotationAdd
BLAST
Domaini2759 – 2936178DOCPROSITE-ProRule annotationAdd
BLAST
Repeati2958 – 300952RCC1 2-11 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati3010 – 306455RCC1 2-21 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati3065 – 311652RCC1 2-31 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati3118 – 316851RCC1 2-41 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati3171 – 322252RCC1 2-51 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati3224 – 327451RCC1 2-61 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati3275 – 332652RCC1 2-71 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati3951 – 400252RCC1 3-11 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati4004 – 405653RCC1 3-21 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati4058 – 410851RCC1 3-31 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati4110 – 416253RCC1 3-41 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati4164 – 421451RCC1 3-51 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati4216 – 426651RCC1 3-61 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati4268 – 431851RCC1 3-71 PublicationPROSITE-ProRule annotationAdd
BLAST
Domaini4457 – 4794338HECTPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili948 – 98033Sequence AnalysisAdd
BLAST

Domaini

The ZZ-type zinc finger mediates binding to SUMO1, and at lowe level SUMO2.1 Publication
The RCC1 repeats are grouped into three seven-bladed beta-propeller regions.1 Publication

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation
Contains 1 DOC domain.PROSITE-ProRule annotation
Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
Contains 1 MIB/HERC2 domain.PROSITE-ProRule annotation
Contains 21 RCC1 repeats.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2702 – 274948ZZ-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00760000118918.
HOVERGENiHBG081598.
InParanoidiO95714.
KOiK10595.
OMAiGHGTDVH.
PhylomeDBiO95714.
TreeFamiTF320636.

Family and domain databases

Gene3Di2.130.10.30. 3 hits.
2.30.30.30. 1 hit.
2.60.120.260. 1 hit.
3.10.120.10. 1 hit.
InterProiIPR004939. APC_su10/DOC_dom.
IPR006624. Beta-propeller_rpt_TECPR.
IPR021097. CPH_domain.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR008979. Galactose-bd-like.
IPR000569. HECT.
IPR010606. Mib_Herc2.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR014722. Rib_L2_dom2.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF03256. APC10. 1 hit.
PF11515. Cul7. 1 hit.
PF00173. Cyt-b5. 1 hit.
PF00632. HECT. 1 hit.
PF06701. MIB_HERC2. 1 hit.
PF00415. RCC1. 18 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SMARTiSM00119. HECTc. 1 hit.
SM00706. TECPR. 5 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF50985. SSF50985. 3 hits.
SSF55856. SSF55856. 1 hit.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50255. CYTOCHROME_B5_2. 1 hit.
PS51284. DOC. 1 hit.
PS50237. HECT. 1 hit.
PS51416. MIB_HERC2. 1 hit.
PS00626. RCC1_2. 1 hit.
PS50012. RCC1_3. 18 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95714-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPSESFCLAA QARLDSKWLK TDIQLAFTRD GLCGLWNEMV KDGEIVYTGT
60 70 80 90 100
ESTQNGELPP RKDDSVEPSG TKKEDLNDKE KKDEEETPAP IYRAKSILDS
110 120 130 140 150
WVWGKQPDVN ELKECLSVLV KEQQALAVQS ATTTLSALRL KQRLVILERY
160 170 180 190 200
FIALNRTVFQ ENVKVKWKSS GISLPPVDKK SSRPAGKGVE GLARVGSRAA
210 220 230 240 250
LSFAFAFLRR AWRSGEDADL CSELLQESLD ALRALPEASL FDESTVSSVW
260 270 280 290 300
LEVVERATRF LRSVVTGDVH GTPATKGPGS IPLQDQHLAL AILLELAVQR
310 320 330 340 350
GTLSQMLSAI LLLLQLWDSG AQETDNERSA QGTSAPLLPL LQRFQSIICR
360 370 380 390 400
KDAPHSEGDM HLLSGPLSPN ESFLRYLTLP QDNELAIDLR QTAVVVMAHL
410 420 430 440 450
DRLATPCMPP LCSSPTSHKG SLQEVIGWGL IGWKYYANVI GPIQCEGLAN
460 470 480 490 500
LGVTQIACAE KRFLILSRNG RVYTQAYNSD TLAPQLVQGL ASRNIVKIAA
510 520 530 540 550
HSDGHHYLAL AATGEVYSWG CGDGGRLGHG DTVPLEEPKV ISAFSGKQAG
560 570 580 590 600
KHVVHIACGS TYSAAITAEG ELYTWGRGNY GRLGHGSSED EAIPMLVAGL
610 620 630 640 650
KGLKVIDVAC GSGDAQTLAV TENGQVWSWG DGDYGKLGRG GSDGCKTPKL
660 670 680 690 700
IEKLQDLDVV KVRCGSQFSI ALTKDGQVYS WGKGDNQRLG HGTEEHVRYP
710 720 730 740 750
KLLEGLQGKK VIDVAAGSTH CLALTEDSEV HSWGSNDQCQ HFDTLRVTKP
760 770 780 790 800
EPAALPGLDT KHIVGIACGP AQSFAWSSCS EWSIGLRVPF VVDICSMTFE
810 820 830 840 850
QLDLLLRQVS EGMDGSADWP PPQEKECVAV ATLNLLRLQL HAAISHQVDP
860 870 880 890 900
EFLGLGLGSI LLNSLKQTVV TLASSAGVLS TVQSAAQAVL QSGWSVLLPT
910 920 930 940 950
AEERARALSA LLPCAVSGNE VNISPGRRFM IDLLVGSLMA DGGLESALHA
960 970 980 990 1000
AITAEIQDIE AKKEAQKEKE IDEQEANAST FHRSRTPLDK DLINTGICES
1010 1020 1030 1040 1050
SGKQCLPLVQ LIQQLLRNIA SQTVARLKDV ARRISSCLDF EQHSRERSAS
1060 1070 1080 1090 1100
LDLLLRFQRL LISKLYPGES IGQTSDISSP ELMGVGSLLK KYTALLCTHI
1110 1120 1130 1140 1150
GDILPVAASI ASTSWRHFAE VAYIVEGDFT GVLLPELVVS IVLLLSKNAG
1160 1170 1180 1190 1200
LMQEAGAVPL LGGLLEHLDR FNHLAPGKER DDHEELAWPG IMESFFTGQN
1210 1220 1230 1240 1250
CRNNEEVTLI RKADLENHNK DGGFWTVIDG KVYDIKDFQT QSLTGNSILA
1260 1270 1280 1290 1300
QFAGEDPVVA LEAALQFEDT RESMHAFCVG QYLEPDQEIV TIPDLGSLSS
1310 1320 1330 1340 1350
PLIDTERNLG LLLGLHASYL AMSTPLSPVE IECAKWLQSS IFSGGLQTSQ
1360 1370 1380 1390 1400
IHYSYNEEKD EDHCSSPGGT PASKSRLCSH RRALGDHSQA FLQAIADNNI
1410 1420 1430 1440 1450
QDHNVKDFLC QIERYCRQCH LTTPIMFPPE HPVEEVGRLL LCCLLKHEDL
1460 1470 1480 1490 1500
GHVALSLVHA GALGIEQVKH RTLPKSVVDV CRVVYQAKCS LIKTHQEQGR
1510 1520 1530 1540 1550
SYKEVCAPVI ERLRFLFNEL RPAVCNDLSI MSKFKLLSSL PRWRRIAQKI
1560 1570 1580 1590 1600
IRERRKKRVP KKPESTDDEE KIGNEESDLE EACILPHSPI NVDKRPIAIK
1610 1620 1630 1640 1650
SPKDKWQPLL STVTGVHKYK WLKQNVQGLY PQSPLLSTIA EFALKEEPVD
1660 1670 1680 1690 1700
VEKMRKCLLK QLERAEVRLE GIDTILKLAS KNFLLPSVQY AMFCGWQRLI
1710 1720 1730 1740 1750
PEGIDIGEPL TDCLKDVDLI PPFNRMLLEV TFGKLYAWAV QNIRNVLMDA
1760 1770 1780 1790 1800
SAKFKELGIQ PVPLQTITNE NPSGPSLGTI PQARFLLVML SMLTLQHGAN
1810 1820 1830 1840 1850
NLDLLLNSGM LALTQTALRL IGPSCDNVEE DMNASAQGAS ATVLEETRKE
1860 1870 1880 1890 1900
TAPVQLPVSG PELAAMMKIG TRVMRGVDWK WGDQDGPPPG LGRVIGELGE
1910 1920 1930 1940 1950
DGWIRVQWDT GSTNSYRMGK EGKYDLKLAE LPAAAQPSAE DSDTEDDSEA
1960 1970 1980 1990 2000
EQTERNIHPT AMMFTSTINL LQTLCLSAGV HAEIMQSEAT KTLCGLLRML
2010 2020 2030 2040 2050
VESGTTDKTS SPNRLVYREQ HRSWCTLGFV RSIALTPQVC GALSSPQWIT
2060 2070 2080 2090 2100
LLMKVVEGHA PFTATSLQRQ ILAVHLLQAV LPSWDKTERA RDMKCLVEKL
2110 2120 2130 2140 2150
FDFLGSLLTT CSSDVPLLRE STLRRRRVRP QASLTATHSS TLAEEVVALL
2160 2170 2180 2190 2200
RTLHSLTQWN GLINKYINSQ LRSITHSFVG RPSEGAQLED YFPDSENPEV
2210 2220 2230 2240 2250
GGLMAVLAVI GGIDGRLRLG GQVMHDEFGE GTVTRITPKG KITVQFSDMR
2260 2270 2280 2290 2300
TCRVCPLNQL KPLPAVAFNV NNLPFTEPML SVWAQLVNLA GSKLEKHKIK
2310 2320 2330 2340 2350
KSTKQAFAGQ VDLDLLRCQQ LKLYILKAGR ALLSHQDKLR QILSQPAVQE
2360 2370 2380 2390 2400
TGTVHTDDGA VVSPDLGDMS PEGPQPPMIL LQQLLASATQ PSPVKAIFDK
2410 2420 2430 2440 2450
QELEAAALAV CQCLAVESTH PSSPGFEDCS SSEATTPVAV QHIRPARVKR
2460 2470 2480 2490 2500
RKQSPVPALP IVVQLMEMGF SRRNIEFALK SLTGASGNAS SLPGVEALVG
2510 2520 2530 2540 2550
WLLDHSDIQV TELSDADTVS DEYSDEEVVE DVDDAAYSMS TGAVVTESQT
2560 2570 2580 2590 2600
YKKRADFLSN DDYAVYVREN IQVGMMVRCC RAYEEVCEGD VGKVIKLDRD
2610 2620 2630 2640 2650
GLHDLNVQCD WQQKGGTYWV RYIHVELIGY PPPSSSSHIK IGDKVRVKAS
2660 2670 2680 2690 2700
VTTPKYKWGS VTHQSVGVVK AFSANGKDII VDFPQQSHWT GLLSEMELVP
2710 2720 2730 2740 2750
SIHPGVTCDG CQMFPINGSR FKCRNCDDFD FCETCFKTKK HNTRHTFGRI
2760 2770 2780 2790 2800
NEPGQSAVFC GRSGKQLKRC HSSQPGMLLD SWSRMVKSLN VSSSVNQASR
2810 2820 2830 2840 2850
LIDGSEPCWQ SSGSQGKHWI RLEIFPDVLV HRLKMIVDPA DSSYMPSLVV
2860 2870 2880 2890 2900
VSGGNSLNNL IELKTININP SDTTVPLLND CTEYHRYIEI AIKQCRSSGI
2910 2920 2930 2940 2950
DCKIHGLILL GRIRAEEEDL AAVPFLASDN EEEEDEKGNS GSLIRKKAAG
2960 2970 2980 2990 3000
LESAATIRTK VFVWGLNDKD QLGGLKGSKI KVPSFSETLS ALNVVQVAGG
3010 3020 3030 3040 3050
SKSLFAVTVE GKVYACGEAT NGRLGLGISS GTVPIPRQIT ALSSYVVKKV
3060 3070 3080 3090 3100
AVHSGGRHAT ALTVDGKVFS WGEGDDGKLG HFSRMNCDKP RLIEALKTKR
3110 3120 3130 3140 3150
IRDIACGSSH SAALTSSGEL YTWGLGEYGR LGHGDNTTQL KPKMVKVLLG
3160 3170 3180 3190 3200
HRVIQVACGS RDAQTLALTD EGLVFSWGDG DFGKLGRGGS EGCNIPQNIE
3210 3220 3230 3240 3250
RLNGQGVCQI ECGAQFSLAL TKSGVVWTWG KGDYFRLGHG SDVHVRKPQV
3260 3270 3280 3290 3300
VEGLRGKKIV HVAVGALHCL AVTDSGQVYA WGDNDHGQQG NGTTTVNRKP
3310 3320 3330 3340 3350
TLVQGLEGQK ITRVACGSSH SVAWTTVDVA TPSVHEPVLF QTARDPLGAS
3360 3370 3380 3390 3400
YLGVPSDADS SAASNKISGA SNSKPNRPSL AKILLSLDGN LAKQQALSHI
3410 3420 3430 3440 3450
LTALQIMYAR DAVVGALMPA AMIAPVECPS FSSAAPSDAS AMASPMNGEE
3460 3470 3480 3490 3500
CMLAVDIEDR LSPNPWQEKR EIVSSEDAVT PSAVTPSAPS ASARPFIPVT
3510 3520 3530 3540 3550
DDLGAASIIA ETMTKTKEDV ESQNKAAGPE PQALDEFTSL LIADDTRVVV
3560 3570 3580 3590 3600
DLLKLSVCSR AGDRGRDVLS AVLSGMGTAY PQVADMLLEL CVTELEDVAT
3610 3620 3630 3640 3650
DSQSGRLSSQ PVVVESSHPY TDDTSTSGTV KIPGAEGLRV EFDRQCSTER
3660 3670 3680 3690 3700
RHDPLTVMDG VNRIVSVRSG REWSDWSSEL RIPGDELKWK FISDGSVNGW
3710 3720 3730 3740 3750
GWRFTVYPIM PAAGPKELLS DRCVLSCPSM DLVTCLLDFR LNLASNRSIV
3760 3770 3780 3790 3800
PRLAASLAAC AQLSALAASH RMWALQRLRK LLTTEFGQSI NINRLLGEND
3810 3820 3830 3840 3850
GETRALSFTG SALAALVKGL PEALQRQFEY EDPIVRGGKQ LLHSPFFKVL
3860 3870 3880 3890 3900
VALACDLELD TLPCCAETHK WAWFRRYCMA SRVAVALDKR TPLPRLFLDE
3910 3920 3930 3940 3950
VAKKIRELMA DSENMDVLHE SHDIFKREQD EQLVQWMNRR PDDWTLSAGG
3960 3970 3980 3990 4000
SGTIYGWGHN HRGQLGGIEG AKVKVPTPCE ALATLRPVQL IGGEQTLFAV
4010 4020 4030 4040 4050
TADGKLYATG YGAGGRLGIG GTESVSTPTL LESIQHVFIK KVAVNSGGKH
4060 4070 4080 4090 4100
CLALSSEGEV YSWGEAEDGK LGHGNRSPCD RPRVIESLRG IEVVDVAAGG
4110 4120 4130 4140 4150
AHSACVTAAG DLYTWGKGRY GRLGHSDSED QLKPKLVEAL QGHRVVDIAC
4160 4170 4180 4190 4200
GSGDAQTLCL TDDDTVWSWG DGDYGKLGRG GSDGCKVPMK IDSLTGLGVV
4210 4220 4230 4240 4250
KVECGSQFSV ALTKSGAVYT WGKGDYHRLG HGSDDHVRRP RQVQGLQGKK
4260 4270 4280 4290 4300
VIAIATGSLH CVCCTEDGEV YTWGDNDEGQ LGDGTTNAIQ RPRLVAALQG
4310 4320 4330 4340 4350
KKVNRVACGS AHTLAWSTSK PASAGKLPAQ VPMEYNHLQE IPIIALRNRL
4360 4370 4380 4390 4400
LLLHHLSELF CPCIPMFDLE GSLDETGLGP SVGFDTLRGI LISQGKEAAF
4410 4420 4430 4440 4450
RKVVQATMVR DRQHGPVVEL NRIQVKRSRS KGGLAGPDGT KSVFGQMCAK
4460 4470 4480 4490 4500
MSSFGPDSLL LPHRVWKVKF VGESVDDCGG GYSESIAEIC EELQNGLTPL
4510 4520 4530 4540 4550
LIVTPNGRDE SGANRDCYLL SPAARAPVHS SMFRFLGVLL GIAIRTGSPL
4560 4570 4580 4590 4600
SLNLAEPVWK QLAGMSLTIA DLSEVDKDFI PGLMYIRDNE ATSEEFEAMS
4610 4620 4630 4640 4650
LPFTVPSASG QDIQLSSKHT HITLDNRAEY VRLAINYRLH EFDEQVAAVR
4660 4670 4680 4690 4700
EGMARVVPVP LLSLFTGYEL ETMVCGSPDI PLHLLKSVAT YKGIEPSASL
4710 4720 4730 4740 4750
IQWFWEVMES FSNTERSLFL RFVWGRTRLP RTIADFRGRD FVIQVLDKYN
4760 4770 4780 4790 4800
PPDHFLPESY TCFFLLKLPR YSCKQVLEEK LKYAIHFCKS IDTDDYARIA
4810 4820 4830
LTGEPAADDS SDDSDNEDVD SFASDSTQDY LTGH
Length:4,834
Mass (Da):527,228
Last modified:October 5, 2010 - v2
Checksum:iA323DC1DA6B221D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1053 – 10531L → W in AAD08657. (PubMed:9949213)Curated
Sequence conflicti1150 – 11501G → D in AAD08657. (PubMed:9949213)Curated
Sequence conflicti1354 – 13541S → R in AAD08657. (PubMed:9949213)Curated
Sequence conflicti1566 – 15661T → M in AAD08657. (PubMed:9949213)Curated
Sequence conflicti1753 – 17531K → T in AAD08657. (PubMed:9949213)Curated
Sequence conflicti2444 – 24441R → H in AAD08657. (PubMed:9949213)Curated
Sequence conflicti2881 – 28811C → Y in AAD08657. (PubMed:9949213)Curated
Sequence conflicti3070 – 30701S → W in AAO27475. (PubMed:10720573)Curated
Sequence conflicti3346 – 33461P → R in AAO27476. (PubMed:10720573)Curated
Sequence conflicti3583 – 35842VA → MP in AAO27480. (PubMed:10720573)Curated
Sequence conflicti3597 – 35971D → N in AAO27480. (PubMed:10720573)Curated
Sequence conflicti3808 – 38081F → S in AAO27481. (PubMed:10720573)Curated

Polymorphismi

Genetic variants in HERC2 define the skin/hair/eye pigmentation variation locus 1 (SHEP1) [MIMi: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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti594 – 5941P → L in MRT38; less stable than wild-type; diffuse cytosolic localization with the formation of abnormal aggregates. 1 Publication
VAR_069282

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF071172 mRNA. Translation: AAD08657.1.
AC091304 Genomic DNA. No translation available.
AC126332 Genomic DNA. No translation available.
AC135329 Genomic DNA. No translation available.
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.
CCDSiCCDS10021.1.
RefSeqiNP_004658.3. NM_004667.5.
UniGeneiHs.434890.
Hs.610412.
Hs.741019.

Genome annotation databases

EnsembliENST00000261609; ENSP00000261609; ENSG00000128731.
GeneIDi8924.
KEGGihsa:8924.
UCSCiuc001zbj.4. human.

Cross-referencesi

Web resourcesi

Hect domain and RLD 2 (HERC2)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF071172 mRNA. Translation: AAD08657.1 .
AC091304 Genomic DNA. No translation available.
AC126332 Genomic DNA. No translation available.
AC135329 Genomic DNA. No translation available.
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 .
CCDSi CCDS10021.1.
RefSeqi NP_004658.3. NM_004667.5.
UniGenei Hs.434890.
Hs.610412.
Hs.741019.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KEO NMR - A 1203-1296 [» ]
3KCI X-ray 1.80 A 3951-4321 [» ]
4L1M X-ray 2.60 A/B/C 417-790 [» ]
ProteinModelPortali O95714.
SMRi O95714. Positions 422-779, 1205-1296, 1867-1929, 3953-4318.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114438. 65 interactions.
DIPi DIP-37632N.
IntActi O95714. 14 interactions.
MINTi MINT-8415335.

PTM databases

PhosphoSitei O95714.

Proteomic databases

MaxQBi O95714.
PaxDbi O95714.
PRIDEi O95714.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261609 ; ENSP00000261609 ; ENSG00000128731 .
GeneIDi 8924.
KEGGi hsa:8924.
UCSCi uc001zbj.4. human.

Organism-specific databases

CTDi 8924.
GeneCardsi GC15M028356.
GeneReviewsi HERC2.
H-InvDB HIX0012044.
HIX0017540.
HIX0038121.
HIX0038320.
HIX0038830.
HIX0173226.
HIX0173299.
HIX0194348.
HGNCi HGNC:4868. HERC2.
HPAi CAB017188.
HPA048389.
MIMi 227220. phenotype.
605837. gene.
615516. phenotype.
neXtProti NX_O95714.
Orphaneti 329195. Developmental delay with autism spectrum disorder and gait instability.
PharmGKBi PA29243.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5021.
GeneTreei ENSGT00760000118918.
HOVERGENi HBG081598.
InParanoidi O95714.
KOi K10595.
OMAi GHGTDVH.
PhylomeDBi O95714.
TreeFami TF320636.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTracei O95714.
GeneWikii HERC2.
GenomeRNAii 8924.
NextBioi 33552.
PROi O95714.
SOURCEi Search...

Gene expression databases

Bgeei O95714.
ExpressionAtlasi O95714. baseline and differential.
Genevestigatori O95714.

Family and domain databases

Gene3Di 2.130.10.30. 3 hits.
2.30.30.30. 1 hit.
2.60.120.260. 1 hit.
3.10.120.10. 1 hit.
InterProi IPR004939. APC_su10/DOC_dom.
IPR006624. Beta-propeller_rpt_TECPR.
IPR021097. CPH_domain.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR008979. Galactose-bd-like.
IPR000569. HECT.
IPR010606. Mib_Herc2.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR014722. Rib_L2_dom2.
IPR000433. Znf_ZZ.
[Graphical view ]
Pfami PF03256. APC10. 1 hit.
PF11515. Cul7. 1 hit.
PF00173. Cyt-b5. 1 hit.
PF00632. HECT. 1 hit.
PF06701. MIB_HERC2. 1 hit.
PF00415. RCC1. 18 hits.
PF00569. ZZ. 1 hit.
[Graphical view ]
PRINTSi PR00633. RCCNDNSATION.
SMARTi SM00119. HECTc. 1 hit.
SM00706. TECPR. 5 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF50985. SSF50985. 3 hits.
SSF55856. SSF55856. 1 hit.
SSF56204. SSF56204. 1 hit.
PROSITEi PS50255. CYTOCHROME_B5_2. 1 hit.
PS51284. DOC. 1 hit.
PS50237. HECT. 1 hit.
PS51416. MIB_HERC2. 1 hit.
PS00626. RCC1_2. 1 hit.
PS50012. RCC1_3. 18 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] [Europe PMC] [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.
  4. "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-2454 AND SER-2928, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: INVOLVEMENT IN SHEP1.
  6. "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] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SHEP1.
  7. "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] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SHEP1, REGULATION OF OCA2.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2928; SER-4810; SER-4811 AND SER-4814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "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-2454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. Cited for: MISCELLANEOUS.
  12. "HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes."
    Bekker-Jensen S., Rendtlew Danielsen J., Fugger K., Gromova I., Nerstedt A., Lukas C., Bartek J., Lukas J., Mailand N.
    Nat. Cell Biol. 12:80-86(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RNF8, PHOSPHORYLATION AT THR-4827, MUTAGENESIS OF THR-4827, SUBCELLULAR LOCATION.
  13. "Circadian control of XPA and excision repair of cisplatin-DNA damage by cryptochrome and HERC2 ubiquitin ligase."
    Kang T.H., Lindsey-Boltz L.A., Reardon J.T., Sancar A.
    Proc. Natl. Acad. Sci. U.S.A. 107:4890-4895(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITIN LIGASE ACTIVITY, INTERACTION WITH XPA, SUBCELLULAR LOCATION.
  14. "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-2454 AND SER-2928, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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 THR-647; THR-1944 AND SER-2928, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger."
    Danielsen J.R., Povlsen L.K., Villumsen B.H., Streicher W., Nilsson J., Wikstrom M., Bekker-Jensen S., Mailand N.
    J. Cell Biol. 197:179-187(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, FUNCTION, SUMO-BINDING, DOMAIN, INTERACTION WITH RNF8, MUTAGENESIS OF CYS-2708 AND CYS-2711.
  18. "Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as novel modulators of centrosome architecture."
    Al-Hakim A.K., Bashkurov M., Gingras A.C., Durocher D., Pelletier L.
    Mol. Cell. Proteomics 11:M111.014233.01-M111.014233.14(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCP110; CEP97 AND NEURL4, SUBCELLULAR LOCATION.
  19. "Structure of the first RCC1-like domain of HERC2."
    Tempel W., Khan M.B., Dong A., Hu J., Li Y., Bountra C., Arrowsmith C.H., Edwards A.M., Tong Y.
    Submitted (JUN-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 417-790, RCC1 REPEATS.
  20. "A homozygous missense mutation in HERC2 associated with global developmental delay and autism spectrum disorder."
    Puffenberger E.G., Jinks R.N., Wang H., Xin B., Fiorentini C., Sherman E.A., Degrazio D., Shaw C., Sougnez C., Cibulskis K., Gabriel S., Kelley R.I., Morton D.H., Strauss K.A.
    Hum. Mutat. 33:1639-1646(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MRT38 LEU-594, CHARACTERIZATION OF VARIANT MRT38 LEU-594.

Entry informationi

Entry nameiHERC2_HUMAN
AccessioniPrimary (citable) accession number: O95714
Secondary accession number(s): Q86SV7
, Q86SV8, Q86SV9, Q86YY3, Q86YY4, Q86YY5, Q86YY6, Q86YY7, Q86YY8, Q86YY9, Q86YZ0, Q86YZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 125 of the entry and version 2 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

Miscellaneous

A regulatory element withinin an intron of the HERC2 gene inhibits OCA2 promoter. There are several single nucleotide polymorphisms within the OCA2 gene and within the HERC2 gene that have a statistical association with human eye color.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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