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O95714

- HERC2_HUMAN

UniProt

O95714 - HERC2_HUMAN

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
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    5. SUMO binding Source: UniProtKB
    6. ubiquitin protein ligase binding Source: UniProtKB
    7. ubiquitin-protein transferase activity Source: UniProtKB
    8. 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

    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. centriole Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB
    3. membrane Source: UniProtKB
    4. mitochondrial inner membrane Source: Ensembl
    5. nucleus Source: UniProtKB

    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

    ArrayExpressiO95714.
    BgeeiO95714.
    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. 45 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.
    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

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    MPSESFCLAA QARLDSKWLK TDIQLAFTRD GLCGLWNEMV KDGEIVYTGT     50
    ESTQNGELPP RKDDSVEPSG TKKEDLNDKE KKDEEETPAP IYRAKSILDS 100
    WVWGKQPDVN ELKECLSVLV KEQQALAVQS ATTTLSALRL KQRLVILERY 150
    FIALNRTVFQ ENVKVKWKSS GISLPPVDKK SSRPAGKGVE GLARVGSRAA 200
    LSFAFAFLRR AWRSGEDADL CSELLQESLD ALRALPEASL FDESTVSSVW 250
    LEVVERATRF LRSVVTGDVH GTPATKGPGS IPLQDQHLAL AILLELAVQR 300
    GTLSQMLSAI LLLLQLWDSG AQETDNERSA QGTSAPLLPL LQRFQSIICR 350
    KDAPHSEGDM HLLSGPLSPN ESFLRYLTLP QDNELAIDLR QTAVVVMAHL 400
    DRLATPCMPP LCSSPTSHKG SLQEVIGWGL IGWKYYANVI GPIQCEGLAN 450
    LGVTQIACAE KRFLILSRNG RVYTQAYNSD TLAPQLVQGL ASRNIVKIAA 500
    HSDGHHYLAL AATGEVYSWG CGDGGRLGHG DTVPLEEPKV ISAFSGKQAG 550
    KHVVHIACGS TYSAAITAEG ELYTWGRGNY GRLGHGSSED EAIPMLVAGL 600
    KGLKVIDVAC GSGDAQTLAV TENGQVWSWG DGDYGKLGRG GSDGCKTPKL 650
    IEKLQDLDVV KVRCGSQFSI ALTKDGQVYS WGKGDNQRLG HGTEEHVRYP 700
    KLLEGLQGKK VIDVAAGSTH CLALTEDSEV HSWGSNDQCQ HFDTLRVTKP 750
    EPAALPGLDT KHIVGIACGP AQSFAWSSCS EWSIGLRVPF VVDICSMTFE 800
    QLDLLLRQVS EGMDGSADWP PPQEKECVAV ATLNLLRLQL HAAISHQVDP 850
    EFLGLGLGSI LLNSLKQTVV TLASSAGVLS TVQSAAQAVL QSGWSVLLPT 900
    AEERARALSA LLPCAVSGNE VNISPGRRFM IDLLVGSLMA DGGLESALHA 950
    AITAEIQDIE AKKEAQKEKE IDEQEANAST FHRSRTPLDK DLINTGICES 1000
    SGKQCLPLVQ LIQQLLRNIA SQTVARLKDV ARRISSCLDF EQHSRERSAS 1050
    LDLLLRFQRL LISKLYPGES IGQTSDISSP ELMGVGSLLK KYTALLCTHI 1100
    GDILPVAASI ASTSWRHFAE VAYIVEGDFT GVLLPELVVS IVLLLSKNAG 1150
    LMQEAGAVPL LGGLLEHLDR FNHLAPGKER DDHEELAWPG IMESFFTGQN 1200
    CRNNEEVTLI RKADLENHNK DGGFWTVIDG KVYDIKDFQT QSLTGNSILA 1250
    QFAGEDPVVA LEAALQFEDT RESMHAFCVG QYLEPDQEIV TIPDLGSLSS 1300
    PLIDTERNLG LLLGLHASYL AMSTPLSPVE IECAKWLQSS IFSGGLQTSQ 1350
    IHYSYNEEKD EDHCSSPGGT PASKSRLCSH RRALGDHSQA FLQAIADNNI 1400
    QDHNVKDFLC QIERYCRQCH LTTPIMFPPE HPVEEVGRLL LCCLLKHEDL 1450
    GHVALSLVHA GALGIEQVKH RTLPKSVVDV CRVVYQAKCS LIKTHQEQGR 1500
    SYKEVCAPVI ERLRFLFNEL RPAVCNDLSI MSKFKLLSSL PRWRRIAQKI 1550
    IRERRKKRVP KKPESTDDEE KIGNEESDLE EACILPHSPI NVDKRPIAIK 1600
    SPKDKWQPLL STVTGVHKYK WLKQNVQGLY PQSPLLSTIA EFALKEEPVD 1650
    VEKMRKCLLK QLERAEVRLE GIDTILKLAS KNFLLPSVQY AMFCGWQRLI 1700
    PEGIDIGEPL TDCLKDVDLI PPFNRMLLEV TFGKLYAWAV QNIRNVLMDA 1750
    SAKFKELGIQ PVPLQTITNE NPSGPSLGTI PQARFLLVML SMLTLQHGAN 1800
    NLDLLLNSGM LALTQTALRL IGPSCDNVEE DMNASAQGAS ATVLEETRKE 1850
    TAPVQLPVSG PELAAMMKIG TRVMRGVDWK WGDQDGPPPG LGRVIGELGE 1900
    DGWIRVQWDT GSTNSYRMGK EGKYDLKLAE LPAAAQPSAE DSDTEDDSEA 1950
    EQTERNIHPT AMMFTSTINL LQTLCLSAGV HAEIMQSEAT KTLCGLLRML 2000
    VESGTTDKTS SPNRLVYREQ HRSWCTLGFV RSIALTPQVC GALSSPQWIT 2050
    LLMKVVEGHA PFTATSLQRQ ILAVHLLQAV LPSWDKTERA RDMKCLVEKL 2100
    FDFLGSLLTT CSSDVPLLRE STLRRRRVRP QASLTATHSS TLAEEVVALL 2150
    RTLHSLTQWN GLINKYINSQ LRSITHSFVG RPSEGAQLED YFPDSENPEV 2200
    GGLMAVLAVI GGIDGRLRLG GQVMHDEFGE GTVTRITPKG KITVQFSDMR 2250
    TCRVCPLNQL KPLPAVAFNV NNLPFTEPML SVWAQLVNLA GSKLEKHKIK 2300
    KSTKQAFAGQ VDLDLLRCQQ LKLYILKAGR ALLSHQDKLR QILSQPAVQE 2350
    TGTVHTDDGA VVSPDLGDMS PEGPQPPMIL LQQLLASATQ PSPVKAIFDK 2400
    QELEAAALAV CQCLAVESTH PSSPGFEDCS SSEATTPVAV QHIRPARVKR 2450
    RKQSPVPALP IVVQLMEMGF SRRNIEFALK SLTGASGNAS SLPGVEALVG 2500
    WLLDHSDIQV TELSDADTVS DEYSDEEVVE DVDDAAYSMS TGAVVTESQT 2550
    YKKRADFLSN DDYAVYVREN IQVGMMVRCC RAYEEVCEGD VGKVIKLDRD 2600
    GLHDLNVQCD WQQKGGTYWV RYIHVELIGY PPPSSSSHIK IGDKVRVKAS 2650
    VTTPKYKWGS VTHQSVGVVK AFSANGKDII VDFPQQSHWT GLLSEMELVP 2700
    SIHPGVTCDG CQMFPINGSR FKCRNCDDFD FCETCFKTKK HNTRHTFGRI 2750
    NEPGQSAVFC GRSGKQLKRC HSSQPGMLLD SWSRMVKSLN VSSSVNQASR 2800
    LIDGSEPCWQ SSGSQGKHWI RLEIFPDVLV HRLKMIVDPA DSSYMPSLVV 2850
    VSGGNSLNNL IELKTININP SDTTVPLLND CTEYHRYIEI AIKQCRSSGI 2900
    DCKIHGLILL GRIRAEEEDL AAVPFLASDN EEEEDEKGNS GSLIRKKAAG 2950
    LESAATIRTK VFVWGLNDKD QLGGLKGSKI KVPSFSETLS ALNVVQVAGG 3000
    SKSLFAVTVE GKVYACGEAT NGRLGLGISS GTVPIPRQIT ALSSYVVKKV 3050
    AVHSGGRHAT ALTVDGKVFS WGEGDDGKLG HFSRMNCDKP RLIEALKTKR 3100
    IRDIACGSSH SAALTSSGEL YTWGLGEYGR LGHGDNTTQL KPKMVKVLLG 3150
    HRVIQVACGS RDAQTLALTD EGLVFSWGDG DFGKLGRGGS EGCNIPQNIE 3200
    RLNGQGVCQI ECGAQFSLAL TKSGVVWTWG KGDYFRLGHG SDVHVRKPQV 3250
    VEGLRGKKIV HVAVGALHCL AVTDSGQVYA WGDNDHGQQG NGTTTVNRKP 3300
    TLVQGLEGQK ITRVACGSSH SVAWTTVDVA TPSVHEPVLF QTARDPLGAS 3350
    YLGVPSDADS SAASNKISGA SNSKPNRPSL AKILLSLDGN LAKQQALSHI 3400
    LTALQIMYAR DAVVGALMPA AMIAPVECPS FSSAAPSDAS AMASPMNGEE 3450
    CMLAVDIEDR LSPNPWQEKR EIVSSEDAVT PSAVTPSAPS ASARPFIPVT 3500
    DDLGAASIIA ETMTKTKEDV ESQNKAAGPE PQALDEFTSL LIADDTRVVV 3550
    DLLKLSVCSR AGDRGRDVLS AVLSGMGTAY PQVADMLLEL CVTELEDVAT 3600
    DSQSGRLSSQ PVVVESSHPY TDDTSTSGTV KIPGAEGLRV EFDRQCSTER 3650
    RHDPLTVMDG VNRIVSVRSG REWSDWSSEL RIPGDELKWK FISDGSVNGW 3700
    GWRFTVYPIM PAAGPKELLS DRCVLSCPSM DLVTCLLDFR LNLASNRSIV 3750
    PRLAASLAAC AQLSALAASH RMWALQRLRK LLTTEFGQSI NINRLLGEND 3800
    GETRALSFTG SALAALVKGL PEALQRQFEY EDPIVRGGKQ LLHSPFFKVL 3850
    VALACDLELD TLPCCAETHK WAWFRRYCMA SRVAVALDKR TPLPRLFLDE 3900
    VAKKIRELMA DSENMDVLHE SHDIFKREQD EQLVQWMNRR PDDWTLSAGG 3950
    SGTIYGWGHN HRGQLGGIEG AKVKVPTPCE ALATLRPVQL IGGEQTLFAV 4000
    TADGKLYATG YGAGGRLGIG GTESVSTPTL LESIQHVFIK KVAVNSGGKH 4050
    CLALSSEGEV YSWGEAEDGK LGHGNRSPCD RPRVIESLRG IEVVDVAAGG 4100
    AHSACVTAAG DLYTWGKGRY GRLGHSDSED QLKPKLVEAL QGHRVVDIAC 4150
    GSGDAQTLCL TDDDTVWSWG DGDYGKLGRG GSDGCKVPMK IDSLTGLGVV 4200
    KVECGSQFSV ALTKSGAVYT WGKGDYHRLG HGSDDHVRRP RQVQGLQGKK 4250
    VIAIATGSLH CVCCTEDGEV YTWGDNDEGQ LGDGTTNAIQ RPRLVAALQG 4300
    KKVNRVACGS AHTLAWSTSK PASAGKLPAQ VPMEYNHLQE IPIIALRNRL 4350
    LLLHHLSELF CPCIPMFDLE GSLDETGLGP SVGFDTLRGI LISQGKEAAF 4400
    RKVVQATMVR DRQHGPVVEL NRIQVKRSRS KGGLAGPDGT KSVFGQMCAK 4450
    MSSFGPDSLL LPHRVWKVKF VGESVDDCGG GYSESIAEIC EELQNGLTPL 4500
    LIVTPNGRDE SGANRDCYLL SPAARAPVHS SMFRFLGVLL GIAIRTGSPL 4550
    SLNLAEPVWK QLAGMSLTIA DLSEVDKDFI PGLMYIRDNE ATSEEFEAMS 4600
    LPFTVPSASG QDIQLSSKHT HITLDNRAEY VRLAINYRLH EFDEQVAAVR 4650
    EGMARVVPVP LLSLFTGYEL ETMVCGSPDI PLHLLKSVAT YKGIEPSASL 4700
    IQWFWEVMES FSNTERSLFL RFVWGRTRLP RTIADFRGRD FVIQVLDKYN 4750
    PPDHFLPESY TCFFLLKLPR YSCKQVLEEK LKYAIHFCKS IDTDDYARIA 4800
    LTGEPAADDS SDDSDNEDVD SFASDSTQDY LTGH 4834
    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. 45 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.
    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

    ArrayExpressi O95714.
    Bgeei O95714.
    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

    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 1, 2014
    This is version 124 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