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O95714

- HERC2_HUMAN

UniProt

O95714 - HERC2_HUMAN

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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 intermediate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2702 – 274948ZZ-type
Add
BLAST

GO - Molecular functioni

  1. SUMO binding Source: UniProtKB
  2. guanyl-nucleotide exchange factor activity Source: UniProtKB
  3. heme binding Source: InterPro
  4. ligase activity Source: UniProtKB-KW
  5. protein 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. DNA repair Source: UniProtKB
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. intracellular protein transport Source: UniProtKB
  4. protein ubiquitination Source: UniProtKB
  5. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
  6. regulation of GTPase activity Source: GOC
  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:HERC2
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.3 Publications

GO - Cellular componenti

  1. centriole Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB
  3. mitochondrial inner membrane Source: Ensembl
  4. 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 HERC2
PRO_0000229739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei647 – 6471Phosphothreonine1 Publication
Modified residuei1577 – 15771Phosphoserine By 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.
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

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.

Miscellaneous databases

EvolutionaryTraceiO95714.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati415 – 46147RCC1 1-1
Add
BLAST
Repeati462 – 51251RCC1 1-2
Add
BLAST
Repeati513 – 56856RCC1 1-3
Add
BLAST
Repeati569 – 62052RCC1 1-4
Add
BLAST
Repeati623 – 67452RCC1 1-5
Add
BLAST
Repeati675 – 72652RCC1 1-6
Add
BLAST
Repeati728 – 77851RCC1 1-7
Add
BLAST
Domaini1207 – 128377Cytochrome b5 heme-binding
Add
BLAST
Domaini1859 – 193274MIB/HERC2
Add
BLAST
Domaini2759 – 2936178DOC
Add
BLAST
Repeati2958 – 300952RCC1 2-1
Add
BLAST
Repeati3010 – 306455RCC1 2-2
Add
BLAST
Repeati3065 – 311652RCC1 2-3
Add
BLAST
Repeati3118 – 316851RCC1 2-4
Add
BLAST
Repeati3171 – 322252RCC1 2-5
Add
BLAST
Repeati3224 – 327451RCC1 2-6
Add
BLAST
Repeati3275 – 332652RCC1 2-7
Add
BLAST
Repeati3951 – 400252RCC1 3-1
Add
BLAST
Repeati4004 – 405653RCC1 3-2
Add
BLAST
Repeati4058 – 410851RCC1 3-3
Add
BLAST
Repeati4110 – 416253RCC1 3-4
Add
BLAST
Repeati4164 – 421451RCC1 3-5
Add
BLAST
Repeati4216 – 426651RCC1 3-6
Add
BLAST
Repeati4268 – 431851RCC1 3-7
Add
BLAST
Domaini4457 – 4794338HECT
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili948 – 98033 Reviewed prediction
Add
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 DOC domain.
Contains 1 MIB/HERC2 domain.
Contains 21 RCC1 repeats.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1053 – 10531L → W in AAD08657. 1 Publication
Sequence conflicti1150 – 11501G → D in AAD08657. 1 Publication
Sequence conflicti1354 – 13541S → R in AAD08657. 1 Publication
Sequence conflicti1566 – 15661T → M in AAD08657. 1 Publication
Sequence conflicti1753 – 17531K → T in AAD08657. 1 Publication
Sequence conflicti2444 – 24441R → H in AAD08657. 1 Publication
Sequence conflicti2881 – 28811C → Y in AAD08657. 1 Publication
Sequence conflicti3070 – 30701S → W in AAO27475. 1 Publication
Sequence conflicti3346 – 33461P → R in AAO27476. 1 Publication
Sequence conflicti3583 – 35842VA → MP in AAO27480. 1 Publication
Sequence conflicti3597 – 35971D → N in AAO27480. 1 Publication
Sequence conflicti3808 – 38081F → S in AAO27481. 1 Publication

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.
ENST00000576092; ENSP00000458767; ENSG00000263162.
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 .
ENST00000576092 ; ENSP00000458767 ; ENSG00000263162 .
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

« 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: September 3, 2014
This is version 123 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

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