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Q9NS91 (RAD18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase RAD18

EC=6.3.2.-
Alternative name(s):
Postreplication repair protein RAD18
Short name=hHR18
Short name=hRAD18
RING finger protein 73
Gene names
Name:RAD18
Synonyms:RNF73
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity. Ref.11 Ref.20

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer. Interacts with UBE2A and UBE2B, one homodimer binding one molecule of UBE2B. Interacts with HLTF and SHPRH. Interacts with SPRTN; leading to enhance chromatin association of RAD18 and RAD18-mediated PCNA ubiquitination and translesion DNA synthesis. Ref.9 Ref.11 Ref.14 Ref.15 Ref.22 Ref.24

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the RAD18 family.

Contains 1 RING-type zinc finger.

Contains 1 SAP domain.

Contains 1 UBZ-type zinc finger.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of DNA recombination

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-UniPathway

response to UV

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentXY body

Inferred from electronic annotation. Source: Ensembl

chromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

replication fork

Inferred from direct assay PubMed 18363965. Source: UniProtKB

   Molecular_functionY-form DNA binding

Inferred from direct assay PubMed 18363965. Source: UniProtKB

damaged DNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

polyubiquitin binding

Inferred from direct assay Ref.21. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.2PubMed 18363965. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495E3 ubiquitin-protein ligase RAD18
PRO_0000056149

Regions

Domain248 – 28235SAP
Zinc finger25 – 6440RING-type
Zinc finger201 – 22424UBZ-type
Motif232 – 2409LR motif

Amino acid modifications

Modified residue11N-acetylmethionine Ref.23
Modified residue991Phosphoserine Ref.8 Ref.12 Ref.13 Ref.17 Ref.18 Ref.19
Modified residue1031Phosphoserine Ref.13 Ref.17
Modified residue1181Phosphothreonine Ref.13
Modified residue1641Phosphoserine Ref.13
Modified residue4711Phosphoserine Ref.10 Ref.18 Ref.19

Natural variations

Natural variant61E → A. Ref.5
Corresponds to variant rs45520133 [ dbSNP | Ensembl ].
VAR_023423
Natural variant3021R → Q. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Corresponds to variant rs373572 [ dbSNP | Ensembl ].
VAR_023424
Natural variant3071I → V. Ref.5
Corresponds to variant rs45569933 [ dbSNP | Ensembl ].
VAR_023425

Experimental info

Mutagenesis271I → A: Lower activity toward PCNA monoubiquitination. Ref.24
Sequence conflict1911P → L in AAF80856. Ref.2
Sequence conflict482 – 4843ESA → GKC in AAF80856. Ref.2

Secondary structure

....................... 495
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NS91 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 744A053A50C65DD7

FASTA49556,223
        10         20         30         40         50         60 
MDSLAESRWP PGLAVMKTID DLLRCGICFE YFNIAMIIPQ CSHNYCSLCI RKFLSYKTQC 

        70         80         90        100        110        120 
PTCCVTVTEP DLKNNRILDE LVKSLNFARN HLLQFALESP AKSPASSSSK NLAVKVYTPV 

       130        140        150        160        170        180 
ASRQSLKQGS RLMDNFLIRE MSGSTSELLI KENKSKFSPQ KEASPAAKTK ETRSVEEIAP 

       190        200        210        220        230        240 
DPSEAKRPEP PSTSTLKQVT KVDCPVCGVN IPESHINKHL DSCLSREEKK ESLRSSVHKR 

       250        260        270        280        290        300 
KPLPKTVYNL LSDRDLKKKL KEHGLSIQGN KQQLIKRHQE FVHMYNAQCD ALHPKSAAEI 

       310        320        330        340        350        360 
VREIENIEKT RMRLEASKLN ESVMVFTKDQ TEKEIDEIHS KYRKKHKSEF QLLVDQARKG 

       370        380        390        400        410        420 
YKKIAGMSQK TVTITKEDES TEKLSSVCMG QEDNMTSVTN HFSQSKLDSP EELEPDREED 

       430        440        450        460        470        480 
SSSCIDIQEV LSSSESDSCN SSSSDIIRDL LEEEEAWEAS HKNDLQDTEI SPRQNRRTRA 

       490 
AESAEIEPRN KRNRN 

« Hide

References

« Hide 'large scale' references
[1]"Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens."
Tateishi S., Sakuraba Y., Masuyama S., Inoue H., Yamaizumi M.
Proc. Natl. Acad. Sci. U.S.A. 97:7927-7932(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-302.
Tissue: Placenta.
[2]"The human RAD18 gene product interacts with HHR6A and HHR6B."
Xin H., Lin W., Sumanasekera W., Zhang Y., Wu X., Wang Z.
Nucleic Acids Res. 28:2847-2854(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-302.
[3]"Identification of human RAD18 (hHR18), a homolog of yeast RAD18."
Jang Y., Chae S.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-302.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-302.
[5]NIEHS SNPs program
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-6; GLN-302 AND VAL-307.
[6]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-302.
Tissue: Placenta.
[8]"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-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination."
Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.
J. Cell Biol. 175:703-708(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHPRH.
[10]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen."
Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V., Hurwitz J., Prakash L., Prakash S., Haracska L.
Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SHPRH.
[12]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-103; THR-118 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination."
Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L., Prakash S., Haracska L.
Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HLTF.
[15]"Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks."
Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.
Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HLTF.
[16]"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].
[17]"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-99 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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-99 AND SER-471, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-471, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling."
Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W., Elledge S.J.
Science 332:1313-1317(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[21]"Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks."
Panier S., Ichijima Y., Fradet-Turcotte A., Leung C.C., Kaustov L., Arrowsmith C.H., Durocher D.
Mol. Cell 47:383-395(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITIN-BINDING, LR MOTIF.
[22]"Spartan/C1orf124, a reader of PCNA ubiquitylation and a regulator of UV-induced DNA damage response."
Centore R.C., Yazinski S.A., Tse A., Zou L.
Mol. Cell 46:625-635(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPRTN.
[23]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Symmetry and asymmetry of the RING-RING dimer of Rad18."
Huang A., Hibbert R.G., de Jong R.N., Das D., Sixma T.K., Boelens R.
J. Mol. Biol. 410:424-435(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-99, SUBUNIT, MUTAGENESIS OF ILE-27.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB035274 mRNA. Translation: BAA99284.1.
AF169796 mRNA. Translation: AAF80856.1.
AY004333 mRNA. Translation: AAF86618.1.
AK023075 mRNA. Translation: BAB14392.1.
AY961989 Genomic DNA. Translation: AAX44049.1.
AC008151 Genomic DNA. No translation available.
AC034186 Genomic DNA. No translation available.
BC001302 mRNA. Translation: AAH01302.1.
RefSeqNP_064550.3. NM_020165.3.
UniGeneHs.375684.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y43X-ray1.80A/B1-99[»]
2YBFX-ray2.00B340-366[»]
ProteinModelPortalQ9NS91.
SMRQ9NS91. Positions 8-95.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121212. 43 interactions.
DIPDIP-29831N.
IntActQ9NS91. 13 interactions.
MINTMINT-3073564.
STRING9606.ENSP00000264926.

PTM databases

PhosphoSiteQ9NS91.

Polymorphism databases

DMDM313104165.

Proteomic databases

PaxDbQ9NS91.
PeptideAtlasQ9NS91.
PRIDEQ9NS91.

Protocols and materials databases

DNASU56852.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264926; ENSP00000264926; ENSG00000070950.
GeneID56852.
KEGGhsa:56852.
UCSCuc003brd.3. human.

Organism-specific databases

CTD56852.
GeneCardsGC03M008896.
H-InvDBHIX0003022.
HGNCHGNC:18278. RAD18.
HPAHPA006716.
HPA008752.
MIM605256. gene.
neXtProtNX_Q9NS91.
PharmGKBPA134912253.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5432.
HOGENOMHOG000234845.
HOVERGENHBG054721.
InParanoidQ9NS91.
KOK10627.
OMARHQEFVQ.
PhylomeDBQ9NS91.
TreeFamTF101214.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9NS91.
BgeeQ9NS91.
CleanExHS_RAD18.
GenevestigatorQ9NS91.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
3.30.40.10. 2 hits.
InterProIPR003034. SAP_dom.
IPR018957. Znf_C3HC4_RING-type.
IPR006642. Znf_Rad18_put.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF02037. SAP. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00513. SAP. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
PROSITEPS50800. SAP. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAD18.
GenomeRNAi56852.
NextBio62262.
PROQ9NS91.
SOURCESearch...

Entry information

Entry nameRAD18_HUMAN
AccessionPrimary (citable) accession number: Q9NS91
Secondary accession number(s): Q58F55, Q9NRT6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM