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Q9NS91

- RAD18_HUMAN

UniProt

Q9NS91 - RAD18_HUMAN

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Protein

E3 ubiquitin-protein ligase RAD18

Gene

RAD18

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

Functioni

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.2 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri25 – 6440RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri201 – 22424UBZ-typeAdd
BLAST

GO - Molecular functioni

  1. damaged DNA binding Source: UniProtKB
  2. ligase activity Source: UniProtKB-KW
  3. polyubiquitin binding Source: UniProtKB
  4. ubiquitin protein ligase binding Source: UniProtKB
  5. Y-form DNA binding Source: UniProtKB
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA repair Source: UniProtKB
  2. negative regulation of DNA recombination Source: Ensembl
  3. protein ubiquitination Source: UniProtKB-UniPathway
  4. response to UV Source: Ensembl
  5. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RAD18
Synonyms:RNF73
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:18278. RAD18.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. chromatin Source: Ensembl
  2. nucleus Source: UniProtKB
  3. replication fork Source: UniProtKB
  4. XY body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271I → A: Lower activity toward PCNA monoubiquitination. 1 Publication

Organism-specific databases

PharmGKBiPA134912253.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495E3 ubiquitin-protein ligase RAD18PRO_0000056149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei99 – 991Phosphoserine6 Publications
Modified residuei103 – 1031Phosphoserine2 Publications
Modified residuei118 – 1181Phosphothreonine1 Publication
Modified residuei164 – 1641Phosphoserine1 Publication
Modified residuei471 – 4711Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NS91.
PaxDbiQ9NS91.
PeptideAtlasiQ9NS91.
PRIDEiQ9NS91.

PTM databases

PhosphoSiteiQ9NS91.

Expressioni

Gene expression databases

BgeeiQ9NS91.
CleanExiHS_RAD18.
ExpressionAtlasiQ9NS91. baseline and differential.
GenevestigatoriQ9NS91.

Organism-specific databases

HPAiHPA006716.
HPA008752.

Interactioni

Subunit structurei

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.6 Publications

Protein-protein interaction databases

BioGridi121212. 52 interactions.
DIPiDIP-29831N.
IntActiQ9NS91. 13 interactions.
MINTiMINT-3073564.
STRINGi9606.ENSP00000264926.

Structurei

Secondary structure

1
495
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 166Combined sources
Helixi17 – 226Combined sources
Turni26 – 283Combined sources
Beta strandi33 – 375Combined sources
Turni39 – 413Combined sources
Beta strandi44 – 463Combined sources
Helixi47 – 548Combined sources
Turni61 – 633Combined sources
Helixi69 – 713Combined sources
Helixi76 – 9015Combined sources
Helixi342 – 3454Combined sources
Helixi347 – 35812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MRFNMR-A198-227[»]
2Y43X-ray1.80A/B1-99[»]
2YBFX-ray2.00B340-366[»]
ProteinModelPortaliQ9NS91.
SMRiQ9NS91. Positions 8-95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini248 – 28235SAPPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi232 – 2409LR motif

Sequence similaritiesi

Belongs to the RAD18 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 1 SAP domain.PROSITE-ProRule annotation
Contains 1 UBZ-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri25 – 6440RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri201 – 22424UBZ-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5432.
GeneTreeiENSGT00390000011230.
HOGENOMiHOG000234845.
HOVERGENiHBG054721.
InParanoidiQ9NS91.
KOiK10627.
OMAiRHQEFVQ.
PhylomeDBiQ9NS91.
TreeFamiTF101214.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.30.40.10. 2 hits.
InterProiIPR003034. 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]
PfamiPF02037. SAP. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00513. SAP. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
PROSITEiPS50800. SAP. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NS91-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSLAESRWP PGLAVMKTID DLLRCGICFE YFNIAMIIPQ CSHNYCSLCI
60 70 80 90 100
RKFLSYKTQC PTCCVTVTEP DLKNNRILDE LVKSLNFARN HLLQFALESP
110 120 130 140 150
AKSPASSSSK NLAVKVYTPV ASRQSLKQGS RLMDNFLIRE MSGSTSELLI
160 170 180 190 200
KENKSKFSPQ KEASPAAKTK ETRSVEEIAP DPSEAKRPEP PSTSTLKQVT
210 220 230 240 250
KVDCPVCGVN IPESHINKHL DSCLSREEKK ESLRSSVHKR KPLPKTVYNL
260 270 280 290 300
LSDRDLKKKL KEHGLSIQGN KQQLIKRHQE FVHMYNAQCD ALHPKSAAEI
310 320 330 340 350
VREIENIEKT RMRLEASKLN ESVMVFTKDQ TEKEIDEIHS KYRKKHKSEF
360 370 380 390 400
QLLVDQARKG YKKIAGMSQK TVTITKEDES TEKLSSVCMG QEDNMTSVTN
410 420 430 440 450
HFSQSKLDSP EELEPDREED SSSCIDIQEV LSSSESDSCN SSSSDIIRDL
460 470 480 490
LEEEEAWEAS HKNDLQDTEI SPRQNRRTRA AESAEIEPRN KRNRN
Length:495
Mass (Da):56,223
Last modified:November 30, 2010 - v2
Checksum:i744A053A50C65DD7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911P → L in AAF80856. (PubMed:10908344)Curated
Sequence conflicti482 – 4843ESA → GKC in AAF80856. (PubMed:10908344)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61E → A.1 Publication
Corresponds to variant rs45520133 [ dbSNP | Ensembl ].
VAR_023423
Natural varianti302 – 3021R → Q.6 Publications
Corresponds to variant rs373572 [ dbSNP | Ensembl ].
VAR_023424
Natural varianti307 – 3071I → V.1 Publication
Corresponds to variant rs45569933 [ dbSNP | Ensembl ].
VAR_023425

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2571.1.
RefSeqiNP_064550.3. NM_020165.3.
UniGeneiHs.375684.

Genome annotation databases

EnsembliENST00000264926; ENSP00000264926; ENSG00000070950.
GeneIDi56852.
KEGGihsa:56852.
UCSCiuc003brd.3. human.

Polymorphism databases

DMDMi313104165.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS2571.1.
RefSeqi NP_064550.3. NM_020165.3.
UniGenei Hs.375684.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2MRF NMR - A 198-227 [» ]
2Y43 X-ray 1.80 A/B 1-99 [» ]
2YBF X-ray 2.00 B 340-366 [» ]
ProteinModelPortali Q9NS91.
SMRi Q9NS91. Positions 8-95.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121212. 52 interactions.
DIPi DIP-29831N.
IntActi Q9NS91. 13 interactions.
MINTi MINT-3073564.
STRINGi 9606.ENSP00000264926.

PTM databases

PhosphoSitei Q9NS91.

Polymorphism databases

DMDMi 313104165.

Proteomic databases

MaxQBi Q9NS91.
PaxDbi Q9NS91.
PeptideAtlasi Q9NS91.
PRIDEi Q9NS91.

Protocols and materials databases

DNASUi 56852.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264926 ; ENSP00000264926 ; ENSG00000070950 .
GeneIDi 56852.
KEGGi hsa:56852.
UCSCi uc003brd.3. human.

Organism-specific databases

CTDi 56852.
GeneCardsi GC03M008896.
H-InvDB HIX0003022.
HGNCi HGNC:18278. RAD18.
HPAi HPA006716.
HPA008752.
MIMi 605256. gene.
neXtProti NX_Q9NS91.
PharmGKBi PA134912253.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5432.
GeneTreei ENSGT00390000011230.
HOGENOMi HOG000234845.
HOVERGENi HBG054721.
InParanoidi Q9NS91.
KOi K10627.
OMAi RHQEFVQ.
PhylomeDBi Q9NS91.
TreeFami TF101214.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

GeneWikii RAD18.
GenomeRNAii 56852.
NextBioi 62262.
PROi Q9NS91.
SOURCEi Search...

Gene expression databases

Bgeei Q9NS91.
CleanExi HS_RAD18.
ExpressionAtlasi Q9NS91. baseline and differential.
Genevestigatori Q9NS91.

Family and domain databases

Gene3Di 1.10.720.30. 1 hit.
3.30.40.10. 2 hits.
InterProi IPR003034. 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 ]
Pfami PF02037. SAP. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
SM00513. SAP. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view ]
PROSITEi PS50800. SAP. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiRAD18_HUMAN
AccessioniPrimary (citable) accession number: Q9NS91
Secondary accession number(s): Q58F55, Q9NRT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 30, 2010
Last modified: November 26, 2014
This is version 127 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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