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Protein

E3 ubiquitin-protein ligase RFWD3

Gene

RFWD3

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

Functioni

E3 ubiquitin-protein ligase that mediates the ubiquitination of p53/TP53 in the late response to DNA damage, and acts as a positive regulator of p53/TP53 stability, thereby regulating the G1/S DNA damage checkpoint. May act by catalyzing the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. In response to ionizing radiation, interacts with MDM2 and enhances p53/TP53 ubiquitination, possibly by restricting MDM2 from extending polyubiquitin chains on ubiquitinated p53/TP53. Plays a role in RPA-mediated DNA damage signaling and repair.3 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri287 – 33145RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • MDM2/MDM4 family protein binding Source: UniProtKB
  • p53 binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • DNA repair Source: UniProtKB-KW
  • mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • mitotic G1 DNA damage checkpoint Source: UniProtKB
  • positive regulation of defense response to virus by host Source: ParkinsonsUK-UCL
  • protein ubiquitination Source: UniProtKB
  • regulation of DNA damage checkpoint Source: UniProtKB
  • response to ionizing radiation Source: UniProtKB
  • xenophagy Source: ParkinsonsUK-UCL
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

SignaLinkiQ6PCD5.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RFWD3 (EC:6.3.2.-)
Alternative name(s):
RING finger and WD repeat domain-containing protein 3
RING finger protein 201
Gene namesi
Name:RFWD3
Synonyms:RNF201
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:25539. RFWD3.

Subcellular locationi

  • Nucleus
  • NucleusPML body
  • Cytoplasm

  • Note: In undamaged cells, found both in the cytoplasm and in the nucleus, partially associated with PML nuclear bodies. In response to replication block, such as that caused by hydroxyurea treatment, or to DNA damage caused by ionizing radiations or doxorubicin, recruited to the nucleus, to stalled replication forks or to sites of DNA repair. This recruitment depends upon RPA2.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461S → A: Markedly decreases phosphorylation following ionizing radiation and abolishes ability to stimulate p53/TP53 ubiquitination; when associated with A-63. 1 Publication
Mutagenesisi63 – 631S → A: Markedly decreases phosphorylation following ionizing radiation and abolishes ability to stimulate p53/TP53 ubiquitination; when associated with A-46. 1 Publication
Mutagenesisi315 – 3151C → A: Abolishes ability to stimulate p53/TP53 ubiquitination. No effect on nuclear localization in response to DNA damage. 2 Publications

Organism-specific databases

PharmGKBiPA134960063.

Polymorphism and mutation databases

BioMutaiRFWD3.
DMDMi126253679.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 774774E3 ubiquitin-protein ligase RFWD3PRO_0000278234Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine; by ATM and ATR1 Publication
Modified residuei63 – 631Phosphoserine; by ATM and ATR1 Publication

Post-translational modificationi

Phosphorylated at Ser-46 and Ser-63 upon DNA damage by ATM or ATR. ATM phosphorylation occurs at early times upon DNA damage, while ATR is the major kinase at later times. Phosphorylation by ATM and ATR is required to stabilize p53/TP53. Part of the phosphorylation depends upon RPA2 presence.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6PCD5.
MaxQBiQ6PCD5.
PaxDbiQ6PCD5.
PeptideAtlasiQ6PCD5.
PRIDEiQ6PCD5.

PTM databases

iPTMnetiQ6PCD5.
PhosphoSiteiQ6PCD5.

Expressioni

Developmental stagei

Up-regulated in the S-G2 phase.1 Publication

Gene expression databases

BgeeiQ6PCD5.
CleanExiHS_RFWD3.
ExpressionAtlasiQ6PCD5. baseline and differential.
GenevisibleiQ6PCD5. HS.

Interactioni

Subunit structurei

Interacts with MDM2 and p53/TP53. Binds to the RPA complex via direct interaction with RPA2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBE2NP610882EBI-2129159,EBI-1052908

GO - Molecular functioni

  • MDM2/MDM4 family protein binding Source: UniProtKB
  • p53 binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120460. 51 interactions.
DIPiDIP-52688N.
IntActiQ6PCD5. 39 interactions.
STRINGi9606.ENSP00000354361.

Structurei

3D structure databases

ProteinModelPortaliQ6PCD5.
SMRiQ6PCD5. Positions 282-343, 479-621.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati495 – 53743WD 1Add
BLAST
Repeati539 – 57739WD 2Add
BLAST
Repeati583 – 62846WD 3Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili361 – 41353Sequence analysisAdd
BLAST

Domaini

The coiled coil domain may be involved in RPA2-binding.

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 3 WD repeats.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri287 – 33145RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, WD repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1645. Eukaryota.
ENOG410XPPE. LUCA.
GeneTreeiENSGT00390000008931.
HOVERGENiHBG093895.
InParanoidiQ6PCD5.
KOiK15691.
OMAiDTCAICF.
OrthoDBiEOG7XM2XD.
PhylomeDBiQ6PCD5.
TreeFamiTF323359.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6PCD5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHEAMEYDV QVQLNHAEQQ PAPAGMASSQ GGPALLQPVP ADVVSSQGVP
60 70 80 90 100
SILQPAPAEV ISSQATPPLL QPAPQLSVDL TEVEVLGEDT VENINPRTSE
110 120 130 140 150
QHRQGSDGNH TIPASSLHSM TNFISGLQRL HGMLEFLRPS SSNHSVGPMR
160 170 180 190 200
TRRRVSASRR ARAGGSQRTD SARLRAPLDA YFQVSRTQPD LPATTYDSET
210 220 230 240 250
RNPVSEELQV SSSSDSDSDS SAEYGGVVDQ AEESGAVILE EQLAGVSAEQ
260 270 280 290 300
EVTCIDGGKT LPKQPSPQKS EPLLPSASMD EEEGDTCTIC LEQWTNAGDH
310 320 330 340 350
RLSALRCGHL FGYRCISTWL KGQVRKCPQC NKKARHSDIV VLYARTLRAL
360 370 380 390 400
DTSEQERMKS SLLKEQMLRK QAELESAQCR LQLQVLTDKC TRLQRRVQDL
410 420 430 440 450
QKLTSHQSQN LQQPRGSQAW VLSCSPSSQG QHKHKYHFQK TFTVSQAGNC
460 470 480 490 500
RIMAYCDALS CLVISQPSPQ ASFLPGFGVK MLSTANMKSS QYIPMHGKQI
510 520 530 540 550
RGLAFSSYLR GLLLSASLDN TIKLTSLETN TVVQTYNAGR PVWSCCWCLD
560 570 580 590 600
EANYIYAGLA NGSILVYDVR NTSSHVQELV AQKARCPLVS LSYMPRAASA
610 620 630 640 650
AFPYGGVLAG TLEDASFWEQ KMDFSHWPHV LPLEPGGCID FQTENSSRHC
660 670 680 690 700
LVTYRPDKNH TTIRSVLMEM SYRLDDTGNP ICSCQPVHTF FGGPTCKLLT
710 720 730 740 750
KNAIFQSPEN DGNILVCTGD EAANSALLWD AASGSLLQDL QTDQPVLDIC
760 770
PFEVNRNSYL ATLTEKMVHI YKWE
Length:774
Mass (Da):85,094
Last modified:February 20, 2007 - v3
Checksum:iEF6E0E186FD2E580
GO

Sequence cautioni

The sequence BAA91662.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAF83889.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG38132.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti221 – 2211S → P in BAF83889 (PubMed:14702039).Curated
Sequence conflicti552 – 5521A → T in BAA91662 (PubMed:14702039).Curated
Sequence conflicti597 – 5971A → V in BAA91662 (PubMed:14702039).Curated
Sequence conflicti741 – 7411Q → R in BAB14169 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901T → N.
Corresponds to variant rs8058922 [ dbSNP | Ensembl ].
VAR_030700
Natural varianti392 – 3921R → K.1 Publication
Corresponds to variant rs17854997 [ dbSNP | Ensembl ].
VAR_030701
Natural varianti564 – 5641I → V.1 Publication
Corresponds to variant rs7193541 [ dbSNP | Ensembl ].
VAR_030702
Natural varianti770 – 7701I → T.1 Publication
Corresponds to variant rs17854996 [ dbSNP | Ensembl ].
VAR_030703

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001382 mRNA. Translation: BAA91662.1. Different initiation.
AK022673 mRNA. Translation: BAB14169.1.
AK291200 mRNA. Translation: BAF83889.1. Different initiation.
AK315786 mRNA. Translation: BAG38132.1. Different initiation.
AC109599 Genomic DNA. No translation available.
CH471114 Genomic DNA. Translation: EAW95680.1.
CH471114 Genomic DNA. Translation: EAW95681.1.
BC002574 mRNA. Translation: AAH02574.2.
BC059371 mRNA. Translation: AAH59371.2.
CCDSiCCDS32486.1.
RefSeqiNP_060594.3. NM_018124.3.
XP_005256078.1. XM_005256021.3.
XP_005256079.1. XM_005256022.3.
XP_011521493.1. XM_011523191.1.
UniGeneiHs.567525.

Genome annotation databases

EnsembliENST00000361070; ENSP00000354361; ENSG00000168411.
ENST00000571750; ENSP00000460049; ENSG00000168411.
GeneIDi55159.
KEGGihsa:55159.
UCSCiuc002fda.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001382 mRNA. Translation: BAA91662.1. Different initiation.
AK022673 mRNA. Translation: BAB14169.1.
AK291200 mRNA. Translation: BAF83889.1. Different initiation.
AK315786 mRNA. Translation: BAG38132.1. Different initiation.
AC109599 Genomic DNA. No translation available.
CH471114 Genomic DNA. Translation: EAW95680.1.
CH471114 Genomic DNA. Translation: EAW95681.1.
BC002574 mRNA. Translation: AAH02574.2.
BC059371 mRNA. Translation: AAH59371.2.
CCDSiCCDS32486.1.
RefSeqiNP_060594.3. NM_018124.3.
XP_005256078.1. XM_005256021.3.
XP_005256079.1. XM_005256022.3.
XP_011521493.1. XM_011523191.1.
UniGeneiHs.567525.

3D structure databases

ProteinModelPortaliQ6PCD5.
SMRiQ6PCD5. Positions 282-343, 479-621.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120460. 51 interactions.
DIPiDIP-52688N.
IntActiQ6PCD5. 39 interactions.
STRINGi9606.ENSP00000354361.

PTM databases

iPTMnetiQ6PCD5.
PhosphoSiteiQ6PCD5.

Polymorphism and mutation databases

BioMutaiRFWD3.
DMDMi126253679.

Proteomic databases

EPDiQ6PCD5.
MaxQBiQ6PCD5.
PaxDbiQ6PCD5.
PeptideAtlasiQ6PCD5.
PRIDEiQ6PCD5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361070; ENSP00000354361; ENSG00000168411.
ENST00000571750; ENSP00000460049; ENSG00000168411.
GeneIDi55159.
KEGGihsa:55159.
UCSCiuc002fda.4. human.

Organism-specific databases

CTDi55159.
GeneCardsiRFWD3.
H-InvDBHIX0013236.
HGNCiHGNC:25539. RFWD3.
MIMi614151. gene.
neXtProtiNX_Q6PCD5.
PharmGKBiPA134960063.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1645. Eukaryota.
ENOG410XPPE. LUCA.
GeneTreeiENSGT00390000008931.
HOVERGENiHBG093895.
InParanoidiQ6PCD5.
KOiK15691.
OMAiDTCAICF.
OrthoDBiEOG7XM2XD.
PhylomeDBiQ6PCD5.
TreeFamiTF323359.

Enzyme and pathway databases

UniPathwayiUPA00143.
SignaLinkiQ6PCD5.

Miscellaneous databases

GenomeRNAii55159.
PROiQ6PCD5.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PCD5.
CleanExiHS_RFWD3.
ExpressionAtlasiQ6PCD5. baseline and differential.
GenevisibleiQ6PCD5. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00320. WD40. 3 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Teratocarcinoma and Trachea.
  2. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-564.
  4. "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], VARIANTS LYS-392 AND THR-770.
    Tissue: Brain and Testis.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "RFWD3-Mdm2 ubiquitin ligase complex positively regulates p53 stability in response to DNA damage."
    Fu X., Yucer N., Liu S., Li M., Yi P., Mu J.J., Yang T., Chu J., Jung S.Y., O'Malley B.W., Gu W., Qin J., Wang Y.
    Proc. Natl. Acad. Sci. U.S.A. 107:4579-4584(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-46 AND SER-63, MUTAGENESIS OF SER-46; SER-63 AND CYS-315.
  7. "E3 ligase RFWD3 participates in replication checkpoint control."
    Gong Z., Chen J.
    J. Biol. Chem. 286:22308-22313(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPA2, SUBCELLULAR LOCATION.
  8. "RING finger and WD repeat domain 3 (RFWD3) associates with replication protein A (RPA) and facilitates RPA-mediated DNA damage response."
    Liu S., Chu J., Yucer N., Leng M., Wang S.Y., Chen B.P., Hittelman W.N., Wang Y.
    J. Biol. Chem. 286:22314-22322(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPA2, SUBCELLULAR LOCATION, PHOSPHORYLATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-315.
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.

Entry informationi

Entry nameiRFWD3_HUMAN
AccessioniPrimary (citable) accession number: Q6PCD5
Secondary accession number(s): A8K585
, B2RE35, D3DUJ8, Q5XKR3, Q9H9Q3, Q9NVT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: July 6, 2016
This is version 120 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.