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Protein

RPA-interacting protein

Gene

Rpain

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Mediates the import of RPA complex into the nucleus, possibly via some interaction with importin beta. Sumoylation mediates the localization of RPA complex into the PML body of the nucleus, thereby participating in RPA function in DNA metabolism (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri137 – 21276RIP-typeAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
RPA-interacting protein
Gene namesi
Name:Rpain
Synonyms:Rip
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1308492. Rpain.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219RPA-interacting proteinPRO_0000076301Add
BLAST

Post-translational modificationi

Sumoylated; required for localization in the nuclear PML body and transport of RPA complex in PML body. Upon UV irradiation and during S phase, it is desumoylated, releasing RPA complex that is translocated to sites of DNA damage. Sumoylation takes place at different Lys residues (By similarity).By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ4G2Y1.

PTM databases

iPTMnetiQ4G2Y1.

Interactioni

Subunit structurei

Interacts with the RPA1 subunit of RPA complex.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009082.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 18017Mediates nuclear exportBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 RIP-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri137 – 21276RIP-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IX54. Eukaryota.
ENOG4111K6G. LUCA.
GeneTreeiENSGT00390000006416.
HOGENOMiHOG000251596.
HOVERGENiHBG082800.
InParanoidiQ4G2Y1.
OMAiEKCLSIM.
OrthoDBiEOG7673BZ.
PhylomeDBiQ4G2Y1.
TreeFamiTF326215.

Family and domain databases

InterProiIPR028156. RIP.
IPR028159. RPA_interact_C_dom.
IPR028155. RPA_interact_central.
IPR028158. RPA_interact_N_dom.
[Graphical view]
PANTHERiPTHR31742. PTHR31742. 1 hit.
PfamiPF14768. RPA_interact_C. 1 hit.
PF14767. RPA_interact_M. 1 hit.
PF14766. RPA_interact_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q4G2Y1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAESSGSPHR LLYKQVGSPP WKETFRQGCL ERMRNSRHKL LNRYRQAAGS
60 70 80 90 100
TLGTASDRLL VQEVMEEEWN SLQSVENCPE ALLQLELPLN LAVLQDIEQE
110 120 130 140 150
LWNEEKSIIS EYEKGLQFDE SCLNSMLAEW EANPLICPVC IKYNLRIMNS
160 170 180 190 200
VVTCPCGLHI PSHSTDLTEQ KLRACLEGNV NEHSAHCPHI PEFSVTGGTE
210
EKPSLLMSCL ACDTWAVIL
Length:219
Mass (Da):24,710
Last modified:December 6, 2005 - v2
Checksum:iE24EAF7CABEA2A8D
GO
Isoform 2 (identifier: Q4G2Y1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     212-219: CDTWAVIL → YKLHC

Show »
Length:216
Mass (Da):24,453
Checksum:iEFD96CA308051679
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431R → T in CF978727 (PubMed:15277470).Curated
Sequence conflicti58 – 581R → G in CF978727 (PubMed:15277470).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei212 – 2198CDTWAVIL → YKLHC in isoform 2. 1 PublicationVSP_016411

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY775322 mRNA. Translation: AAX14376.1.
AABR03073214 Genomic DNA. No translation available.
CF978727 mRNA. No translation available.
RefSeqiNP_001028232.1. NM_001033060.1. [Q4G2Y1-2]
XP_006246730.1. XM_006246668.2. [Q4G2Y1-1]
UniGeneiRn.43464.

Genome annotation databases

EnsembliENSRNOT00000009082; ENSRNOP00000009082; ENSRNOG00000006913. [Q4G2Y1-1]
ENSRNOT00000044363; ENSRNOP00000040269; ENSRNOG00000006913. [Q4G2Y1-2]
GeneIDi287463.
KEGGirno:287463.
UCSCiRGD:1308492. rat. [Q4G2Y1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY775322 mRNA. Translation: AAX14376.1.
AABR03073214 Genomic DNA. No translation available.
CF978727 mRNA. No translation available.
RefSeqiNP_001028232.1. NM_001033060.1. [Q4G2Y1-2]
XP_006246730.1. XM_006246668.2. [Q4G2Y1-1]
UniGeneiRn.43464.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009082.

PTM databases

iPTMnetiQ4G2Y1.

Proteomic databases

PaxDbiQ4G2Y1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009082; ENSRNOP00000009082; ENSRNOG00000006913. [Q4G2Y1-1]
ENSRNOT00000044363; ENSRNOP00000040269; ENSRNOG00000006913. [Q4G2Y1-2]
GeneIDi287463.
KEGGirno:287463.
UCSCiRGD:1308492. rat. [Q4G2Y1-1]

Organism-specific databases

CTDi84268.
RGDi1308492. Rpain.

Phylogenomic databases

eggNOGiENOG410IX54. Eukaryota.
ENOG4111K6G. LUCA.
GeneTreeiENSGT00390000006416.
HOGENOMiHOG000251596.
HOVERGENiHBG082800.
InParanoidiQ4G2Y1.
OMAiEKCLSIM.
OrthoDBiEOG7673BZ.
PhylomeDBiQ4G2Y1.
TreeFamiTF326215.

Miscellaneous databases

PROiQ4G2Y1.

Family and domain databases

InterProiIPR028156. RIP.
IPR028159. RPA_interact_C_dom.
IPR028155. RPA_interact_central.
IPR028158. RPA_interact_N_dom.
[Graphical view]
PANTHERiPTHR31742. PTHR31742. 1 hit.
PfamiPF14768. RPA_interact_C. 1 hit.
PF14767. RPA_interact_M. 1 hit.
PF14766. RPA_interact_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, expression pattern, and subcellular location of human RIP isoforms."
    Chen J.-Z., Huang S.-D., Ji C.-N., Pang R.-Y., Xie Y., Xue J.-L.
    DNA Cell Biol. 24:464-469(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Gene expression profiling of purified rat retinal ganglion cells."
    Farkas R.H., Qian J., Goldberg J.L., Quigley H.A., Zack D.J.
    Invest. Ophthalmol. Vis. Sci. 45:2503-2513(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-219 (ISOFORM 1).

Entry informationi

Entry nameiRIP_RAT
AccessioniPrimary (citable) accession number: Q4G2Y1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: June 8, 2016
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.