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Q86UA6 (RIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RPA-interacting protein

Short name=hRIP
Gene names
Name:RPAIN
Synonyms:RIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the import of RPA complex into the nucleus, possibly via some interaction with importin beta. Isoform 2 is sumoylated and mediates the localization of RPA complex into the PML body of the nucleus, thereby participating in RPA function in DNA metabolism. Ref.2

Subunit structure

Interacts with the RPA1 subunit of RPA complex. Ref.2

Subcellular location

Isoform 1: Cytoplasm. Nucleus Ref.1 Ref.2.

Isoform 2: NucleusPML body Ref.1 Ref.2.

Tissue specificity

Widely expressed. Expressed in pancreas, kidney, muscle, liver, lung, placenta, brain, heart, leukocytes, colon, intestine, ovary, testis, prostate, thymus and spleen. Ref.1

Post-translational modification

Isoform 2 is sumoylated. Sumoylation is 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. Ref.2

Sequence similarities

Contains 1 RIP-type zinc finger.

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86UA6-1)

Also known as: Alpha; hRIPalpha;

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.
Note: Major isoform with isoform 2.
Isoform 2 (identifier: Q86UA6-2)

Also known as: Beta; hRIPbeta;

The sequence of this isoform differs from the canonical sequence as follows:
     164-210: Missing.
Note: Major isoform with isoform 1.
Isoform 3 (identifier: Q86UA6-3)

Also known as: Gamma2;

The sequence of this isoform differs from the canonical sequence as follows:
     143-219: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. May be due to an intron retention.
Isoform 4 (identifier: Q86UA6-4)

Also known as: Gamma1;

The sequence of this isoform differs from the canonical sequence as follows:
     142-145: KYNL → NLLS
     146-219: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 5 (identifier: Q86UA6-5)

Also known as: Delta2;

The sequence of this isoform differs from the canonical sequence as follows:
     105-106: EQ → VF
     107-219: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 6 (identifier: Q86UA6-6)

Also known as: Delta3;

The sequence of this isoform differs from the canonical sequence as follows:
     105-106: EQ → GL
     107-219: Missing.
Isoform 7 (identifier: Q86UA6-7)

Also known as: Delta1; Delta 4;

The sequence of this isoform differs from the canonical sequence as follows:
     105-107: EQS → GTT
     108-219: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 8 (identifier: Q86UA6-8)

The sequence of this isoform differs from the canonical sequence as follows:
     211-219: ACDTWAVIL → VSVSWDPLCGKRDLWLVLFPP
Note: No experimental confirmation available.
Isoform 9 (identifier: Q86UA6-9)

The sequence of this isoform differs from the canonical sequence as follows:
     143-219: YNLRITSGVV...LACDTWAVIL → PVILGL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 219219RPA-interacting protein
PRO_0000076299

Regions

Zinc finger137 – 21276RIP-type
Region164 – 18017Mediates nuclear export

Amino acid modifications

Cross-link103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); in isoform 2 Probable
Cross-link121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); in isoform 2 Probable

Natural variations

Alternative sequence105 – 1073EQS → GTT in isoform 7.
VSP_016402
Alternative sequence105 – 1062EQ → VF in isoform 5.
VSP_016403
Alternative sequence105 – 1062EQ → GL in isoform 6.
VSP_016404
Alternative sequence107 – 219113Missing in isoform 5 and isoform 6.
VSP_016405
Alternative sequence108 – 219112Missing in isoform 7.
VSP_016406
Alternative sequence142 – 1454KYNL → NLLS in isoform 4.
VSP_016407
Alternative sequence143 – 21977Missing in isoform 3.
VSP_016408
Alternative sequence143 – 21977YNLRI…WAVIL → PVILGL in isoform 9.
VSP_046795
Alternative sequence146 – 21974Missing in isoform 4.
VSP_016409
Alternative sequence164 – 21047Missing in isoform 2.
VSP_016410
Alternative sequence211 – 2199ACDTWAVIL → VSVSWDPLCGKRDLWLVLFP P in isoform 8.
VSP_045356
Natural variant1031K → N Common polymorphism; results in a decrease in sumoylation. Ref.2 Ref.3 Ref.5
Corresponds to variant rs12761 [ dbSNP | Ensembl ].
VAR_023947

Experimental info

Mutagenesis1141K → R: Abolishes sumoylation; when associated with N-103; R-121 and R-142. Ref.2
Mutagenesis1211K → R: Induces a strong decrease in sumoylation; when associated with N-103. Abolishes sumoylation; when associated with N-103; R-114 and R-142. Ref.2
Mutagenesis1421K → R: Abolishes sumoylation; when associated with N-103; R-114 and R-121. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) (hRIPalpha) [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 4AF573893850704E

FASTA21924,784
        10         20         30         40         50         60 
MAESLRSPRR SLYKLVGSPP WKEAFRQRCL ERMRNSRDRL LNRYRQAGSS GPGNSQNSFL 

        70         80         90        100        110        120 
VQEVMEEEWN ALQSVENCPE DLAQLEELID MAVLEEIQQE LIKQEQSIIS EYEKSLQFDE 

       130        140        150        160        170        180 
KCLSIMLAEW EANPLICPVC TKYNLRITSG VVVCQCGLSI PSHSSELTEQ KLRACLEGSI 

       190        200        210 
NEHSAHCPHT PEFSVTGGTE EKSSLLMSCL ACDTWAVIL 

« Hide

Isoform 2 (Beta) (hRIPbeta) [UniParc].

Checksum: 0B6AA34C1429D384
Show »

FASTA17219,727
Isoform 3 (Gamma2) [UniParc].

Checksum: B08C00B3708D8E58
Show »

FASTA14216,525
Isoform 4 (Gamma1) [UniParc].

Checksum: A7977D77FC00B370
Show »

FASTA14516,824
Isoform 5 (Delta2) [UniParc].

Checksum: 184280661713B68C
Show »

FASTA10612,399
Isoform 6 (Delta3) [UniParc].

Checksum: 16B830661713B68C
Show »

FASTA10612,323
Isoform 7 (Delta1) (Delta 4) [UniParc].

Checksum: A2803830661713B6
Show »

FASTA10712,412
Isoform 8 [UniParc].

Checksum: 224CC8977EF906E9
Show »

FASTA23126,221
Isoform 9 [UniParc].

Checksum: 67DFE6F2628D308C
Show »

FASTA14817,118

References

« Hide 'large scale' references
[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] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Sumoylation of the novel protein hRIPbeta is involved in replication protein A deposition in PML nuclear bodies."
Park J., Seo T., Kim H., Choe J.
Mol. Cell. Biol. 25:8202-8214(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6 AND 7), FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-103 AND LYS-121, INTERACTION WITH RPA1, MUTAGENESIS OF LYS-114; LYS-121 AND LYS-142, VARIANT ASN-103.
[3]"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] (ISOFORMS 3 AND 8), VARIANT ASN-103.
Tissue: Corpus callosum and Placenta.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1; 4 AND 6), VARIANT ASN-103.
Tissue: Eye.
[6]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY775314 mRNA. Translation: AAX14368.1.
AY775315 mRNA. Translation: AAX14369.1.
AY775316 mRNA. Translation: AAX14370.1.
AY775317 mRNA. Translation: AAX14371.1.
AY775318 mRNA. Translation: AAX14372.1.
AY775319 mRNA. Translation: AAX14373.1.
AY775320 mRNA. Translation: AAX14374.1.
AY775321 mRNA. Translation: AAX14375.1.
AY775323 mRNA. Translation: AAX14377.1.
AY680654 mRNA. Translation: AAT80872.1.
AY680655 mRNA. Translation: AAT80873.1.
AY680656 mRNA. Translation: AAT80874.1.
AY680657 mRNA. Translation: AAT80875.1.
AY680658 mRNA. Translation: AAT80876.1.
AY680659 mRNA. Translation: AAT80877.1.
AY680660 mRNA. Translation: AAT80878.1.
AK295394 mRNA. Translation: BAG58348.1.
AK300409 mRNA. Translation: BAG62139.1.
AC004148 Genomic DNA. No translation available.
BC004451 mRNA. Translation: AAH04451.1.
BC046349 mRNA. Translation: AAH46349.1.
BC051849 mRNA. Translation: AAH51849.1.
RefSeqNP_001028174.2. NM_001033002.3.
NP_001153715.1. NM_001160243.1.
NP_001153716.1. NM_001160244.1.
NP_001153718.1. NM_001160246.1.
NP_001153738.1. NM_001160266.1.
UniGeneHs.462086.
Hs.555866.

3D structure databases

ProteinModelPortalQ86UA6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123995. 5 interactions.
IntActQ86UA6. 4 interactions.

PTM databases

PhosphoSiteQ86UA6.

Polymorphism databases

DMDM74727468.

Proteomic databases

PaxDbQ86UA6.
PRIDEQ86UA6.

Protocols and materials databases

DNASU84268.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000536255; ENSP00000439939; ENSG00000129197.
ENST00000539417; ENSP00000446453; ENSG00000129197.
GeneID84268.
KEGGhsa:84268.

Organism-specific databases

CTD84268.
GeneCardsGC17P005263.
H-InvDBHIX0013468.
HGNCHGNC:28641. RPAIN.
HPAHPA023924.
HPA031526.
neXtProtNX_Q86UA6.
PharmGKBPA145007849.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46030.
HOVERGENHBG082800.
InParanoidQ86UA6.
OrthoDBEOG7673BZ.
PhylomeDBQ86UA6.
TreeFamTF326215.

Gene expression databases

ArrayExpressQ86UA6.
BgeeQ86UA6.
CleanExHS_RPAIN.
GenevestigatorQ86UA6.

Family and domain databases

InterProIPR028156. RIP.
IPR028159. RPA_interact_C_dom.
IPR028155. RPA_interact_central.
IPR028158. RPA_interact_N_dom.
[Graphical view]
PANTHERPTHR31742:SF0. PTHR31742:SF0. 1 hit.
PfamPF14768. RPA_interact_C. 1 hit.
PF14767. RPA_interact_M. 1 hit.
PF14766. RPA_interact_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPAIN. human.
GeneWikiRPAIN.
GenomeRNAi84268.
NextBio35534920.
PROQ86UA6.

Entry information

Entry nameRIP_HUMAN
AccessionPrimary (citable) accession number: Q86UA6
Secondary accession number(s): B4DI36 expand/collapse secondary AC list , B4DTX7, E9PES3, J3KNH8, Q4G2Y0, Q4G2Y5, Q4G2Y8, Q6B4V9, Q6B4W0, Q6B4W1, Q6B4W4, Q86X49, Q9BT00
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 90 of the entry and version 1 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

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 17

Human chromosome 17: entries, gene names and cross-references to MIM