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Q96B01 (R51A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RAD51-associated protein 1
Alternative name(s):
RAD51-interacting protein
Gene names
Name:RAD51AP1
Synonyms:PIR51
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May participate in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Functionally cooperates with PALB2 in promoting of D-loop formation by RAD51. Binds to single and double stranded DNA, and is capable of aggregating DNA. Also binds RNA. Ref.1 Ref.7

Subunit structure

Isoform 2 interacts with RAD51. Interacts with PALB2. Ref.1 Ref.5 Ref.7

Subcellular location

Nucleus By similarity. Note: Colocalizes with RAD51 to multiple nuclear foci By similarity.

Tissue specificity

Highly expressed in testis and thymus. Lower levels in colon and small intestine. Little or no expression in spleen, prostate, ovary and peripheral blood leukocytes. Ref.1

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
RNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdouble-strand break repair via homologous recombination

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

   Cellular_componentnucleus

Inferred by curator Ref.1. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from direct assay Ref.1. Source: UniProtKB

double-stranded DNA binding

Inferred from direct assay Ref.1. Source: UniProtKB

single-stranded DNA binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAD51Q066095EBI-1178748,EBI-297202

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q96B01-1)

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.
Isoform 2 Ref.1 (identifier: Q96B01-2)

The sequence of this isoform differs from the canonical sequence as follows:
     71-87: Missing.
Isoform 3 Ref.1 (identifier: Q96B01-3)

The sequence of this isoform differs from the canonical sequence as follows:
     258-307: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352RAD51-associated protein 1
PRO_0000097140

Regions

Region313 – 35240Interaction with RAD51

Amino acid modifications

Modified residue191Phosphoserine Ref.6 Ref.8
Modified residue211Phosphoserine Ref.6 Ref.8
Modified residue1201Phosphoserine Ref.8 Ref.10
Modified residue2801Phosphoserine Ref.6 Ref.8
Modified residue3271Phosphoserine Ref.6

Natural variations

Alternative sequence71 – 8717Missing in isoform 2. Ref.1
VSP_051739
Alternative sequence258 – 30750Missing in isoform 3. Ref.1
VSP_051740
Natural variant681K → Q.
Corresponds to variant rs34810644 [ dbSNP | Ensembl ].
VAR_056976

Experimental info

Mutagenesis3331R → A: Strongly decreases interaction with RAD51; when associated with Q-336; A-345 and A-346. Ref.5
Mutagenesis3361L → Q: Strongly decreases interaction with RAD51; when associated with A-333; A-345 and A-346. Ref.5
Mutagenesis345 – 3462LH → AA: Strongly decreases interaction with RAD51; when associated with A-333; and Q-336.

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: E582EE4BC459DD92

FASTA35238,457
        10         20         30         40         50         60 
MVRPVRHKKP VNYSQFDHSD SDDDFVSATV PLNKKSRTAP KELKQDKPKP NLNNLRKEEI 

        70         80         90        100        110        120 
PVQEKTPKKR LPEGTFSIPA SAVPCTKMAL DDKLYQRDLE VALALSVKEL PTVTTNVQNS 

       130        140        150        160        170        180 
QDKSIEKHGS SKIETMNKSP HISNCSVASD YLDLDKITVE DDVGGVQGKR KAASKAAAQQ 

       190        200        210        220        230        240 
RKILLEGSDG DSANDTEPDF APGEDSEDDS DFCESEDNDE DFSMRKSKVK EIKKKEVKVK 

       250        260        270        280        290        300 
SPVEKKEKKS KSKCNALVTS VDSAPAAVKS ESQSLPKKVS LSSDTTRKPL EIRSPSAESK 

       310        320        330        340        350 
KPKWVPPAAS GGSRSSSSPL VVVSVKSPNQ SLRLGLSRLA RVKPLHPNAT ST

« Hide

Isoform 2 [UniParc].

Checksum: 71BBA478F55C5D39
Show »

FASTA33536,757
Isoform 3 [UniParc].

Checksum: F667DBB6B8DF19E6
Show »

FASTA30233,142

References

« Hide 'large scale' references
[1]"A novel nucleic acid-binding protein that interacts with human rad51 recombinase."
Kovalenko O.V., Golub E.I., Bray-Ward P., Ward D.C., Radding C.M.
Nucleic Acids Res. 25:4946-4953(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION WITH RAD51, TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[2]"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 1 AND 2).
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 2).
Tissue: Bone marrow and Urinary bladder.
[5]"RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51."
Kovalenko O.V., Wiese C., Schild D.
Nucleic Acids Res. 34:5081-5092(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAD51, MUTAGENESIS OF ARG-333; LEU-336 AND 345-LEU-HIS-346.
[6]"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-19; SER-21; SER-280 AND SER-327, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"Enhancement of RAD51 recombinase activity by the tumor suppressor PALB2."
Dray E., Etchin J., Wiese C., Saro D., Williams G.J., Hammel M., Yu X., Galkin V.E., Liu D., Tsai M.S., Sy S.M., Schild D., Egelman E., Chen J., Sung P.
Nat. Struct. Mol. Biol. 17:1255-1259(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PALB2.
[8]"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-19; SER-21; SER-120 AND SER-280, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-120, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF006259 mRNA. Translation: AAC39554.1.
AK096930 mRNA. Translation: BAC04902.1.
AK291948 mRNA. Translation: BAF84637.1.
CH471116 Genomic DNA. Translation: EAW88844.1.
BC006992 mRNA. Translation: AAH06992.1.
BC016330 mRNA. Translation: AAH16330.1.
IPIIPI00093253.
IPI00396551.
IPI00607574.
RefSeqNP_001124334.1. NM_001130862.1.
NP_006470.1. NM_006479.4.
UniGeneHs.730696.

3D structure databases

ProteinModelPortalQ96B01.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35257N.
IntActQ96B01. 5 interactions.
STRING9606.ENSP00000228843.

PTM databases

PhosphoSiteQ96B01.

Polymorphism databases

DMDM68565925.

Proteomic databases

PaxDbQ96B01.
PRIDEQ96B01.

Protocols and materials databases

DNASU10635.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228843; ENSP00000228843; ENSG00000111247.
ENST00000321524; ENSP00000323750; ENSG00000111247.
ENST00000352618; ENSP00000309479; ENSG00000111247.
GeneID10635.
KEGGhsa:10635.
UCSCuc001qmu.3. human.
uc001qmw.3. human.

Organism-specific databases

CTD10635.
GeneCardsGC12P004647.
HGNCHGNC:16956. RAD51AP1.
HPAHPA051499.
MIM603070. gene.
neXtProtNX_Q96B01.
PharmGKBPA134871784.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG28637.
HOGENOMHOG000116153.
HOVERGENHBG079699.
InParanoidQ96B01.
OMADFCESED.
PhylomeDBQ96B01.

Gene expression databases

ArrayExpressQ96B01.
BgeeQ96B01.
CleanExHS_RAD51AP1.
GenevestigatorQ96B01.
GermOnlineENSG00000111247. Homo sapiens.

Family and domain databases

InterProIPR026632. RAD51-assoc_prot_1.
[Graphical view]
PANTHERPTHR15361:SF2. PTHR15361:SF2. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRAD51AP1. human.
GenomeRNAi10635.
NextBio40421.
SOURCESearch...

Entry information

Entry nameR51A1_HUMAN
AccessionPrimary (citable) accession number: Q96B01
Secondary accession number(s): A8K7D3, O43403, Q7Z779
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 96 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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

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