Q96B01 (R51A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RAD51-associated protein 1

Alternative name(s):
RAD51-interacting protein

Gene names

Name:	RAD51AP1
Synonyms:	PIR51

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10
Subunit structure	Isoform 2 interacts with RAD51. Interacts with PALB2. Ref.1 Ref.5 Ref.10
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
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 Ref.8

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	double-strand break repair via homologous recombination Non-traceable author statement Ref.1. Source: UniProtKB
Cellular component	nucleus Inferred by curator Ref.1. Source: UniProtKB
Molecular function	RNA binding Inferred from direct assay Ref.1. Source: UniProtKB double-stranded DNA binding Inferred from direct assay Ref.1. Source: UniProtKB protein binding Inferred from physical interaction Ref.10Ref.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
RAD51	Q06609	4	EBI-1178743,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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 352	352	RAD51-associated protein 1		PRO_0000097140
Regions
	Region	313 – 352	40	Interaction with RAD51
Amino acid modifications
	Modified residue	19	1	Phosphoserine Ref.7
	Modified residue	21	1	Phosphoserine Ref.7
	Modified residue	66	1	Phosphothreonine Ref.7
	Modified residue	120	1	Phosphoserine Ref.6 Ref.8
	Modified residue	280	1	Phosphoserine Ref.7
	Modified residue	327	1	Phosphoserine Ref.7
	Modified residue	343	1	N6-acetyllysine Ref.9
Natural variations
	Alternative sequence	71 – 87	17	Missing in isoform 2. Ref.1		VSP_051739
	Alternative sequence	258 – 307	50	Missing in isoform 3. Ref.1		VSP_051740
	Natural variant	68	1	K → Q. Corresponds to variant rs34810644 [ dbSNP | Ensembl ].		VAR_056976
Experimental info
	Mutagenesis	333	1	R → A: Strongly decreases interaction with RAD51; when associated with Q-336; A-345 and A-346. Ref.5
	Mutagenesis	336	1	L → Q: Strongly decreases interaction with RAD51; when associated with A-333; A-345 and A-346. Ref.5
	Mutagenesis	345 – 346	2	LH → AA: Strongly decreases interaction with RAD51; when associated with A-333; and Q-336.

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: E582EE4BC459DD92	FASTA	352	38,457
	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
	Isoform 2 [UniParc]. Checksum: 71BBA478F55C5D39	FASTA	335	36,757
	10 20 30 40 50 60 MVRPVRHKKP VNYSQFDHSD SDDDFVSATV PLNKKSRTAP KELKQDKPKP NLNNLRKEEI 70 80 90 100 110 120 PVQEKTPKKR MALDDKLYQR DLEVALALSV KELPTVTTNV QNSQDKSIEK HGSSKIETMN 130 140 150 160 170 180 KSPHISNCSV ASDYLDLDKI TVEDDVGGVQ GKRKAASKAA AQQRKILLEG SDGDSANDTE 190 200 210 220 230 240 PDFAPGEDSE DDSDFCESED NDEDFSMRKS KVKEIKKKEV KVKSPVEKKE KKSKSKCNAL 250 260 270 280 290 300 VTSVDSAPAA VKSESQSLPK KVSLSSDTTR KPLEIRSPSA ESKKPKWVPP AASGGSRSSS 310 320 330 SPLVVVSVKS PNQSLRLGLS RLARVKPLHP NATST
	Isoform 3 [UniParc]. Checksum: F667DBB6B8DF19E6	FASTA	302	33,142
	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 KSKCNALAAS GGSRSSSSPL VVVSVKSPNQ SLRLGLSRLA RVKPLHPNAT ST

References

	« Hide 'large scale' referencesShow '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: 9396801] [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. , 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: 14702039] [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. , 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: 15489334] [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: 16990250] [Abstract] Cited for: INTERACTION WITH RAD51, MUTAGENESIS OF ARG-333; LEU-336 AND 345-LEU-HIS-346.
[6]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-21; THR-66; SER-280 AND SER-327, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-343, MASS SPECTROMETRY.
[10]	"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: 20871616] [Abstract] Cited for: FUNCTION, INTERACTION WITH PALB2.
+	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.
IPI	IPI00093253. IPI00396551. IPI00607574.
RefSeq	NP_001124334.1. NM_001130862.1. NP_006470.1. NM_006479.4.
UniGene	Hs.504550.
3D structure databases
ProteinModelPortal	Q96B01.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35257N.
IntAct	Q96B01. 7 interactions.
STRING	Q96B01.
PTM databases
PhosphoSite	Q96B01.
Polymorphism databases
DMDM	68565925.
Proteomic databases
PRIDE	Q96B01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000228843; ENSP00000228843; ENSG00000111247.
GeneID	10635.
KEGG	hsa:10635.
UCSC	uc001qmu.1. human. uc001qmw.1. human.
Organism-specific databases
CTD	10635.
GeneCards	GC12P004647.
H-InvDB	HIX0010349.
HGNC	HGNC:16956. RAD51AP1.
MIM	603070. gene.
neXtProt	NX_Q96B01.
PharmGKB	PA134871784.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG17266.
GeneTree	ENSGT00530000063784.
HOGENOM	HBG283205.
HOVERGEN	HBG079699.
InParanoid	Q96B01.
OMA	DSEPDFA.
PhylomeDB	Q96B01.
Gene expression databases
ArrayExpress	Q96B01.
Bgee	Q96B01.
CleanEx	HS_RAD51AP1.
Genevestigator	Q96B01.
GermOnline	ENSG00000111247. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other
NextBio	40421.
SOURCE	Search...

Entry information

Entry name

R51A1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.