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P08240 (SRPR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 120. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal recognition particle receptor subunit alpha

Short name=SR-alpha
Alternative name(s):
Docking protein alpha
Short name=DP-alpha
Gene names
Name:SRPR
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system.

Subunit structure

Heterodimer with SRPRB. Ref.10

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Note: Thought to be anchored in the membrane through an interaction with SR-beta, which contains a bona fide transmembrane domain.

Sequence similarities

Belongs to the GTP-binding SRP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 638638Signal recognition particle receptor subunit alpha
PRO_0000101213

Regions

Nucleotide binding425 – 4328GTP By similarity
Nucleotide binding520 – 5245GTP By similarity
Nucleotide binding588 – 5914GTP By similarity

Amino acid modifications

Modified residue2611Phosphotyrosine Ref.6
Modified residue2961Phosphoserine Ref.7 Ref.8
Modified residue2971Phosphoserine Ref.7 Ref.8
Modified residue2981Phosphoserine Ref.7 Ref.8

Experimental info

Sequence conflict811K → R in CAA29608. Ref.1
Sequence conflict2011G → E in CAA29608. Ref.1
Sequence conflict306 – 3072NS → TL in CAA29608. Ref.1

Secondary structure

........................ 638
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08240 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: 967F943CEE3FA79E

FASTA63869,811
        10         20         30         40         50         60 
MLDFFTIFSK GGLVLWCFQG VSDSCTGPVN ALIRSVLLQE RGGNNSFTHE ALTLKYKLDN 

        70         80         90        100        110        120 
QFELVFVVGF QKILTLTYVD KLIDDVHRLF RDKYRTEIQQ QSALSLLNGT FDFQNDFLRL 

       130        140        150        160        170        180 
LREAEESSKI RAPTTMKKFE DSEKAKKPVR SMIETRGEKP KEKAKNSKKK GAKKEGSDGP 

       190        200        210        220        230        240 
LATSKPVPAE KSGLPVGPEN GVELSKEELI RRKREEFIQK HGRGMEKSNK STKSDAPKEK 

       250        260        270        280        290        300 
GKKAPRVWEL GGCANKEVLD YSTPTTNGTP EAALSEDINL IRGTGSGGQL QDLDCSSSDD 

       310        320        330        340        350        360 
EGAAQNSTKP SATKGTLGGM FGMLKGLVGS KSLSREDMES VLDKMRDHLI AKNVAADIAV 

       370        380        390        400        410        420 
QLCESVANKL EGKVMGTFST VTSTVKQALQ ESLVQILQPQ RRVDMLRDIM DAQRRQRPYV 

       430        440        450        460        470        480 
VTFCGVNGVG KSTNLAKISF WLLENGFSVL IAACDTFRAG AVEQLRTHTR RLSALHPPEK 

       490        500        510        520        530        540 
HGGRTMVQLF EKGYGKDAAG IAMEAIAFAR NQGFDVVLVD TAGRMQDNAP LMTALAKLIT 

       550        560        570        580        590        600 
VNTPDLVLFV GEALVGNEAV DQLVKFNRAL ADHSMAQTPR LIDGIVLTKF DTIDDKVGAA 

       610        620        630 
ISMTYITSKP IVFVGTGQTY CDLRSLNAKA VVAALMKA 

« Hide

References

« Hide 'large scale' references
[1]"Complete cDNA sequence coding for human docking protein."
Hortsch M., Labeit S., Meyer D.I.
Nucleic Acids Res. 16:361-362(1988) [PubMed: 3340536] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed: 16554811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung, Muscle and Placenta.
[6]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-261, MASS SPECTROMETRY.
[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-296; SER-297 AND SER-298, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-297 AND SER-298, MASS SPECTROMETRY.
[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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains."
Schlenker O., Hendricks A., Sinning I., Wild K.
J. Biol. Chem. 281:8898-8906(2006) [PubMed: 16439358] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 3-176 IN COMPLEX WITH SRPRB, SUBUNIT.
[11]"Signal recognition particle receptor exposes the ribosomal translocon binding site."
Halic M., Gartmann M., Schlenker O., Mielke T., Pool M.R., Sinning I., Beckmann R.
Science 312:745-747(2006) [PubMed: 16675701] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF 3-176 OF SIGNAL RECOGNITION PARTICLE IN COMPLEX WITH THE 80S RIBOSOME AND THE SRP RECEPTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06272 mRNA. Translation: CAA29608.1.
AK312377 mRNA. Translation: BAG35295.1.
AP001318 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67686.1.
BC001162 mRNA. Translation: AAH01162.1.
BC009110 mRNA. Translation: AAH09110.1.
BC013583 mRNA. Translation: AAH13583.1.
IPIIPI00385267.
PIRA29440.
RefSeqNP_001171313.1. NM_001177842.1.
NP_003130.2. NM_003139.3.
UniGeneHs.368376.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FH5X-ray2.45A3-176[»]
2GO5electron microscopy7.4013-176[»]
ProteinModelPortalP08240.
SMRP08240. Positions 1-130, 330-637.
ModBaseSearch...

Protein-protein interaction databases

IntActP08240. 2 interactions.
MINTMINT-1404634.
STRINGP08240.

PTM databases

PhosphoSiteP08240.

Polymorphism databases

DMDM20455516.

Proteomic databases

PRIDEP08240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332118; ENSP00000328023; ENSG00000182934.
GeneID6734.
KEGGhsa:6734.
UCSCuc001qdh.1. human.

Organism-specific databases

CTD6734.
GeneCardsGC11M126132.
H-InvDBHIX0010252.
HGNCHGNC:11307. SRPR.
MIM182180. gene.
neXtProtNX_P08240.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12415.
HOGENOMHBG562580.
HOVERGENHBG047566.
InParanoidP08240.
OMADNQFELV.
OrthoDBEOG4W0XCP.
PhylomeDBP08240.

Enzyme and pathway databases

ReactomeREACT_15380. Diabetes pathways.

Gene expression databases

ArrayExpressP08240.
BgeeP08240.
CleanExHS_SRPR.
GenevestigatorP08240.
GermOnlineENSG00000182934. Homo sapiens.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR011012. Longin-like.
IPR007222. Sig_recog_particle_rcpt_asu_N.
IPR000897. Signal_recog_part_SRP54_GTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
[Graphical view]
Gene3DG3DSA:1.20.120.140. SRP54_helical. 1 hit.
KOK13431.
PfamPF04086. SRP-alpha_N. 1 hit.
PF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMSSF64356. Longin_like. 1 hit.
SSF47364. SRP54. 1 hit.
PROSITEPS00300. SRP54. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio26272.
SOURCESearch...

Entry information

Entry nameSRPR_HUMAN
AccessionPrimary (citable) accession number: P08240
Secondary accession number(s): A6NIB3, B2R5Z8, Q9BVJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 2, 2002
Last modified: January 25, 2012
This is version 120 of the entry and version 2 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 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families