Reviewed, UniProtKB/Swiss-Prot P43307 (SSRA_HUMAN)

Names and origin

Protein names

Recommended name:
    Translocon-associated protein subunit alpha
      Short name=TRAP-alpha
Alternative name(s):
    Signal sequence receptor subunit alpha
      Short name=SSR-alpha

Gene names

Name:	SSR1
Synonyms:	TRAPA
ORF Names:	PSEC0262

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	286 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.
Subunit structure	Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Domain	Shows a remarkable charge distribution with the N-terminus being highly negatively charged, and the cytoplasmic C-terminus positively charged.
Post-translational modification	Phosphorylated in its cytoplasmic tail By similarity.
Miscellaneous	Seems to bind calcium.
Sequence similarities	Belongs to the TRAP-alpha family.
Sequence caution	The sequence CAI16444.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane
Ligand	Calcium
PTM	Glycoprotein Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cotranslational protein targeting to membrane Ref.1 Traceable author statement. Source: ProtInc positive regulation of cell proliferation Ref.2 Traceable author statement. Source: ProtInc
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW signal sequence binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P43307-1)

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 (identifier: P43307-2)

The sequence of this isoform differs from the canonical sequence as follows:
     68-94: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Ref.10
	Chain	19 – 286	268	Translocon-associated protein subunit alpha		PRO_0000033281
Regions
	Topological domain	19 – 207	189	Lumenal Potential
	Transmembrane	208 – 228	21	Potential
	Topological domain	229 – 286	58	Cytoplasmic Potential
Amino acid modifications
	Modified residue	247	1	Phosphoserine Ref.14
	Modified residue	260	1	Phosphothreonine By similarity
	Modified residue	268	1	Phosphoserine Ref.14 Ref.12 Ref.13
	Glycosylation	136	1	N-linked (GlcNAc...) Ref.11
	Glycosylation	191	1	N-linked (GlcNAc...)
Natural variations
	Alternative sequence	68 – 94	27	Missing in isoform 2.		VSP_013621
	Natural variant	28	1	L → S: dbSNP rs10004. Ref.1 Ref.7		VAR_022427
Experimental info
	Sequence conflict	6	1	R → G in BAC11701. Ref.4
	Sequence conflict	37	1	E → A in BAD96529. Ref.7
	Sequence conflict	130	1	Y → H in CAA78290. Ref.1
	Sequence conflict	190	1	F → Y in BAF84239. Ref.3
	Sequence conflict	220	1	L → P in BAD96529. Ref.7
	Sequence conflict	263	1	Q → R in BAF84239. Ref.3
	Sequence conflict	286	1	E → D in CAG33242. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 13, 2002. Version 3. Checksum: 2C631DC0CC3EB489	FASTA	286	32,235
	10 20 30 40 50 60 MRLLPRLLLL LLLVFPATVL FRGGPRGLLA VAQDLTEDEE TVEDSIIEDE DDEAEVEEDE 70 80 90 100 110 120 PTDLVEDKEE EDVSGEPEAS PSADTTILFV KGEDFPANNI VKFLVGFTNK GTEDFIVESL 130 140 150 160 170 180 DASFRYPQDY QFYIQNFTAL PLNTVVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDL 190 200 210 220 230 240 NGNVFQDAVF NQTVTVIERE DGLDGETIFM YMFLAGLGLL VIVGLHQLLE SRKRKRPIQK 250 260 270 280 VEMGTSSQND VDMSWIPQET LNQINKASPR RLPRKRAQKR SVGSDE
	Isoform 2. Checksum: D79F40EE756B1CB5	FASTA	259	29,373
	10 20 30 40 50 60 MRLLPRLLLL LLLVFPATVL FRGGPRGLLA VAQDLTEDEE TVEDSIIEDE DDEAEVEEDE 70 80 90 100 110 120 PTDLVEDFPA NNIVKFLVGF TNKGTEDFIV ESLDASFRYP QDYQFYIQNF TALPLNTVVP 130 140 150 160 170 180 PQRQATFEYS FIPAEPMGGR PFGLVINLNY KDLNGNVFQD AVFNQTVTVI EREDGLDGET 190 200 210 220 230 240 IFMYMFLAGL GLLVIVGLHQ LLESRKRKRP IQKVEMGTSS QNDVDMSWIP QETLNQINKA 250 SPRRLPRKRA QKRSVGSDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The N-terminal region of the alpha-subunit of the TRAP complex has a conserved cluster of negative charges." Hartmann E., Prehn S. FEBS Lett. 349:324-326(1994) [PubMed: 8050590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-28.
[2]	"Translocon-associated protein alpha transcripts are induced by granulocyte-macrophage colony-stimulating factor and exhibit complex alternative polyadenylation." Hirama T., Miller C.W., Koeffler H.P. FEBS Lett. 455:223-227(1999) [PubMed: 10437777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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. , 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] (ISOFORM 1). Tissue: Placenta.
[4]	"HRI human cDNA sequencing project." Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S., Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y., Nagahari K., Sugano S., Isogai T. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Teratocarcinoma.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-28. Tissue: Liver.
[8]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORM 1). Tissue: B-cell.
[10]	"HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides." Wei M.L., Cresswell P. Nature 356:443-446(1992) [PubMed: 1557127] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-31.
[11]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-136.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, MASS SPECTROMETRY.
[14]	"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-247 AND SER-268, MASS SPECTROMETRY.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-191, MASS SPECTROMETRY. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z12830 mRNA. Translation: CAA78290.1. AF156965 mRNA. Translation: AAD48778.1. AK291550 mRNA. Translation: BAF84239.1. AK075562 mRNA. Translation: BAC11701.1. BT007387 mRNA. Translation: AAP36051.1. CR456961 mRNA. Translation: CAG33242.1. AK222762 mRNA. Translation: BAD96482.1. AK222809 mRNA. Translation: BAD96529.1. AL139095 Genomic DNA. Translation: CAI16444.1. Sequence problems. BC007710 mRNA. Translation: AAH07710.1.
IPI	IPI00301021. IPI00449669.
PIR	I38246.
RefSeq	NP_003135.2.
UniGene	Hs.114033
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P43307. 9 interactions.
PTM databases
PhosphoSite	P43307.
Proteomic databases
PeptideAtlas	P43307.
PRIDE	P43307.
Genome annotation databases
Ensembl	ENSG00000124783. Homo sapiens. [Contig view]
GeneID	6745.
KEGG	hsa:6745.
Organism-specific databases
GeneCards	GC06M007232.
H-InvDB	HIX0005562.
HGNC	HGNC:11323. SSR1.
HPA	HPA011276. HPA017062.
MIM	600868. gene.
PharmGKB	PA36147.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P43307.
Gene expression databases
ArrayExpress	P43307.
Bgee	P43307.
GermOnline	ENSG00000124783. Homo sapiens.
Family and domain databases
InterPro	IPR005595. TRAP_alpha. [Graphical view]
Pfam	PF03896. TRAP_alpha. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	26310.
SOURCE	Search...

Entry information

Entry name

SSRA_HUMAN

Accession

Primary (citable) accession number: P43307
Secondary accession number(s): A8K685 , Q53GX2, Q53H19, Q5TAM3, Q6IB43, Q8NBH9, Q96IA2, Q9TNQ8, Q9UN49

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	August 13, 2002
Last modified:	June 16, 2009
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)