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P43307

- SSRA_HUMAN

UniProt

P43307 - SSRA_HUMAN

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Protein

Translocon-associated protein subunit alpha

Gene

SSR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. cotranslational protein targeting to membrane Source: ProtInc
  4. endoplasmic reticulum unfolded protein response Source: Reactome
  5. gene expression Source: Reactome
  6. positive regulation of cell proliferation Source: ProtInc
  7. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  8. translation Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_18273. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Translocon-associated protein subunit alpha
Short name:
TRAP-alpha
Alternative name(s):
Signal sequence receptor subunit alpha
Short name:
SSR-alpha
Gene namesi
Name:SSR1
Synonyms:TRAPA
ORF Names:PSEC0262
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:11323. SSR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 207189LumenalSequence AnalysisAdd
BLAST
Transmembranei208 – 22821HelicalSequence AnalysisAdd
BLAST
Topological domaini229 – 28658CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: HPA
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36147.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 286268Translocon-associated protein subunit alphaPRO_0000033281Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi136 – 1361N-linked (GlcNAc...)2 Publications
Glycosylationi191 – 1911N-linked (GlcNAc...)1 Publication
Modified residuei247 – 2471Phosphoserine1 Publication
Modified residuei260 – 2601Phosphothreonine1 Publication
Modified residuei268 – 2681Phosphoserine6 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP43307.
PaxDbiP43307.
PeptideAtlasiP43307.
PRIDEiP43307.

PTM databases

PhosphoSiteiP43307.

Expressioni

Gene expression databases

BgeeiP43307.
ExpressionAtlasiP43307. baseline and differential.
GenevestigatoriP43307.

Organism-specific databases

HPAiHPA011276.
HPA017062.

Interactioni

Subunit structurei

Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma. Interacts with palmitoylated calnexin (CALX), the interaction is required for efficient folding of glycosylated proteins.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CANXP278245EBI-714168,EBI-355947
SERPINA1P010094EBI-714168,EBI-986224

Protein-protein interaction databases

BioGridi112623. 35 interactions.
IntActiP43307. 23 interactions.
MINTiMINT-1379984.

Structurei

3D structure databases

ProteinModelPortaliP43307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Shows a remarkable charge distribution with the N-terminus being highly negatively charged, and the cytoplasmic C-terminus positively charged.

Sequence similaritiesi

Belongs to the TRAP-alpha family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG127973.
GeneTreeiENSGT00400000022103.
HOVERGENiHBG009736.
InParanoidiP43307.
KOiK13249.
PhylomeDBiP43307.
TreeFamiTF321074.

Family and domain databases

InterProiIPR005595. TRAP_alpha.
[Graphical view]
PfamiPF03896. TRAP_alpha. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P43307-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRLLPRLLLL LLLVFPATVL FRGGPRGLLA VAQDLTEDEE TVEDSIIEDE
60 70 80 90 100
DDEAEVEEDE PTDLVEDKEE EDVSGEPEAS PSADTTILFV KGEDFPANNI
110 120 130 140 150
VKFLVGFTNK GTEDFIVESL DASFRYPQDY QFYIQNFTAL PLNTVVPPQR
160 170 180 190 200
QATFEYSFIP AEPMGGRPFG LVINLNYKDL NGNVFQDAVF NQTVTVIERE
210 220 230 240 250
DGLDGETIFM YMFLAGLGLL VIVGLHQLLE SRKRKRPIQK VEMGTSSQND
260 270 280
VDMSWIPQET LNQINKASPR RLPRKRAQKR SVGSDE
Length:286
Mass (Da):32,235
Last modified:August 13, 2002 - v3
Checksum:i2C631DC0CC3EB489
GO
Isoform 2 (identifier: P43307-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:259
Mass (Da):29,373
Checksum:iD79F40EE756B1CB5
GO

Sequence cautioni

The sequence CAI16444.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61R → G in BAC11701. (PubMed:16303743)Curated
Sequence conflicti37 – 371E → A in BAD96529. 1 PublicationCurated
Sequence conflicti130 – 1301Y → H in CAA78290. (PubMed:8050590)Curated
Sequence conflicti190 – 1901F → Y in BAF84239. (PubMed:14702039)Curated
Sequence conflicti220 – 2201L → P in BAD96529. 1 PublicationCurated
Sequence conflicti263 – 2631Q → R in BAF84239. (PubMed:14702039)Curated
Sequence conflicti286 – 2861E → D in CAG33242. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281L → S.2 Publications
Corresponds to variant rs10004 [ dbSNP | Ensembl ].
VAR_022427

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei68 – 9427Missing in isoform 2. 1 PublicationVSP_013621Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12830 mRNA. Translation: CAA78290.1.
AF156965 mRNA. Translation: AAD48778.1.
BT007387 mRNA. Translation: AAP36051.1.
AK291550 mRNA. Translation: BAF84239.1.
CR456961 mRNA. Translation: CAG33242.1.
AK222762 mRNA. Translation: BAD96482.1.
AK222809 mRNA. Translation: BAD96529.1.
AK075562 mRNA. Translation: BAC11701.1.
AL139095 Genomic DNA. Translation: CAI16444.1. Sequence problems.
BC007710 mRNA. Translation: AAH07710.1.
CCDSiCCDS4499.1. [P43307-1]
PIRiI38246.
RefSeqiNP_001278937.1. NM_001292008.1.
NP_003135.2. NM_003144.4. [P43307-1]
UniGeneiHs.114033.

Genome annotation databases

EnsembliENST00000244763; ENSP00000244763; ENSG00000124783. [P43307-1]
GeneIDi6745.
KEGGihsa:6745.
UCSCiuc003mxf.4. human. [P43307-1]

Polymorphism databases

DMDMi22261821.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12830 mRNA. Translation: CAA78290.1 .
AF156965 mRNA. Translation: AAD48778.1 .
BT007387 mRNA. Translation: AAP36051.1 .
AK291550 mRNA. Translation: BAF84239.1 .
CR456961 mRNA. Translation: CAG33242.1 .
AK222762 mRNA. Translation: BAD96482.1 .
AK222809 mRNA. Translation: BAD96529.1 .
AK075562 mRNA. Translation: BAC11701.1 .
AL139095 Genomic DNA. Translation: CAI16444.1 . Sequence problems.
BC007710 mRNA. Translation: AAH07710.1 .
CCDSi CCDS4499.1. [P43307-1 ]
PIRi I38246.
RefSeqi NP_001278937.1. NM_001292008.1.
NP_003135.2. NM_003144.4. [P43307-1 ]
UniGenei Hs.114033.

3D structure databases

ProteinModelPortali P43307.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112623. 35 interactions.
IntActi P43307. 23 interactions.
MINTi MINT-1379984.

PTM databases

PhosphoSitei P43307.

Polymorphism databases

DMDMi 22261821.

Proteomic databases

MaxQBi P43307.
PaxDbi P43307.
PeptideAtlasi P43307.
PRIDEi P43307.

Protocols and materials databases

DNASUi 6745.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244763 ; ENSP00000244763 ; ENSG00000124783 . [P43307-1 ]
GeneIDi 6745.
KEGGi hsa:6745.
UCSCi uc003mxf.4. human. [P43307-1 ]

Organism-specific databases

CTDi 6745.
GeneCardsi GC06M007232.
HGNCi HGNC:11323. SSR1.
HPAi HPA011276.
HPA017062.
MIMi 600868. gene.
neXtProti NX_P43307.
PharmGKBi PA36147.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG127973.
GeneTreei ENSGT00400000022103.
HOVERGENi HBG009736.
InParanoidi P43307.
KOi K13249.
PhylomeDBi P43307.
TreeFami TF321074.

Enzyme and pathway databases

Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSi SSR1. human.
GeneWikii SSR1.
GenomeRNAii 6745.
NextBioi 26310.
PROi P43307.
SOURCEi Search...

Gene expression databases

Bgeei P43307.
ExpressionAtlasi P43307. baseline and differential.
Genevestigatori P43307.

Family and domain databases

InterProi IPR005595. TRAP_alpha.
[Graphical view ]
Pfami PF03896. TRAP_alpha. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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).
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  5. "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).
  6. 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.
  7. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Teratocarcinoma.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-191.
    Tissue: Liver.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "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 THR-260 AND SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Palmitoylated calnexin is a key component of the ribosome-translocon complex."
    Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic S., Kunz B., Kihara A., Dal Peraro M., van der Goot F.G.
    EMBO J. 31:1823-1835(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CALNEXIN.

Entry informationi

Entry nameiSSRA_HUMAN
AccessioniPrimary (citable) accession number: P43307
Secondary accession number(s): A8K685
, Q53GX2, Q53H19, Q5TAM3, Q6IB43, Q8NBH9, Q96IA2, Q9TNQ8, Q9UN49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 13, 2002
Last modified: October 29, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Seems to bind calcium.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3