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P51571

- SSRD_HUMAN

UniProt

P51571 - SSRD_HUMAN

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Protein
Translocon-associated protein subunit delta
Gene
SSR4, TRAPD
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.

GO - Biological processi

  1. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. gene expression Source: Reactome
  4. translation Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Translocon-associated protein subunit delta
Short name:
TRAP-delta
Alternative name(s):
Signal sequence receptor subunit delta
Short name:
SSR-delta
Gene namesi
Name:SSR4
Synonyms:TRAPD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:11326. SSR4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 144121Lumenal Reviewed prediction
Add
BLAST
Transmembranei145 – 16521Helical; Reviewed prediction
Add
BLAST
Topological domaini166 – 1738Cytoplasmic Reviewed prediction

GO - Cellular componenti

  1. Sec61 translocon complex Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti370927. SSR4-CDG.
PharmGKBiPA36150.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 173150Translocon-associated protein subunit delta
PRO_0000033292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 57 By similarity
Cross-linki73 – 73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Keywords - PTMi

Disulfide bond, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP51571.
PaxDbiP51571.
PRIDEiP51571.

PTM databases

PhosphoSiteiP51571.

Expressioni

Gene expression databases

ArrayExpressiP51571.
BgeeiP51571.
CleanExiHS_SSR4.
GenevestigatoriP51571.

Organism-specific databases

HPAiHPA045209.

Interactioni

Subunit structurei

Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma.

Protein-protein interaction databases

BioGridi112626. 38 interactions.
IntActiP51571. 15 interactions.
MINTiMINT-1160772.
STRINGi9606.ENSP00000317331.

Structurei

3D structure databases

ProteinModelPortaliP51571.

Family & Domainsi

Sequence similaritiesi

Belongs to the TRAP-delta family.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG249692.
HOGENOMiHOG000293353.
HOVERGENiHBG002293.
InParanoidiP51571.
KOiK04571.
OMAiHRGAWNG.
PhylomeDBiP51571.
TreeFamiTF313158.

Family and domain databases

InterProiIPR008855. TRAP-delta.
[Graphical view]
PANTHERiPTHR12731. PTHR12731. 1 hit.
PfamiPF05404. TRAP-delta. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P51571-1 [UniParc]FASTAAdd to Basket

« Hide

MAAMASLGAL ALLLLSSLSR CSAEACLEPQ ITPSYYTTSD AVISTETVFI    50
VEISLTCKNR VQNMALYADV GGKQFPVTRG QDVGRYQVSW SLDHKSAHAG 100
TYEVRFFDEE SYSLLRKAQR NNEDISIIPP LFTVSVDHRG TWNGPWVSTE 150
VLAAAIGLVI YYLAFSAKSH IQA 173
Length:173
Mass (Da):18,999
Last modified:October 1, 1996 - v1
Checksum:i063CD2C8F6CE368B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1441G → R.1 Publication
VAR_064161

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091E → K1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X90583 mRNA. Translation: CAA62211.1.
Z68129 Genomic DNA. Translation: CAA92215.1.
Z69043 mRNA. Translation: CAA93157.1.
BT007192 mRNA. Translation: AAP35856.1.
AK290493 mRNA. Translation: BAF83182.1.
U52111 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72811.1.
BC003371 mRNA. Translation: AAH03371.1.
BC032351 mRNA. No translation available.
CCDSiCCDS14731.1.
PIRiS59865.
RefSeqiNP_001191455.1. NM_001204526.1.
NP_006271.1. NM_006280.2.
UniGeneiHs.409223.

Genome annotation databases

EnsembliENST00000320857; ENSP00000317331; ENSG00000180879.
ENST00000370086; ENSP00000359103; ENSG00000180879.
ENST00000370087; ENSP00000359104; ENSG00000180879.
ENST00000594475; ENSP00000471489; ENSG00000269520.
ENST00000599490; ENSP00000470405; ENSG00000269520.
ENST00000599757; ENSP00000473104; ENSG00000269520.
GeneIDi6748.
KEGGihsa:6748.
UCSCiuc004fiv.3. human.

Polymorphism databases

DMDMi1711550.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X90583 mRNA. Translation: CAA62211.1 .
Z68129 Genomic DNA. Translation: CAA92215.1 .
Z69043 mRNA. Translation: CAA93157.1 .
BT007192 mRNA. Translation: AAP35856.1 .
AK290493 mRNA. Translation: BAF83182.1 .
U52111 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72811.1 .
BC003371 mRNA. Translation: AAH03371.1 .
BC032351 mRNA. No translation available.
CCDSi CCDS14731.1.
PIRi S59865.
RefSeqi NP_001191455.1. NM_001204526.1.
NP_006271.1. NM_006280.2.
UniGenei Hs.409223.

3D structure databases

ProteinModelPortali P51571.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112626. 38 interactions.
IntActi P51571. 15 interactions.
MINTi MINT-1160772.
STRINGi 9606.ENSP00000317331.

PTM databases

PhosphoSitei P51571.

Polymorphism databases

DMDMi 1711550.

Proteomic databases

MaxQBi P51571.
PaxDbi P51571.
PRIDEi P51571.

Protocols and materials databases

DNASUi 6748.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320857 ; ENSP00000317331 ; ENSG00000180879 .
ENST00000370086 ; ENSP00000359103 ; ENSG00000180879 .
ENST00000370087 ; ENSP00000359104 ; ENSG00000180879 .
ENST00000594475 ; ENSP00000471489 ; ENSG00000269520 .
ENST00000599490 ; ENSP00000470405 ; ENSG00000269520 .
ENST00000599757 ; ENSP00000473104 ; ENSG00000269520 .
GeneIDi 6748.
KEGGi hsa:6748.
UCSCi uc004fiv.3. human.

Organism-specific databases

CTDi 6748.
GeneCardsi GC0XP153058.
H-InvDB HIX0016177.
HGNCi HGNC:11326. SSR4.
HPAi HPA045209.
MIMi 300090. gene.
neXtProti NX_P51571.
Orphaneti 370927. SSR4-CDG.
PharmGKBi PA36150.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249692.
HOGENOMi HOG000293353.
HOVERGENi HBG002293.
InParanoidi P51571.
KOi K04571.
OMAi HRGAWNG.
PhylomeDBi P51571.
TreeFami TF313158.

Enzyme and pathway databases

Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.

Miscellaneous databases

ChiTaRSi SSR4. human.
GeneWikii SSR4.
GenomeRNAii 6748.
NextBioi 26324.
PROi P51571.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51571.
Bgeei P51571.
CleanExi HS_SSR4.
Genevestigatori P51571.

Family and domain databases

InterProi IPR008855. TRAP-delta.
[Graphical view ]
PANTHERi PTHR12731. PTHR12731. 1 hit.
Pfami PF05404. TRAP-delta. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Translocon-associated protein TRAP delta and a novel TRAP-like protein are coordinately expressed with pro-opiomelanocortin in Xenopus intermediate pituitary."
    Holthuis J.C.M., van Riel M.C.H.M., Martens G.J.M.
    Biochem. J. 312:205-213(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Genomic organization of two novel genes on human Xq28: compact head to head arrangement of IDH gamma and TRAP delta is conserved in rat and mouse."
    Brenner V., Nyakatura G., Rosenthal A., Platzer M.
    Genomics 44:8-14(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Liver, Placenta and Spleen.
  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].
  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].
    Tissue: Brain.
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Leukocyte and Placenta.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: VARIANT ARG-144.

Entry informationi

Entry nameiSSRD_HUMAN
AccessioniPrimary (citable) accession number: P51571
Secondary accession number(s): A8K378, Q53XY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 127 of the entry and version 1 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

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