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Protein

Translocon-associated protein subunit delta

Gene

SSR4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. SRP-dependent cotranslational protein targeting to membrane 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 – 144121LumenalSequence AnalysisAdd
BLAST
Transmembranei145 – 16521HelicalSequence AnalysisAdd
BLAST
Topological domaini166 – 1738CytoplasmicSequence Analysis

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. Sec61 translocon complex Source: UniProtKB
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 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 173150Translocon-associated protein subunit deltaPRO_0000033292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 57By 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

BgeeiP51571.
CleanExiHS_SSR4.
ExpressionAtlasiP51571. baseline and differential.
GenevestigatoriP51571.

Organism-specific databases

HPAiHPA045209.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi112626. 39 interactions.
IntActiP51571. 15 interactions.
MINTiMINT-1160772.
STRINGi9606.ENSP00000317331.

Structurei

3D structure databases

ProteinModelPortaliP51571.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TRAP-delta family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG249692.
GeneTreeiENSGT00390000008992.
HOGENOMiHOG000293353.
HOVERGENiHBG002293.
InParanoidiP51571.
KOiK04571.
OMAiAEACMEP.
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

        10         20         30         40         50
MAAMASLGAL ALLLLSSLSR CSAEACLEPQ ITPSYYTTSD AVISTETVFI
60 70 80 90 100
VEISLTCKNR VQNMALYADV GGKQFPVTRG QDVGRYQVSW SLDHKSAHAG
110 120 130 140 150
TYEVRFFDEE SYSLLRKAQR NNEDISIIPP LFTVSVDHRG TWNGPWVSTE
160 170
VLAAAIGLVI YYLAFSAKSH IQA
Length:173
Mass (Da):18,999
Last modified:October 1, 1996 - v1
Checksum:i063CD2C8F6CE368B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091E → K(PubMed:9286695)Curated

Natural variant

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
GeneIDi6748.
KEGGihsa:6748.
UCSCiuc004fiv.3. human.

Polymorphism databases

DMDMi1711550.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP51571.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112626. 39 interactions.
IntActiP51571. 15 interactions.
MINTiMINT-1160772.
STRINGi9606.ENSP00000317331.

PTM databases

PhosphoSiteiP51571.

Polymorphism databases

DMDMi1711550.

Proteomic databases

MaxQBiP51571.
PaxDbiP51571.
PRIDEiP51571.

Protocols and materials databases

DNASUi6748.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320857; ENSP00000317331; ENSG00000180879.
ENST00000370086; ENSP00000359103; ENSG00000180879.
ENST00000370087; ENSP00000359104; ENSG00000180879.
GeneIDi6748.
KEGGihsa:6748.
UCSCiuc004fiv.3. human.

Organism-specific databases

CTDi6748.
GeneCardsiGC0XP153058.
H-InvDBHIX0016177.
HGNCiHGNC:11326. SSR4.
HPAiHPA045209.
MIMi300090. gene.
neXtProtiNX_P51571.
Orphaneti370927. SSR4-CDG.
PharmGKBiPA36150.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG249692.
GeneTreeiENSGT00390000008992.
HOGENOMiHOG000293353.
HOVERGENiHBG002293.
InParanoidiP51571.
KOiK04571.
OMAiAEACMEP.
PhylomeDBiP51571.
TreeFamiTF313158.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.

Miscellaneous databases

ChiTaRSiSSR4. human.
GeneWikiiSSR4.
GenomeRNAii6748.
NextBioi26324.
PROiP51571.
SOURCEiSearch...

Gene expression databases

BgeeiP51571.
CleanExiHS_SSR4.
ExpressionAtlasiP51571. baseline and differential.
GenevestigatoriP51571.

Family and domain databases

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

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: January 7, 2015
This is version 130 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.