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Protein

Serum deprivation-response protein

Gene

SDPR

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

Functioni

May play a role in targeting PRKCA to caveolae.By similarity

GO - Molecular functioni

  • phosphatidylserine binding Source: UniProtKB
  • phospholipid binding Source: ProtInc
  • protein kinase C binding Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serum deprivation-response protein
Alternative name(s):
Cavin-2
PS-p68
Phosphatidylserine-binding protein
Gene namesi
Name:SDPRImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10690. SDPR.

Subcellular locationi

GO - Cellular componenti

  • caveola Source: GO_Central
  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • membrane raft Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35615.

Polymorphism and mutation databases

BioMutaiSDPR.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 425424Serum deprivation-response proteinPRO_0000238918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine1 Publication
Modified residuei27 – 271PhosphoserineBy similarity
Modified residuei35 – 351PhosphoserineCombined sources
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei51 – 511PhosphoserineBy similarity
Modified residuei196 – 1961PhosphothreonineCombined sources
Modified residuei199 – 1991PhosphothreonineCombined sources
Modified residuei203 – 2031PhosphoserineCombined sources
Modified residuei204 – 2041PhosphoserineCombined sources
Modified residuei218 – 2181PhosphoserineCombined sources
Modified residuei283 – 2831PhosphoserineBy similarity
Modified residuei284 – 2841PhosphoserineBy similarity
Modified residuei287 – 2871PhosphoserineCombined sources
Modified residuei288 – 2881PhosphoserineCombined sources
Modified residuei293 – 2931PhosphoserineCombined sources
Modified residuei332 – 3321PhosphoserineBy similarity
Modified residuei341 – 3411PhosphoserineBy similarity
Modified residuei366 – 3661PhosphoserineBy similarity
Modified residuei370 – 3701PhosphoserineBy similarity
Modified residuei375 – 3751PhosphothreonineBy similarity
Modified residuei395 – 3951PhosphotyrosineBy similarity
Modified residuei403 – 4031PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on Ser residues.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO95810.
MaxQBiO95810.
PaxDbiO95810.
PeptideAtlasiO95810.
PRIDEiO95810.
TopDownProteomicsiO95810.

2D gel databases

OGPiO95810.

PTM databases

iPTMnetiO95810.
PhosphoSiteiO95810.
SwissPalmiO95810.

Expressioni

Tissue specificityi

Highly expressed in heart and lung, and expressed at lower levels in brain, kidney, liver, pancreas, placenta, and skeletal muscle.1 Publication

Inductioni

Up-regulated in asyncronously growing fibroblasts following serum deprivation but not following contact inhibition. Down-regulated during synchronous cell cycle re-entry.1 Publication

Gene expression databases

BgeeiENSG00000168497.
CleanExiHS_SDPR.
GenevisibleiO95810. HS.

Organism-specific databases

HPAiHPA039325.

Interactioni

Subunit structurei

Binds to PRKCA in the presence of phosphatidylserine (By similarity). Interacts with MURC; this augments the transactivation of NPPA by MURC.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
A1CFQ9NQ94-23EBI-742141,EBI-10311892
PLEKP085674EBI-742141,EBI-2565501

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114016. 7 interactions.
DIPiDIP-56943N.
IntActiO95810. 9 interactions.
MINTiMINT-1436848.
STRINGi9606.ENSP00000305675.

Structurei

3D structure databases

ProteinModelPortaliO95810.
SMRiO95810. Positions 54-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili61 – 8222Sequence analysisAdd
BLAST
Coiled coili125 – 15430Sequence analysisAdd
BLAST
Coiled coili210 – 26859Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the PTRF/SDPR family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEZA. Eukaryota.
ENOG410XP8W. LUCA.
GeneTreeiENSGT00530000063058.
HOGENOMiHOG000293135.
HOVERGENiHBG056807.
InParanoidiO95810.
OMAiERMDRQC.
OrthoDBiEOG091G09Y1.
PhylomeDBiO95810.
TreeFamiTF331031.

Family and domain databases

InterProiIPR026752. Cavin_fam.
IPR033298. SDPR.
[Graphical view]
PANTHERiPTHR15240. PTHR15240. 1 hit.
PTHR15240:SF1. PTHR15240:SF1. 1 hit.
PfamiPF15237. PTRF_SDPR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O95810-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEDAAQAEK FQHPGSDMRQ EKPSSPSPMP SSTPSPSLNL GNTEEAIRDN
60 70 80 90 100
SQVNAVTVLT LLDKLVNMLD AVQENQHKME QRQISLEGSV KGIQNDLTKL
110 120 130 140 150
SKYQASTSNT VSKLLEKSRK VSAHTRAVKE RMDRQCAQVK RLENNHAQLL
160 170 180 190 200
RRNHFKVLIF QEENEIPASV FVKQPVSGAV EGKEELPDEN KSLEETLHTV
210 220 230 240 250
DLSSDDDLPH DEEALEDSAE EKVEESRAEK IKRSSLKKVD SLKKAFSRQN
260 270 280 290 300
IEKKMNKLGT KIVSVERREK IKKSLTSNHQ KISSGKSSPF KVSPLTFGRK
310 320 330 340 350
KVREGESHAE NETKSEDLPS SEQMPNDQEE ESFAEGHSEA SLASALVEGE
360 370 380 390 400
IAEEAAEKAT SRGSNSGMDS NIDLTIVEDE EEESVALEQA QKVRYEGSYA
410 420
LTSEEAERSD GDPVQPAVLQ VHQTS
Length:425
Mass (Da):47,173
Last modified:January 23, 2007 - v3
Checksum:i0631CBF4BED537F9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti130 – 1301E → D.
Corresponds to variant rs35012125 [ dbSNP | Ensembl ].
VAR_034422

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085481 mRNA. Translation: AAD17795.1.
AC098872 Genomic DNA. Translation: AAY24078.1.
BC016475 mRNA. Translation: AAH16475.1.
CCDSiCCDS2313.1.
RefSeqiNP_004648.1. NM_004657.5.
UniGeneiHs.26530.

Genome annotation databases

EnsembliENST00000304141; ENSP00000305675; ENSG00000168497.
GeneIDi8436.
KEGGihsa:8436.
UCSCiuc002utb.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085481 mRNA. Translation: AAD17795.1.
AC098872 Genomic DNA. Translation: AAY24078.1.
BC016475 mRNA. Translation: AAH16475.1.
CCDSiCCDS2313.1.
RefSeqiNP_004648.1. NM_004657.5.
UniGeneiHs.26530.

3D structure databases

ProteinModelPortaliO95810.
SMRiO95810. Positions 54-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114016. 7 interactions.
DIPiDIP-56943N.
IntActiO95810. 9 interactions.
MINTiMINT-1436848.
STRINGi9606.ENSP00000305675.

PTM databases

iPTMnetiO95810.
PhosphoSiteiO95810.
SwissPalmiO95810.

Polymorphism and mutation databases

BioMutaiSDPR.

2D gel databases

OGPiO95810.

Proteomic databases

EPDiO95810.
MaxQBiO95810.
PaxDbiO95810.
PeptideAtlasiO95810.
PRIDEiO95810.
TopDownProteomicsiO95810.

Protocols and materials databases

DNASUi8436.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304141; ENSP00000305675; ENSG00000168497.
GeneIDi8436.
KEGGihsa:8436.
UCSCiuc002utb.4. human.

Organism-specific databases

CTDi8436.
GeneCardsiSDPR.
HGNCiHGNC:10690. SDPR.
HPAiHPA039325.
MIMi606728. gene.
neXtProtiNX_O95810.
PharmGKBiPA35615.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEZA. Eukaryota.
ENOG410XP8W. LUCA.
GeneTreeiENSGT00530000063058.
HOGENOMiHOG000293135.
HOVERGENiHBG056807.
InParanoidiO95810.
OMAiERMDRQC.
OrthoDBiEOG091G09Y1.
PhylomeDBiO95810.
TreeFamiTF331031.

Miscellaneous databases

GeneWikiiSDPR.
GenomeRNAii8436.
PROiO95810.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000168497.
CleanExiHS_SDPR.
GenevisibleiO95810. HS.

Family and domain databases

InterProiIPR026752. Cavin_fam.
IPR033298. SDPR.
[Graphical view]
PANTHERiPTHR15240. PTHR15240. 1 hit.
PTHR15240:SF1. PTHR15240:SF1. 1 hit.
PfamiPF15237. PTRF_SDPR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSDPR_HUMAN
AccessioniPrimary (citable) accession number: O95810
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 122 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

Binds phosphatidylserine (PS) in a calcium-independent manner. PS-binding is inhibited by phosphotidic acid and phosphatidylinositol. Does not bind phosphatidylcholine.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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 one 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.