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Protein

Switch-associated protein 70

Gene

SWAP70

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

Functioni

Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which, independently of RAS, transduces signals from tyrosine kinase receptors to RAC. It also mediates signaling of membrane ruffling. Regulates the actin cytoskeleton as an effector or adapter protein in response to agonist stimulated phosphatidylinositol (3,4)-bisphosphate production and cell protrusion (By similarity).By similarity2 Publications

GO - Molecular functioni

  • ATP binding Source: Ensembl
  • cadherin binding Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • DNA binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Switch-associated protein 70
Short name:
SWAP-70
Gene namesi
Name:SWAP70
Synonyms:KIAA0640
ORF Names:HSPC321
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000133789.14.
HGNCiHGNC:17070. SWAP70.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi223 – 224RR → EE: Abolishes binding to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid and the localization to the loose actin filament arrays. 1 Publication2
Mutagenesisi230R → C: Reduced binding to phosphatidylinositol 3,4-bisphosphate and reduced association with actin filament. 1 Publication1
Mutagenesisi297W → A: Abolishes binding to plasma membrane. 1 Publication1
Mutagenesisi526 – 585Missing : Affects targeting to loose actin filament arrays. 1 PublicationAdd BLAST60

Organism-specific databases

DisGeNETi23075.
OpenTargetsiENSG00000133789.
PharmGKBiPA165543694.

Polymorphism and mutation databases

BioMutaiSWAP70.
DMDMi74753323.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002402801 – 585Switch-associated protein 70Add BLAST585

Post-translational modificationi

Tyrosine-phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UH65.
MaxQBiQ9UH65.
PaxDbiQ9UH65.
PeptideAtlasiQ9UH65.
PRIDEiQ9UH65.

PTM databases

iPTMnetiQ9UH65.
PhosphoSitePlusiQ9UH65.

Expressioni

Tissue specificityi

Expressed only in mature B-cells including those associated with mucosa-associated tissue and bronchus-associated tissue (PubMed:10681448). Widely expressed. Abundant in spleen, and fairly abundant in kidney, lung and liver. Also found in monocytes and macrophages (PubMed:12925760).2 Publications

Gene expression databases

BgeeiENSG00000133789.
ExpressionAtlasiQ9UH65. baseline and differential.
GenevisibleiQ9UH65. HS.

Organism-specific databases

HPAiHPA006810.

Interactioni

Subunit structurei

The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ZBTB5O150623EBI-310749,EBI-722671

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi116707. 31 interactors.
IntActiQ9UH65. 4 interactors.
STRINGi9606.ENSP00000315630.

Structurei

Secondary structure

1585
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi212 – 220Combined sources9
Beta strandi227 – 234Combined sources8
Beta strandi239 – 244Combined sources6
Beta strandi248 – 254Combined sources7
Beta strandi261 – 265Combined sources5
Beta strandi273 – 278Combined sources6
Beta strandi283 – 287Combined sources5
Helixi291 – 310Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DN6NMR-A211-312[»]
ProteinModelPortaliQ9UH65.
SMRiQ9UH65.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UH65.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini210 – 306PHPROSITE-ProRule annotationAdd BLAST97

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili316 – 539Sequence analysisAdd BLAST224

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi291 – 294Poly-Lys4

Domaini

The PH domain is essential for phosphatidylinositol 3,4,5-trisphosphate binding.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410ITNV. Eukaryota.
ENOG4111DEK. LUCA.
GeneTreeiENSGT00390000005512.
HOGENOMiHOG000285974.
HOVERGENiHBG053201.
InParanoidiQ9UH65.
KOiK20072.
OMAiIKCFDKT.
OrthoDBiEOG091G0SJG.
PhylomeDBiQ9UH65.
TreeFamiTF333160.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiView protein in InterPro
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR011993. PH-like_dom_sf.
IPR001849. PH_domain.
PfamiView protein in Pfam
PF00169. PH. 1 hit.
SMARTiView protein in SMART
SM00233. PH. 1 hit.
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiView protein in PROSITE
PS50003. PH_DOMAIN. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9UH65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSLKEELLK AIWHAFTALD QDHSGKVSKS QLKVLSHNLC TVLKVPHDPV
60 70 80 90 100
ALEEHFRDDD EGPVSNQGYM PYLNRFILEK VQDNFDKIEF NRMCWTLCVK
110 120 130 140 150
KNLTKNPLLI TEEDAFKIWV IFNFLSEDKY PLIIVSEEIE YLLKKLTEAM
160 170 180 190 200
GGGWQQEQFE HYKINFDDSK NGLSAWELIE LIGNGQFSKG MDRQTVSMAI
210 220 230 240 250
NEVFNELILD VLKQGYMMKK GHRRKNWTER WFVLKPNIIS YYVSEDLKDK
260 270 280 290 300
KGDILLDENC CVESLPDKDG KKCLFLVKCF DKTFEISASD KKKKQEWIQA
310 320 330 340 350
IHSTIHLLKL GSPPPHKEAR QRRKELRKKQ LAEQEELERQ MKELQAANES
360 370 380 390 400
KQQELEAVRK KLEEAASRAA EEEKKRLQTQ VELQARFSTE LEREKLIRQQ
410 420 430 440 450
MEEQVAQKSS ELEQYLQRVR ELEDMYLKLQ EALEDERQAR QDEETVRKLQ
460 470 480 490 500
ARLLEEESSK RAELEKWHLE QQQAIQTTEA EKQELENQRV LKEQALQEAM
510 520 530 540 550
EQLEQLELER KQALEQYEEV KKKLEMATNK TKSWKDKVAH HEGLIRLIEP
560 570 580
GSKNPHLITN WGPAAFTEAE LEEREKNWKE KKTTE
Length:585
Mass (Da):68,998
Last modified:May 1, 2000 - v1
Checksum:iB42B63CF033E612F
GO

Sequence cautioni

The sequence AAF28999 differs from that shown. Reason: Frameshift at positions 480 and 483.Curated
The sequence BAA31615 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti385A → S (Ref. 7) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_059548230R → G. Corresponds to variant dbSNP:rs397686Ensembl.1
Natural variantiVAR_026717505Q → E4 PublicationsCorresponds to variant dbSNP:rs415895Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF210818 mRNA. Translation: AAF24486.1.
AF134894 mRNA. Translation: AAF61403.1.
AB014540 mRNA. Translation: BAA31615.1. Different initiation.
CH471064 Genomic DNA. Translation: EAW68582.1.
CH471064 Genomic DNA. Translation: EAW68583.1.
BC000616 mRNA. Translation: AAH00616.1.
AF161439 mRNA. Translation: AAF28999.1. Frameshift.
CCDSiCCDS31426.1.
PIRiT00379.
RefSeqiNP_001284643.1. NM_001297714.1.
NP_055870.2. NM_015055.3.
UniGeneiHs.153026.

Genome annotation databases

EnsembliENST00000318950; ENSP00000315630; ENSG00000133789.
GeneIDi23075.
KEGGihsa:23075.
UCSCiuc001mhw.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSWP70_HUMAN
AccessioniPrimary (citable) accession number: Q9UH65
Secondary accession number(s): D3DQV1
, O75135, Q7LCY6, Q9P061, Q9P0Z8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: May 1, 2000
Last modified: November 22, 2017
This is version 143 of the entry and version 1 of the sequence. See 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references