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Q5TCZ1

- SPD2A_HUMAN

UniProt

Q5TCZ1 - SPD2A_HUMAN

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Protein

SH3 and PX domain-containing protein 2A

Gene

SH3PXD2A

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

Functioni

Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of beta-amyloid peptide.5 Publications

GO - Molecular functioni

  1. phosphatidylinositol binding Source: InterPro

GO - Biological processi

  1. superoxide metabolic process Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
SH3 and PX domain-containing protein 2A
Alternative name(s):
Adapter protein TKS5
Five SH3 domain-containing protein
SH3 multiple domains protein 1
Tyrosine kinase substrate with five SH3 domains
Gene namesi
Name:SH3PXD2A
Synonyms:FISH, KIAA0418, SH3MD1, TKS5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:23664. SH3PXD2A.

Subcellular locationi

Cytoplasm. Cell projectionpodosome
Note: Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells.

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB-KW
  4. podosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421R → A: Loss of binding to (PtdIns(3)P) and (PtdIns(3,4)P2). 1 Publication
Mutagenesisi93 – 931R → A: Loss of binding to (PtdIns(3)P) and (PtdIns(3,4)P2). 1 Publication

Organism-specific databases

PharmGKBiPA134956816.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11331133SH3 and PX domain-containing protein 2APRO_0000278488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei421 – 4211Phosphoserine1 Publication
Modified residuei547 – 5471Phosphoserine1 Publication
Modified residuei567 – 5671Phosphoserine1 Publication
Modified residuei593 – 5931Phosphoserine1 Publication
Modified residuei644 – 6441Phosphoserine1 Publication
Modified residuei731 – 7311Phosphothreonine1 Publication
Modified residuei819 – 8191PhosphoserineBy similarity
Modified residuei1002 – 10021Phosphoserine2 Publications
Modified residuei1016 – 10161Phosphoserine1 Publication
Modified residuei1017 – 10171Phosphoserine1 Publication
Modified residuei1038 – 10381Phosphoserine1 Publication

Post-translational modificationi

Tyrosine phosphorylated by SRC. Phosphorylation plays a regulatory role in the protein localization. The intramolecular interaction of the PX domain with the third SH3 domain maintains the protein in the cytoplasm and phosphorylation disrupts this interaction, resulting in the redistribution of the protein from cytoplasm to the perimembrane region. Phosphorylated on serine upon DNA damage, probably by ATM or ATR.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5TCZ1.
PaxDbiQ5TCZ1.
PRIDEiQ5TCZ1.

PTM databases

PhosphoSiteiQ5TCZ1.

Expressioni

Tissue specificityi

Found in several cancer cell lines, particularly invasive breast carcinomas and melanomas.1 Publication

Gene expression databases

BgeeiQ5TCZ1.
CleanExiHS_SH3PXD2A.
ExpressionAtlasiQ5TCZ1. baseline and differential.
GenevestigatoriQ5TCZ1.

Organism-specific databases

HPAiHPA037922.
HPA037923.

Interactioni

Subunit structurei

Interacts (via N-terminus) with CYBA (By similarity). Interacts with ADAM12, ADAM15 and ADAM19. Interacts with NOXO1. Interacts (via SH3 domains) with NOXA1. Interacts with FASLG.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAM15Q134442EBI-2483234,EBI-77818
Dnm1P215752EBI-7014859,EBI-80070From a different organism.
SOS1Q078895EBI-7014859,EBI-297487

Protein-protein interaction databases

BioGridi115002. 12 interactions.
IntActiQ5TCZ1. 12 interactions.
MINTiMINT-2792114.
STRINGi9606.ENSP00000348215.

Structurei

Secondary structure

1
1133
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi181 – 1844
Beta strandi194 – 1985
Beta strandi202 – 2076
Beta strandi212 – 2165
Helixi217 – 2193
Beta strandi221 – 2233
Beta strandi268 – 2725
Beta strandi292 – 2954
Beta strandi300 – 3089
Beta strandi311 – 3166
Helixi317 – 3193
Beta strandi843 – 8475
Beta strandi866 – 8727
Beta strandi876 – 8827
Beta strandi885 – 8906
Turni891 – 8933
Beta strandi1075 – 10795
Beta strandi1087 – 10893
Beta strandi1097 – 11004
Beta strandi1107 – 11137
Beta strandi1116 – 11183
Beta strandi1120 – 11256
Helixi1126 – 11283
Beta strandi1129 – 11313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNUNMR-A268-325[»]
2EGANMR-A168-224[»]
2EGCNMR-A1072-1133[»]
2EKHNMR-A842-908[»]
ProteinModelPortaliQ5TCZ1.
SMRiQ5TCZ1. Positions 6-126, 162-329, 448-506, 842-908, 1072-1133.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5TCZ1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 128125PXPROSITE-ProRule annotationAdd
BLAST
Domaini166 – 22560SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini266 – 32560SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini448 – 50760SH3 3PROSITE-ProRule annotationAdd
BLAST
Domaini840 – 89960SH3 4PROSITE-ProRule annotationAdd
BLAST
Domaini1071 – 113363SH3 5PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili917 – 94630Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi634 – 72491Ser-richAdd
BLAST

Domaini

The PX domain is required for podosome localization because of its ability to bind phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-phosphate (PtdIns4P), phosphatidylinositol 5-phosphate (PtdIns5P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain (By similarity).By similarity
The fifth SH3 domain mediates binding with ADAM12, ADAM15 and ADAM19.2 Publications

Sequence similaritiesi

Belongs to the SH3PXD2 family.Curated
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
Contains 5 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG148927.
GeneTreeiENSGT00530000063010.
HOGENOMiHOG000154376.
HOVERGENiHBG089589.
InParanoidiQ5TCZ1.
OMAiLESGWWY.
OrthoDBiEOG7H4DSQ.
PhylomeDBiQ5TCZ1.
TreeFamiTF329347.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00787. PX. 1 hit.
PF00018. SH3_1. 4 hits.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 5 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 5 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 5 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5TCZ1-1) [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
MLAYCVQDAT VVDVEKRRNP SKHYVYIINV TWSDSTSQTI YRRYSKFFDL
60 70 80 90 100
QMQLLDKFPI EGGQKDPKQR IIPFLPGKIL FRRSHIRDVA VKRLKPIDEY
110 120 130 140 150
CRALVRLPPH ISQCDEVFRF FEARPEDVNP PKEDYGSSKR KSVWLSSWAE
160 170 180 190 200
SPKKDVTGAD ATAEPMILEQ YVVVSNYKKQ ENSELSLQAG EVVDVIEKNE
210 220 230 240 250
SGWWFVSTSE EQGWVPATYL EAQNGTRDDS DINTSKTGEV SKRRKAHLRR
260 270 280 290 300
LDRRWTLGGM VNRQHSREEK YVTVQPYTSQ SKDEIGFEKG VTVEVIRKNL
310 320 330 340 350
EGWWYIRYLG KEGWAPASYL KKAKDDLPTR KKNLAGPVEI IGNIMEISNL
360 370 380 390 400
LNKKASGDKE TPPAEGEGHE APIAKKEISL PILCNASNGS AVGVPDRTVS
410 420 430 440 450
RLAQGSPAVA RIAPQRAQIS SPNLRTRPPP RRESSLGFQL PKPPEPPSVE
460 470 480 490 500
VEYYTIAEFQ SCISDGISFR GGQKAEVIDK NSGGWWYVQI GEKEGWAPAS
510 520 530 540 550
YIDKRKKPNL SRRTSTLTRP KVPPPAPPSK PKEAEEGPTG ASESQDSPRK
560 570 580 590 600
LKYEEPEYDI PAFGFDSEPE LSEEPVEDRA SGERRPAQPH RPSPASSLQR
610 620 630 640 650
ARFKVGESSE DVALEEETIY ENEGFRPYAE DTLSARGSSG DSDSPGSSSL
660 670 680 690 700
SLTRKNSPKS GSPKSSSLLK LKAEKNAQAE MGKNHSSASF SSSITINTTC
710 720 730 740 750
CSSSSSSSSS LSKTSGDLKP RSASDAGIRG TPKVRAKKDA DANAGLTSCP
760 770 780 790 800
RAKPSVRPKP FLNRAESQSQ EKMDISTLRR QLRPTGQLRG GLKGSKSEDS
810 820 830 840 850
ELPPQTASEA PSEGSRRSSS DLITLPATTP PCPTKKEWEG PATSYMTCSA
860 870 880 890 900
YQKVQDSEIS FPAGVEVQVL EKQESGWWYV RFGELEGWAP SHYLVLDENE
910 920 930 940 950
QPDPSGKELD TVPAKGRQNE GKSDSLEKIE RRVQALNTVN QSKKATPPIP
960 970 980 990 1000
SKPPGGFGKT SGTPAVKMRN GVRQVAVRPQ SVFVSPPPKD NNLSCALRRN
1010 1020 1030 1040 1050
ESLTATDGLR GVRRNSSFST ARSAAAEAKG RLAERAASQG SDSPLLPAQR
1060 1070 1080 1090 1100
NSIPVSPVRP KPIEKSQFIH NNLKDVYVSI ADYEGDEETA GFQEGVSMEV
1110 1120 1130
LERNPNGWWY CQILDGVKPF KGWVPSNYLE KKN
Length:1,133
Mass (Da):125,289
Last modified:December 21, 2004 - v1
Checksum:iD485F49E9192359C
GO
Isoform 2 (identifier: Q5TCZ1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-165: Missing.
     240-267: Missing.

Show »
Length:940
Mass (Da):102,618
Checksum:i1CA24D7BC03B8AC3
GO
Isoform 3 (identifier: Q5TCZ1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     240-267: Missing.

Note: Gene prediction based on similarity to mouse ortholog and partial transcript data.

Show »
Length:1,105
Mass (Da):121,836
Checksum:i384ECB9785EE3FAB
GO

Sequence cautioni

The sequence BAA24848.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti659 – 6591K → Q.
Corresponds to variant rs11818820 [ dbSNP | Ensembl ].
VAR_030781
Natural varianti1035 – 10351R → Q.
Corresponds to variant rs3781365 [ dbSNP | Ensembl ].
VAR_030782
Natural varianti1073 – 10731L → P.
Corresponds to variant rs12764700 [ dbSNP | Ensembl ].
VAR_056993

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 165165Missing in isoform 2. 1 PublicationVSP_023312Add
BLAST
Alternative sequencei240 – 26728Missing in isoform 2 and isoform 3. 1 PublicationVSP_023313Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB007878 mRNA. Translation: BAA24848.2. Different initiation.
AL121929, AL133355 Genomic DNA. Translation: CAI13961.1.
AL121929, AL133355 Genomic DNA. Translation: CAI13962.1.
AL121929 Genomic DNA. Translation: CAI13963.1.
AL133355, AL121929 Genomic DNA. Translation: CAI15351.1.
AL133355, AL121929 Genomic DNA. Translation: CAI15352.1.
CH471066 Genomic DNA. Translation: EAW49623.1.
CH471066 Genomic DNA. Translation: EAW49624.1.
CCDSiCCDS31278.1. [Q5TCZ1-3]
PIRiT00056.
RefSeqiNP_055446.2. NM_014631.2. [Q5TCZ1-3]
XP_005270351.1. XM_005270294.2. [Q5TCZ1-1]
UniGeneiHs.678727.

Genome annotation databases

EnsembliENST00000355946; ENSP00000348215; ENSG00000107957. [Q5TCZ1-3]
ENST00000369774; ENSP00000358789; ENSG00000107957. [Q5TCZ1-1]
GeneIDi9644.
KEGGihsa:9644.
UCSCiuc001kxj.1. human. [Q5TCZ1-3]
uc009xxn.1. human. [Q5TCZ1-2]
uc010qqu.1. human. [Q5TCZ1-1]

Polymorphism databases

DMDMi74746151.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB007878 mRNA. Translation: BAA24848.2 . Different initiation.
AL121929 , AL133355 Genomic DNA. Translation: CAI13961.1 .
AL121929 , AL133355 Genomic DNA. Translation: CAI13962.1 .
AL121929 Genomic DNA. Translation: CAI13963.1 .
AL133355 , AL121929 Genomic DNA. Translation: CAI15351.1 .
AL133355 , AL121929 Genomic DNA. Translation: CAI15352.1 .
CH471066 Genomic DNA. Translation: EAW49623.1 .
CH471066 Genomic DNA. Translation: EAW49624.1 .
CCDSi CCDS31278.1. [Q5TCZ1-3 ]
PIRi T00056.
RefSeqi NP_055446.2. NM_014631.2. [Q5TCZ1-3 ]
XP_005270351.1. XM_005270294.2. [Q5TCZ1-1 ]
UniGenei Hs.678727.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DNU NMR - A 268-325 [» ]
2EGA NMR - A 168-224 [» ]
2EGC NMR - A 1072-1133 [» ]
2EKH NMR - A 842-908 [» ]
ProteinModelPortali Q5TCZ1.
SMRi Q5TCZ1. Positions 6-126, 162-329, 448-506, 842-908, 1072-1133.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115002. 12 interactions.
IntActi Q5TCZ1. 12 interactions.
MINTi MINT-2792114.
STRINGi 9606.ENSP00000348215.

PTM databases

PhosphoSitei Q5TCZ1.

Polymorphism databases

DMDMi 74746151.

Proteomic databases

MaxQBi Q5TCZ1.
PaxDbi Q5TCZ1.
PRIDEi Q5TCZ1.

Protocols and materials databases

DNASUi 9644.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355946 ; ENSP00000348215 ; ENSG00000107957 . [Q5TCZ1-3 ]
ENST00000369774 ; ENSP00000358789 ; ENSG00000107957 . [Q5TCZ1-1 ]
GeneIDi 9644.
KEGGi hsa:9644.
UCSCi uc001kxj.1. human. [Q5TCZ1-3 ]
uc009xxn.1. human. [Q5TCZ1-2 ]
uc010qqu.1. human. [Q5TCZ1-1 ]

Organism-specific databases

CTDi 9644.
GeneCardsi GC10M105345.
HGNCi HGNC:23664. SH3PXD2A.
HPAi HPA037922.
HPA037923.
neXtProti NX_Q5TCZ1.
PharmGKBi PA134956816.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG148927.
GeneTreei ENSGT00530000063010.
HOGENOMi HOG000154376.
HOVERGENi HBG089589.
InParanoidi Q5TCZ1.
OMAi LESGWWY.
OrthoDBi EOG7H4DSQ.
PhylomeDBi Q5TCZ1.
TreeFami TF329347.

Miscellaneous databases

ChiTaRSi SH3PXD2A. human.
EvolutionaryTracei Q5TCZ1.
GeneWikii SH3PXD2A.
GenomeRNAii 9644.
NextBioi 36199.
PROi Q5TCZ1.

Gene expression databases

Bgeei Q5TCZ1.
CleanExi HS_SH3PXD2A.
ExpressionAtlasi Q5TCZ1. baseline and differential.
Genevestigatori Q5TCZ1.

Family and domain databases

Gene3Di 3.30.1520.10. 1 hit.
InterProi IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00787. PX. 1 hit.
PF00018. SH3_1. 4 hits.
[Graphical view ]
SMARTi SM00312. PX. 1 hit.
SM00326. SH3. 5 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 5 hits.
SSF64268. SSF64268. 1 hit.
PROSITEi PS50195. PX. 1 hit.
PS50002. SH3. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
    Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. Okazaki N., Kikuno R.F., Nagase T., Ohara O., Koga H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells."
    Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M., Courtneidge S.A.
    J. Biol. Chem. 278:16844-16851(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH ADAM12; ADAM15 AND ADAM19, MUTAGENESIS OF ARG-42 AND ARG-93.
  6. "The adaptor protein Tks5/Fish is required for podosome formation and function, and for the protease-driven invasion of cancer cells."
    Seals D.F., Azucena E.F. Jr., Pass I., Tesfay L., Gordon R., Woodrow M., Resau J.H., Courtneidge S.A.
    Cancer Cell 7:155-165(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, TISSUE SPECIFICITY.
  7. "Amyloid-beta neurotoxicity is mediated by FISH adapter protein and ADAM12 metalloprotease activity."
    Malinin N.L., Wright S., Seubert P., Schenk D., Griswold-Prenner I.
    Proc. Natl. Acad. Sci. U.S.A. 102:3058-3063(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ADAM12, PTM.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "A role for the podosome/invadopodia scaffold protein Tks5 in tumor growth in vivo."
    Blouw B., Seals D.F., Pass I., Diaz B., Courtneidge S.A.
    Eur. J. Cell Biol. 87:555-567(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421; SER-547; SER-567; SER-593; SER-644; THR-731; SER-1002; SER-1016; SER-1017 AND SER-1038, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  12. "Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity."
    Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A., Bokoch G.M.
    Sci. Signal. 2:RA54-RA54(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NOXA1.
  13. "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 SER-1002, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation."
    Gianni D., Dermardirossian C., Bokoch G.M.
    Eur. J. Cell Biol. 90:164-171(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NOXA1 AND NOXO1.
  15. "Solution structure of the SH3 domains from human KIAA0418 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 168-325 AND 1072-1133.

Entry informationi

Entry nameiSPD2A_HUMAN
AccessioniPrimary (citable) accession number: Q5TCZ1
Secondary accession number(s): D3DR98
, O43302, Q5TCZ2, Q5TDQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 103 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3