Q5TCZ1 (SPD2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SH3PXD2A
Synonyms:	FISH, KIAA0418, SH3MD1, TKS5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1133 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6 Ref.7 Ref.12 Ref.14
Subunit structure	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. Ref.5 Ref.7 Ref.11 Ref.12 Ref.14
Subcellular location	Cytoplasm. Cell projection › podosome. Note: Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells. Ref.5 Ref.6 Ref.9
Tissue specificity	Found in several cancer cell lines, particularly invasive breast carcinomas and melanomas. Ref.6
Domain	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. Ref.5 Ref.6 The fifth SH3 domain mediates binding with ADAM12, ADAM15 and ADAM19. Ref.5 Ref.6
Post-translational modification	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.
Sequence similarities	Belongs to the SH3PXD2 family. Contains 1 PX (phox homology) domain. Contains 5 SH3 domains.
Sequence caution	The sequence BAA24848.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cell junction Cell projection Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell communication Inferred from electronic annotation. Source: InterPro superoxide metabolic process Inferred from direct assay Ref.12. Source: UniProtKB
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell projection Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell podosome Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	phosphatidylinositol binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5TCZ1-1)

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.

Isoform 2 (identifier: Q5TCZ1-2)

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

Isoform 3 (identifier: Q5TCZ1-3)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1133

1133

SH3 and PX domain-containing protein 2A

PRO_0000278488

Regions

Domain

4 – 128

125

PX

Domain

166 – 225

60

SH3 1

Domain

266 – 325

60

SH3 2

Domain

448 – 507

60

SH3 3

Domain

840 – 899

60

SH3 4

Domain

1071 – 1133

63

SH3 5

Coiled coil

917 – 946

30

Potential

Compositional bias

634 – 724

91

Ser-rich

Amino acid modifications

Modified residue

421

1

Phosphoserine Ref.10

Modified residue

547

1

Phosphoserine Ref.10

Modified residue

567

1

Phosphoserine Ref.10

Modified residue

593

1

Phosphoserine Ref.10

Modified residue

644

1

Phosphoserine Ref.10

Modified residue

731

1

Phosphothreonine Ref.10

Modified residue

1002

1

Phosphoserine Ref.10 Ref.13

Modified residue

1016

1

Phosphoserine Ref.10

Modified residue

1017

1

Phosphoserine Ref.10

Modified residue

1038

1

Phosphoserine Ref.10

Natural variations

Alternative sequence

1 – 165

165

Missing in isoform 2.

VSP_023312

Alternative sequence

240 – 267

28

Missing in isoform 2 and isoform 3.

VSP_023313

Natural variant

659

1

K → Q.
Corresponds to variant rs11818820 [ dbSNP | Ensembl ].

VAR_030781

Natural variant

1035

1

R → Q.
Corresponds to variant rs3781365 [ dbSNP | Ensembl ].

VAR_030782

Natural variant

1073

1

L → P.
Corresponds to variant rs12764700 [ dbSNP | Ensembl ].

VAR_056993

Experimental info

Mutagenesis

42

1

R → A: Loss of binding to (PtdIns(3)P) and (PtdIns(3,4)P2). Ref.5

Mutagenesis

93

1

R → A: Loss of binding to (PtdIns(3)P) and (PtdIns(3,4)P2). Ref.5

Secondary structure

1

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1133

Helix Strand Turn

Details...

Beta strand

181 – 184

4

Beta strand

194 – 198

5

Beta strand

202 – 207

6

Beta strand

212 – 216

5

Helix

217 – 219

3

Beta strand

221 – 223

3

Beta strand

268 – 272

5

Beta strand

292 – 295

4

Beta strand

300 – 308

9

Beta strand

311 – 316

6

Helix

317 – 319

3

Beta strand

843 – 847

5

Beta strand

866 – 872

7

Beta strand

876 – 882

7

Beta strand

885 – 890

6

Turn

891 – 893

3

Beta strand

1075 – 1079

5

Beta strand

1087 – 1089

3

Beta strand

1097 – 1100

4

Beta strand

1107 – 1113

7

Beta strand

1116 – 1118

3

Beta strand

1120 – 1125

6

Helix

1126 – 1128

3

Beta strand

1129 – 1131

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: D485F49E9192359C	FASTA	1,133	125,289
	10 20 30 40 50 60 MLAYCVQDAT VVDVEKRRNP SKHYVYIINV TWSDSTSQTI YRRYSKFFDL QMQLLDKFPI 70 80 90 100 110 120 EGGQKDPKQR IIPFLPGKIL FRRSHIRDVA VKRLKPIDEY CRALVRLPPH ISQCDEVFRF 130 140 150 160 170 180 FEARPEDVNP PKEDYGSSKR KSVWLSSWAE SPKKDVTGAD ATAEPMILEQ YVVVSNYKKQ 190 200 210 220 230 240 ENSELSLQAG EVVDVIEKNE SGWWFVSTSE EQGWVPATYL EAQNGTRDDS DINTSKTGEV 250 260 270 280 290 300 SKRRKAHLRR LDRRWTLGGM VNRQHSREEK YVTVQPYTSQ SKDEIGFEKG VTVEVIRKNL 310 320 330 340 350 360 EGWWYIRYLG KEGWAPASYL KKAKDDLPTR KKNLAGPVEI IGNIMEISNL LNKKASGDKE 370 380 390 400 410 420 TPPAEGEGHE APIAKKEISL PILCNASNGS AVGVPDRTVS RLAQGSPAVA RIAPQRAQIS 430 440 450 460 470 480 SPNLRTRPPP RRESSLGFQL PKPPEPPSVE VEYYTIAEFQ SCISDGISFR GGQKAEVIDK 490 500 510 520 530 540 NSGGWWYVQI GEKEGWAPAS YIDKRKKPNL SRRTSTLTRP KVPPPAPPSK PKEAEEGPTG 550 560 570 580 590 600 ASESQDSPRK LKYEEPEYDI PAFGFDSEPE LSEEPVEDRA SGERRPAQPH RPSPASSLQR 610 620 630 640 650 660 ARFKVGESSE DVALEEETIY ENEGFRPYAE DTLSARGSSG DSDSPGSSSL SLTRKNSPKS 670 680 690 700 710 720 GSPKSSSLLK LKAEKNAQAE MGKNHSSASF SSSITINTTC CSSSSSSSSS LSKTSGDLKP 730 740 750 760 770 780 RSASDAGIRG TPKVRAKKDA DANAGLTSCP RAKPSVRPKP FLNRAESQSQ EKMDISTLRR 790 800 810 820 830 840 QLRPTGQLRG GLKGSKSEDS ELPPQTASEA PSEGSRRSSS DLITLPATTP PCPTKKEWEG 850 860 870 880 890 900 PATSYMTCSA YQKVQDSEIS FPAGVEVQVL EKQESGWWYV RFGELEGWAP SHYLVLDENE 910 920 930 940 950 960 QPDPSGKELD TVPAKGRQNE GKSDSLEKIE RRVQALNTVN QSKKATPPIP SKPPGGFGKT 970 980 990 1000 1010 1020 SGTPAVKMRN GVRQVAVRPQ SVFVSPPPKD NNLSCALRRN ESLTATDGLR GVRRNSSFST 1030 1040 1050 1060 1070 1080 ARSAAAEAKG RLAERAASQG SDSPLLPAQR NSIPVSPVRP KPIEKSQFIH NNLKDVYVSI 1090 1100 1110 1120 1130 ADYEGDEETA GFQEGVSMEV LERNPNGWWY CQILDGVKPF KGWVPSNYLE KKN
	Isoform 2 [UniParc]. Checksum: 1CA24D7BC03B8AC3	FASTA	940	102,618
	10 20 30 40 50 60 MILEQYVVVS NYKKQENSEL SLQAGEVVDV IEKNESGWWF VSTSEEQGWV PATYLEAQNG 70 80 90 100 110 120 TRDDSDINTS KTGEEEKYVT VQPYTSQSKD EIGFEKGVTV EVIRKNLEGW WYIRYLGKEG 130 140 150 160 170 180 WAPASYLKKA KDDLPTRKKN LAGPVEIIGN IMEISNLLNK KASGDKETPP AEGEGHEAPI 190 200 210 220 230 240 AKKEISLPIL CNASNGSAVG VPDRTVSRLA QGSPAVARIA PQRAQISSPN LRTRPPPRRE 250 260 270 280 290 300 SSLGFQLPKP PEPPSVEVEY YTIAEFQSCI SDGISFRGGQ KAEVIDKNSG GWWYVQIGEK 310 320 330 340 350 360 EGWAPASYID KRKKPNLSRR TSTLTRPKVP PPAPPSKPKE AEEGPTGASE SQDSPRKLKY 370 380 390 400 410 420 EEPEYDIPAF GFDSEPELSE EPVEDRASGE RRPAQPHRPS PASSLQRARF KVGESSEDVA 430 440 450 460 470 480 LEEETIYENE GFRPYAEDTL SARGSSGDSD SPGSSSLSLT RKNSPKSGSP KSSSLLKLKA 490 500 510 520 530 540 EKNAQAEMGK NHSSASFSSS ITINTTCCSS SSSSSSSLSK TSGDLKPRSA SDAGIRGTPK 550 560 570 580 590 600 VRAKKDADAN AGLTSCPRAK PSVRPKPFLN RAESQSQEKM DISTLRRQLR PTGQLRGGLK 610 620 630 640 650 660 GSKSEDSELP PQTASEAPSE GSRRSSSDLI TLPATTPPCP TKKEWEGPAT SYMTCSAYQK 670 680 690 700 710 720 VQDSEISFPA GVEVQVLEKQ ESGWWYVRFG ELEGWAPSHY LVLDENEQPD PSGKELDTVP 730 740 750 760 770 780 AKGRQNEGKS DSLEKIERRV QALNTVNQSK KATPPIPSKP PGGFGKTSGT PAVKMRNGVR 790 800 810 820 830 840 QVAVRPQSVF VSPPPKDNNL SCALRRNESL TATDGLRGVR RNSSFSTARS AAAEAKGRLA 850 860 870 880 890 900 ERAASQGSDS PLLPAQRNSI PVSPVRPKPI EKSQFIHNNL KDVYVSIADY EGDEETAGFQ 910 920 930 940 EGVSMEVLER NPNGWWYCQI LDGVKPFKGW VPSNYLEKKN
	Isoform 3 [UniParc]. Checksum: 384ECB9785EE3FAB	FASTA	1,105	121,836
	10 20 30 40 50 60 MLAYCVQDAT VVDVEKRRNP SKHYVYIINV TWSDSTSQTI YRRYSKFFDL QMQLLDKFPI 70 80 90 100 110 120 EGGQKDPKQR IIPFLPGKIL FRRSHIRDVA VKRLKPIDEY CRALVRLPPH ISQCDEVFRF 130 140 150 160 170 180 FEARPEDVNP PKEDYGSSKR KSVWLSSWAE SPKKDVTGAD ATAEPMILEQ YVVVSNYKKQ 190 200 210 220 230 240 ENSELSLQAG EVVDVIEKNE SGWWFVSTSE EQGWVPATYL EAQNGTRDDS DINTSKTGEE 250 260 270 280 290 300 EKYVTVQPYT SQSKDEIGFE KGVTVEVIRK NLEGWWYIRY LGKEGWAPAS YLKKAKDDLP 310 320 330 340 350 360 TRKKNLAGPV EIIGNIMEIS NLLNKKASGD KETPPAEGEG HEAPIAKKEI SLPILCNASN 370 380 390 400 410 420 GSAVGVPDRT VSRLAQGSPA VARIAPQRAQ ISSPNLRTRP PPRRESSLGF QLPKPPEPPS 430 440 450 460 470 480 VEVEYYTIAE FQSCISDGIS FRGGQKAEVI DKNSGGWWYV QIGEKEGWAP ASYIDKRKKP 490 500 510 520 530 540 NLSRRTSTLT RPKVPPPAPP SKPKEAEEGP TGASESQDSP RKLKYEEPEY DIPAFGFDSE 550 560 570 580 590 600 PELSEEPVED RASGERRPAQ PHRPSPASSL QRARFKVGES SEDVALEEET IYENEGFRPY 610 620 630 640 650 660 AEDTLSARGS SGDSDSPGSS SLSLTRKNSP KSGSPKSSSL LKLKAEKNAQ AEMGKNHSSA 670 680 690 700 710 720 SFSSSITINT TCCSSSSSSS SSLSKTSGDL KPRSASDAGI RGTPKVRAKK DADANAGLTS 730 740 750 760 770 780 CPRAKPSVRP KPFLNRAESQ SQEKMDISTL RRQLRPTGQL RGGLKGSKSE DSELPPQTAS 790 800 810 820 830 840 EAPSEGSRRS SSDLITLPAT TPPCPTKKEW EGPATSYMTC SAYQKVQDSE ISFPAGVEVQ 850 860 870 880 890 900 VLEKQESGWW YVRFGELEGW APSHYLVLDE NEQPDPSGKE LDTVPAKGRQ NEGKSDSLEK 910 920 930 940 950 960 IERRVQALNT VNQSKKATPP IPSKPPGGFG KTSGTPAVKM RNGVRQVAVR PQSVFVSPPP 970 980 990 1000 1010 1020 KDNNLSCALR RNESLTATDG LRGVRRNSSF STARSAAAEA KGRLAERAAS QGSDSPLLPA 1030 1040 1050 1060 1070 1080 QRNSIPVSPV RPKPIEKSQF IHNNLKDVYV SIADYEGDEE TAGFQEGVSM EVLERNPNGW 1090 1100 WYCQILDGVK PFKGWVPSNY LEKKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00400923.
IPI00456943.
IPI00640092.

PIR

T00056.

RefSeq

NP_055446.2. NM_014631.2.

UniGene

Hs.594708.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q5TCZ1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q5TCZ1. 4 interactions.

MINT

MINT-2792114.

STRING

9606.ENSP00000348215.

PTM databases

PhosphoSite

Q5TCZ1.

Polymorphism databases

DMDM

74746151.

Proteomic databases

PaxDb

Q5TCZ1.

PRIDE

Q5TCZ1.

Protocols and materials databases

DNASU

9644.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000315994; ENSP00000318135; ENSG00000107957.
ENST00000355946; ENSP00000348215; ENSG00000107957.
ENST00000369774; ENSP00000358789; ENSG00000107957.

GeneID

9644.

KEGG

hsa:9644.

UCSC

uc001kxj.1. human.
uc009xxn.1. human.
uc010qqu.1. human.

Organism-specific databases

CTD

9644.

GeneCards

GC10M105345.

HGNC

HGNC:23664. SH3PXD2A.

HPA

HPA037922.
HPA037923.

neXtProt

NX_Q5TCZ1.

PharmGKB

PA134956816.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG148927.

HOGENOM

HOG000154376.

HOVERGEN

HBG089589.

InParanoid

Q5TCZ1.

OMA

LESGWWY.

OrthoDB

EOG4NKBTR.

Gene expression databases

ArrayExpress

Q5TCZ1.

Bgee

Q5TCZ1.

CleanEx

HS_SH3PXD2A.

Genevestigator

Q5TCZ1.

Family and domain databases

Gene3D

3.30.1520.10. 1 hit.

InterPro

IPR001683. Phox.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00787. PX. 1 hit.
PF00018. SH3_1. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]

SMART

SM00312. PX. 1 hit.
SM00326. SH3. 5 hits.
[Graphical view]

SUPFAM

SSF64268. PX. 1 hit.
SSF50044. SH3. 5 hits.

PROSITE

PS50195. PX. 1 hit.
PS50002. SH3. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SH3PXD2A. human.

EvolutionaryTrace

Q5TCZ1.

GenomeRNAi

9644.

NextBio

36199.

Entry information

Entry name

SPD2A_HUMAN

Accession

Primary (citable) accession number: Q5TCZ1
Secondary accession number(s): D3DR98 , O43302, Q5TCZ2, Q5TDQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 20, 2007
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.