CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014026
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SH3 and PX domain-containing protein 2A 
Protein Synonyms/Alias
 Adapter protein TKS5; Five SH3 domain-containing protein; SH3 multiple domains protein 1; Tyrosine kinase substrate with five SH3 domains 
Gene Name
 SH3PXD2A 
Gene Synonyms/Alias
 FISH; KIAA0418; SH3MD1; TKS5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
78IIPFLPGKILFRRSHubiquitination[1, 2, 3]
236DSDINTSKTGEVSKRubiquitination[4]
282QPYTSQSKDEIGFEKubiquitination[2, 4]
915ELDTVPAKGRQNEGKacetylation[5]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 4 128 PX.
 DOMAIN 166 225 SH3 1.
 DOMAIN 266 325 SH3 2.
 DOMAIN 448 507 SH3 3.
 DOMAIN 840 899 SH3 4.
 DOMAIN 1071 1133 SH3 5.
 MOD_RES 421 421 Phosphoserine.
 MOD_RES 547 547 Phosphoserine.
 MOD_RES 567 567 Phosphoserine.
 MOD_RES 593 593 Phosphoserine.
 MOD_RES 644 644 Phosphoserine.
 MOD_RES 731 731 Phosphothreonine.
 MOD_RES 1002 1002 Phosphoserine.
 MOD_RES 1016 1016 Phosphoserine.
 MOD_RES 1017 1017 Phosphoserine.
 MOD_RES 1038 1038 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell junction; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1133 AA 
Protein Sequence
MLAYCVQDAT VVDVEKRRNP SKHYVYIINV TWSDSTSQTI YRRYSKFFDL QMQLLDKFPI 60
EGGQKDPKQR IIPFLPGKIL FRRSHIRDVA VKRLKPIDEY CRALVRLPPH ISQCDEVFRF 120
FEARPEDVNP PKEDYGSSKR KSVWLSSWAE SPKKDVTGAD ATAEPMILEQ YVVVSNYKKQ 180
ENSELSLQAG EVVDVIEKNE SGWWFVSTSE EQGWVPATYL EAQNGTRDDS DINTSKTGEV 240
SKRRKAHLRR LDRRWTLGGM VNRQHSREEK YVTVQPYTSQ SKDEIGFEKG VTVEVIRKNL 300
EGWWYIRYLG KEGWAPASYL KKAKDDLPTR KKNLAGPVEI IGNIMEISNL LNKKASGDKE 360
TPPAEGEGHE APIAKKEISL PILCNASNGS AVGVPDRTVS RLAQGSPAVA RIAPQRAQIS 420
SPNLRTRPPP RRESSLGFQL PKPPEPPSVE VEYYTIAEFQ SCISDGISFR GGQKAEVIDK 480
NSGGWWYVQI GEKEGWAPAS YIDKRKKPNL SRRTSTLTRP KVPPPAPPSK PKEAEEGPTG 540
ASESQDSPRK LKYEEPEYDI PAFGFDSEPE LSEEPVEDRA SGERRPAQPH RPSPASSLQR 600
ARFKVGESSE DVALEEETIY ENEGFRPYAE DTLSARGSSG DSDSPGSSSL SLTRKNSPKS 660
GSPKSSSLLK LKAEKNAQAE MGKNHSSASF SSSITINTTC CSSSSSSSSS LSKTSGDLKP 720
RSASDAGIRG TPKVRAKKDA DANAGLTSCP RAKPSVRPKP FLNRAESQSQ EKMDISTLRR 780
QLRPTGQLRG GLKGSKSEDS ELPPQTASEA PSEGSRRSSS DLITLPATTP PCPTKKEWEG 840
PATSYMTCSA YQKVQDSEIS FPAGVEVQVL EKQESGWWYV RFGELEGWAP SHYLVLDENE 900
QPDPSGKELD TVPAKGRQNE GKSDSLEKIE RRVQALNTVN QSKKATPPIP SKPPGGFGKT 960
SGTPAVKMRN GVRQVAVRPQ SVFVSPPPKD NNLSCALRRN ESLTATDGLR GVRRNSSFST 1020
ARSAAAEAKG RLAERAASQG SDSPLLPAQR NSIPVSPVRP KPIEKSQFIH NNLKDVYVSI 1080
ADYEGDEETA GFQEGVSMEV LERNPNGWWY CQILDGVKPF KGWVPSNYLE KKN 1133 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0042995; C:cell projection; IEA:UniProtKB-KW.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0002102; C:podosome; IDA:UniProtKB.
 GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
 GO:0007154; P:cell communication; IEA:InterPro.
 GO:0006801; P:superoxide metabolic process; IDA:UniProtKB. 
Interpro
 IPR001683; Phox.
 IPR011511; SH3_2.
 IPR001452; SH3_domain. 
Pfam
 PF00787; PX
 PF00018; SH3_1
 PF07653; SH3_2 
SMART
 SM00312; PX
 SM00326; SH3 
PROSITE
 PS50195; PX
 PS50002; SH3 
PRINTS