CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024326
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SH3 and PX domain-containing protein 2B 
Protein Synonyms/Alias
 Factor for adipocyte differentiation 49; Tyrosine kinase substrate with four SH3 domains 
Gene Name
 Sh3pxd2b 
Gene Synonyms/Alias
 Fad49; Tks4 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
598MGLECGHKVLAKEVKacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
 Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. 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. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation. 
Sequence Annotation
 DOMAIN 5 129 PX.
 DOMAIN 152 211 SH3 1.
 DOMAIN 221 280 SH3 2.
 DOMAIN 368 427 SH3 3.
 DOMAIN 846 908 SH3 4.
 MOD_RES 25 25 Phosphotyrosine (Probable).
 MOD_RES 279 279 Phosphoserine (By similarity).
 MOD_RES 291 291 Phosphoserine (By similarity).
 MOD_RES 528 528 Phosphoserine.
 MOD_RES 672 672 Phosphoserine.
 MOD_RES 840 840 Phosphoserine.  
Keyword
 Cell junction; Cell projection; Complete proteome; Cytoplasm; Differentiation; Phosphoprotein; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 908 AA 
Protein Sequence
MPPRRSIVEV KVLDVQKRRV PNKHYVYIIR VTWSSGATEA IYRRYSKFFD LQMQMLDKFP 60
MEGGQKDPKQ RIIPFLPGKI LFRRSHIRDV AVKRLIPIDE YCKALIQLPP YISQCDEVLQ 120
FFETRPEDLN PPKEEHIGKK KSGNDPTSVD PMVLEQYVVV ADYQKQESSE ISLSVGQVVD 180
IIEKNESGWW FVSTAEEQGW VPATCLEGQD GVQDEFSLQP EEEEKYTVIY PYTARDQDEM 240
NLERGAVVEV VQKNLEGWWK IRYQGKEGWA PASYLKKNSG EPLPPKLGPS SPAHSGALDL 300
DGVSRHQNAM GREKELLNNQ RDGRFEGRLV PDGDVKQRSP KMRQRPPPRR DMTIPRGLNL 360
PKPPIPPQVE EEYYTIAEFQ TTIPDGISFQ AGLKVEVIEK SLSGWWYIQM EDKEGWAPAT 420
FIDKYKKTSS ASRPNFLAPL PHEMTQLRLG DAAATENNTG PEAVGPSRPL PEAPHGAVDS 480
GMLWSKDWKG GKEAPRKASS DLSASTGYEE ISDPTQEEKP SLPPRKESII KSEEELLERE 540
RQKMEPLRGS SPKPPGMILP MIPAKHAPLA RDSRKPEPKL DKSKFPLRND MGLECGHKVL 600
AKEVKKPNLR PISRSKAELS EEKVDPTSQN LFMKSRPQVR PKPTPSPKTE PAQSEDHVDI 660
YNLRSKLRPA KSQEKALLDG ESHHAAGSHD TALSRSFLPG EGPGHGQDRS GRQDGLSPKE 720
TPCRAPPRPA KTTDPGPKNV PVPVQEATLQ QRPVVPPRRP PPPKKTSSSP LSCRPLPEVR 780
GAQREESRVA PAAGRALLVP PKAKPFLSNS SVGQDDMRGK GGLGPRVTGK VGETREKAAS 840
FLNADGPKDS LYVAVANFEG DEDTSSFQEG TVFEVREKNS SGWWFCQVLS GAPSWEGWIP 900
SNYLRKKP 908 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0042995; C:cell projection; IEA:UniProtKB-KW.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0002102; C:podosome; IDA:UniProtKB.
 GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
 GO:0032266; F:phosphatidylinositol-3-phosphate binding; IMP:UniProtKB.
 GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
 GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB.
 GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
 GO:0060612; P:adipose tissue development; IMP:UniProtKB.
 GO:0060348; P:bone development; IMP:UniProtKB.
 GO:0007154; P:cell communication; IEA:InterPro.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0022617; P:extracellular matrix disassembly; IEA:Compara.
 GO:0001654; P:eye development; IMP:UniProtKB.
 GO:0007507; P:heart development; IMP:UniProtKB.
 GO:0071800; P:podosome assembly; IMP:UniProtKB.
 GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
 GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
 GO:0006801; P:superoxide metabolic process; ISS: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