CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024298
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SH3 and PX domain-containing protein 2B 
Protein Synonyms/Alias
 Adapter protein HOFI; Factor for adipocyte differentiation 49; Tyrosine kinase substrate with four SH3 domains 
Gene Name
 SH3PXD2B 
Gene Synonyms/Alias
 FAD49; KIAA1295; TKS4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17VKVLDVQKRRVPNKHacetylation[1]
79IIPFLPGKILFRRSHubiquitination[2, 3]
Reference
 [1] 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]
 [2] 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]
 [3] 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] 
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 (By similarity). 
Sequence Annotation
 DOMAIN 5 129 PX.
 DOMAIN 152 211 SH3 1.
 DOMAIN 221 280 SH3 2.
 DOMAIN 368 427 SH3 3.
 DOMAIN 849 911 SH3 4.
 MOD_RES 279 279 Phosphoserine.
 MOD_RES 291 291 Phosphoserine.
 MOD_RES 528 528 Phosphoserine (By similarity).
 MOD_RES 675 675 Phosphoserine (By similarity).
 MOD_RES 843 843 Phosphoserine (By similarity).  
Keyword
 Cell junction; Cell projection; Complete proteome; Cytoplasm; Differentiation; Disease mutation; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 911 AA 
Protein Sequence
MPPRRSIVEV KVLDVQKRRV PNKHYVYIIR VTWSSGSTEA IYRRYSKFFD LQMQMLDKFP 60
MEGGQKDPKQ RIIPFLPGKI LFRRSHIRDV AVKRLIPIDE YCKALIQLPP YISQCDEVLQ 120
FFETRPEDLN PPKEEHIGKK KSGGDQTSVD PMVLEQYVVV ANYQKQESSE ISLSVGQVVD 180
IIEKNESGWW FVSTAEEQGW VPATCLEGQD GVQDEFSLQP EEEEKYTVIY PYTARDQDEM 240
NLERGAVVEV IQKNLEGWWK IRYQGKEGWA PASYLKKNSG EPLPPKPGPG SPSHPGALDL 300
DGVSRQQNAV GREKELLSSQ RDGRFEGRPV PDGDAKQRSP KMRQRPPPRR DMTIPRGLNL 360
PKPPIPPQVE EEYYTIAEFQ TTIPDGISFQ AGLKVEVIEK NLSGWWYIQI EDKEGWAPAT 420
FIDKYKKTSN ASRPNFLAPL PHEVTQLRLG EAAALENNTG SEATGPSRPL PDAPHGVMDS 480
GLPWSKDWKG SKDVLRKASS DMSASAGYEE ISDPDMEEKP SLPPRKESII KSEGELLERE 540
RERQRTEQLR GPTPKPPGVI LPMMPAKHIP PARDSRRPEP KPDKSRLFQL KNDMGLECGH 600
KVLAKEVKKP NLRPISKSKT DLPEEKPDAT PQNPFLKSRP QVRPKPAPSP KTEPPQGEDQ 660
VDICNLRSKL RPAKSQDKSL LDGEGPQAVG GQDVAFSRSF LPGEGPGRAQ DRTGKQDGLS 720
PKEISCRAPP RPAKTTDPVS KSVPVPLQEA PQQRPVVPPR RPPPPKKTSS SSRPLPEVRG 780
PQCEGHESRA APTPGRALLV PPKAKPFLSN SLGGQDDTRG KGSLGPWGTG KIGENREKAA 840
AASVPNADGL KDSLYVAVAD FEGDKDTSSF QEGTVFEVRE KNSSGWWFCQ VLSGAPSWEG 900
WIPSNYLRKK P 911 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0042995; C:cell projection; IEA:UniProtKB-KW.
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0002102; C:podosome; ISS:UniProtKB.
 GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
 GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
 GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:Compara.
 GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISS:UniProtKB.
 GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
 GO:0060612; P:adipose tissue development; ISS: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; IMP:UniProtKB.
 GO:0001654; P:eye development; IMP:UniProtKB.
 GO:0007507; P:heart development; IMP:UniProtKB.
 GO:0071800; P:podosome assembly; ISS:UniProtKB.
 GO:0045600; P:positive regulation of fat cell differentiation; IEA:Compara.
 GO:0072657; P:protein localization to membrane; IDA:UniProtKB.
 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