Search Results

Overview

Uniprot IDA1X283
Protein NameSH3 and PX domain-containing protein 2B
Gene NameSH3PXD2B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
619 LRPISKSKTDLPEEK
669 DICNLRSKLRPAKSQ
734 RAPPRPAKTTDPVSK
821 GQDDTRGKGSLGPWG
831 LGPWGTGKIGENREK
838 KIGENREKAAAASVP

Function

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)

Protein Sequence

10 MPPRRSIVEV 20 KVLDVQKRRV 30 PNKHYVYIIR 40 VTWSSGSTEA 50 IYRRYSKFFD 60 LQMQMLDKFP 70 MEGGQKDPKQ 80 RIIPFLPGKI 90 LFRRSHIRDV 100 AVKRLIPIDE 110 YCKALIQLPP 120 YISQCDEVLQ 130 FFETRPEDLN 140 PPKEEHIGKK 150 KSGGDQTSVD 160 PMVLEQYVVV 170 ANYQKQESSE 180 ISLSVGQVVD 190 IIEKNESGWW 200 FVSTAEEQGW 210 VPATCLEGQD 220 GVQDEFSLQP 230 EEEEKYTVIY 240 PYTARDQDEM 250 NLERGAVVEV 260 IQKNLEGWWK 270 IRYQGKEGWA 280 PASYLKKNSG 290 EPLPPKPGPG 300 SPSHPGALDL 310 DGVSRQQNAV 320 GREKELLSSQ 330 RDGRFEGRPV 340 PDGDAKQRSP 350 KMRQRPPPRR 360 DMTIPRGLNL 370 PKPPIPPQVE 380 EEYYTIAEFQ 390 TTIPDGISFQ 400 AGLKVEVIEK 410 NLSGWWYIQI 420 EDKEGWAPAT 430 FIDKYKKTSN 440 ASRPNFLAPL 450 PHEVTQLRLG 460 EAAALENNTG 470 SEATGPSRPL 480 PDAPHGVMDS 490 GLPWSKDWKG 500 SKDVLRKASS 510 DMSASAGYEE 520 ISDPDMEEKP 530 SLPPRKESII 540 KSEGELLERE 550 RERQRTEQLR 560 GPTPKPPGVI 570 LPMMPAKHIP 580 PARDSRRPEP 590 KPDKSRLFQL 600 KNDMGLECGH 610 KVLAKEVKKP 620 NLRPISKSKT 630 DLPEEKPDAT 640 PQNPFLKSRP 650 QVRPKPAPSP 660 KTEPPQGEDQ 670 VDICNLRSKL 680 RPAKSQDKSL 690 LDGEGPQAVG 700 GQDVAFSRSF 710 LPGEGPGRAQ 720 DRTGKQDGLS 730 PKEISCRAPP 740 RPAKTTDPVS 750 KSVPVPLQEA 760 PQQRPVVPPR 770 RPPPPKKTSS 780 SSRPLPEVRG 790 PQCEGHESRA 800 APTPGRALLV 810 PPKAKPFLSN 820 SLGGQDDTRG 830 KGSLGPWGTG 840 KIGENREKAA 850 AASVPNADGL 860 KDSLYVAVAD 870 FEGDKDTSSF 880 QEGTVFEVRE 890 KNSSGWWFCQ 900 VLSGAPSWEG 910 WIPSNYLRKK P

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0002102 podosome
Molecular Function GO:0080025 phosphatidylinositol-3,5-bisphosphate binding
Molecular Function GO:0032266 phosphatidylinositol-3-phosphate binding
Molecular Function GO:0010314 phosphatidylinositol-5-phosphate binding
Molecular Function GO:0042169 SH2 domain binding
Molecular Function GO:0016176 superoxide-generating NADPH oxidase activator activity
Biological Process GO:0060612 adipose tissue development
Biological Process GO:0060348 bone development
Biological Process GO:0030154 cell differentiation
Biological Process GO:0022617 extracellular matrix disassembly
Biological Process GO:0001654 eye development
Biological Process GO:0007507 heart development
Biological Process GO:0071800 podosome assembly
Biological Process GO:0072657 protein localization to membrane
Biological Process GO:0001501 skeletal system development
Biological Process GO:0042554 superoxide anion generation
Biological Process GO:0006801 superoxide metabolic process

Reference

[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[2] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.