SPD2B_MOUSE - dbPTM
SPD2B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPD2B_MOUSE
UniProt AC A2AAY5
Protein Name SH3 and PX domain-containing protein 2B
Gene Name Sh3pxd2b
Organism Mus musculus (Mouse).
Sequence Length 908
Subcellular Localization Cytoplasm. Cell projection, podosome. Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells.
Protein 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..
Protein Sequence MPPRRSIVEVKVLDVQKRRVPNKHYVYIIRVTWSSGATEAIYRRYSKFFDLQMQMLDKFPMEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLIPIDEYCKALIQLPPYISQCDEVLQFFETRPEDLNPPKEEHIGKKKSGNDPTSVDPMVLEQYVVVADYQKQESSEISLSVGQVVDIIEKNESGWWFVSTAEEQGWVPATCLEGQDGVQDEFSLQPEEEEKYTVIYPYTARDQDEMNLERGAVVEVVQKNLEGWWKIRYQGKEGWAPASYLKKNSGEPLPPKLGPSSPAHSGALDLDGVSRHQNAMGREKELLNNQRDGRFEGRLVPDGDVKQRSPKMRQRPPPRRDMTIPRGLNLPKPPIPPQVEEEYYTIAEFQTTIPDGISFQAGLKVEVIEKSLSGWWYIQMEDKEGWAPATFIDKYKKTSSASRPNFLAPLPHEMTQLRLGDAAATENNTGPEAVGPSRPLPEAPHGAVDSGMLWSKDWKGGKEAPRKASSDLSASTGYEEISDPTQEEKPSLPPRKESIIKSEEELLERERQKMEPLRGSSPKPPGMILPMIPAKHAPLARDSRKPEPKLDKSKFPLRNDMGLECGHKVLAKEVKKPNLRPISRSKAELSEEKVDPTSQNLFMKSRPQVRPKPTPSPKTEPAQSEDHVDIYNLRSKLRPAKSQEKALLDGESHHAAGSHDTALSRSFLPGEGPGHGQDRSGRQDGLSPKETPCRAPPRPAKTTDPGPKNVPVPVQEATLQQRPVVPPRRPPPPKKTSSSPLSCRPLPEVRGAQREESRVAPAAGRALLVPPKAKPFLSNSSVGQDDMRGKGGLGPRVTGKVGETREKAASFLNADGPKDSLYVAVANFEGDEDTSSFQEGTVFEVREKNSSGWWFCQVLSGAPSWEGWIPSNYLRKKP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
25PhosphorylationRRVPNKHYVYIIRVT
CCCCCCEEEEEEEEE
9.1419144821
42PhosphorylationSGATEAIYRRYSKFF
CCHHHHHHHHHHHHH
8.9722817900
85PhosphorylationGKILFRRSHIRDVAV
CCEEEECHHHHHHHH
21.0020531401
226PhosphorylationQPEEEEKYTVIYPYT
CCCCHHCEEEEEEEC
14.9829514104
230PhosphorylationEEKYTVIYPYTARDQ
HHCEEEEEEECCCCC
5.95-
279PhosphorylationASYLKKNSGEPLPPK
HHHCCCCCCCCCCCC
54.11-
290PhosphorylationLPPKLGPSSPAHSGA
CCCCCCCCCCCCCCC
47.3522942356
291PhosphorylationPPKLGPSSPAHSGAL
CCCCCCCCCCCCCCC
29.2827087446
295PhosphorylationGPSSPAHSGALDLDG
CCCCCCCCCCCCCCH
28.0622942356
304PhosphorylationALDLDGVSRHQNAMG
CCCCCHHHHHHHCHH
29.5825777480
339PhosphorylationDGDVKQRSPKMRQRP
CCCHHHCCCCHHCCC
26.7824453211
353PhosphorylationPPPRRDMTIPRGLNL
CCCCCCCCCCCCCCC
31.92-
429PhosphorylationIDKYKKTSSASRPNF
HHHHHCCCCCCCCCC
32.5524719451
499PhosphorylationKEAPRKASSDLSAST
CCCCCCHHCCCCHHC
27.6727742792
500PhosphorylationEAPRKASSDLSASTG
CCCCCHHCCCCHHCC
47.6427742792
503PhosphorylationRKASSDLSASTGYEE
CCHHCCCCHHCCCCC
25.7625619855
505PhosphorylationASSDLSASTGYEEIS
HHCCCCHHCCCCCCC
20.9925619855
506PhosphorylationSSDLSASTGYEEISD
HCCCCHHCCCCCCCC
43.4225619855
508PhosphorylationDLSASTGYEEISDPT
CCCHHCCCCCCCCCC
15.5225619855
512PhosphorylationSTGYEEISDPTQEEK
HCCCCCCCCCCCCCC
40.6025619855
515PhosphorylationYEEISDPTQEEKPSL
CCCCCCCCCCCCCCC
54.3125619855
521PhosphorylationPTQEEKPSLPPRKES
CCCCCCCCCCCCHHH
65.6525619855
528PhosphorylationSLPPRKESIIKSEEE
CCCCCHHHHHCCHHH
32.4226824392
532PhosphorylationRKESIIKSEEELLER
CHHHHHCCHHHHHHH
39.5725619855
550PhosphorylationKMEPLRGSSPKPPGM
HCCCCCCCCCCCCCC
36.7126160508
551PhosphorylationMEPLRGSSPKPPGMI
CCCCCCCCCCCCCCE
39.5026824392
573PhosphorylationHAPLARDSRKPEPKL
CCCCCCCCCCCCCCC
36.3324719451
598AcetylationMGLECGHKVLAKEVK
CCCCCCHHHHHHHHC
24.9922826441
613PhosphorylationKPNLRPISRSKAELS
CCCCCCCCCCHHHHC
32.9329176673
620PhosphorylationSRSKAELSEEKVDPT
CCCHHHHCCCCCCCH
34.9023737553
661PhosphorylationSEDHVDIYNLRSKLR
CCCCEEHHHHHHHHC
12.0425338131
672PhosphorylationSKLRPAKSQEKALLD
HHHCCCHHHHHHHHC
45.7525159016
682PhosphorylationKALLDGESHHAAGSH
HHHHCCCCCCCCCCC
26.5429514104
688PhosphorylationESHHAAGSHDTALSR
CCCCCCCCCCCCCCC
17.2925338131
717PhosphorylationSGRQDGLSPKETPCR
CCCCCCCCCCCCCCC
39.1821743459
723GlutathionylationLSPKETPCRAPPRPA
CCCCCCCCCCCCCCC
8.2724333276
766PhosphorylationRPPPPKKTSSSPLSC
CCCCCCCCCCCCCCC
39.7123984901
767PhosphorylationPPPPKKTSSSPLSCR
CCCCCCCCCCCCCCC
37.3823984901
768PhosphorylationPPPKKTSSSPLSCRP
CCCCCCCCCCCCCCC
41.0024453211
769PhosphorylationPPKKTSSSPLSCRPL
CCCCCCCCCCCCCCC
29.6324453211
772PhosphorylationKTSSSPLSCRPLPEV
CCCCCCCCCCCCCHH
16.0924453211
840PhosphorylationETREKAASFLNADGP
CCHHHHHHHHCCCCC
34.8226824392

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SPD2B_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPD2B_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SPD2B_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SPD2B_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPD2B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-672 ANDSER-840, AND MASS SPECTROMETRY.

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