dbPTM

SPD2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPD2B_HUMAN
UniProt AC	A1X283
Protein Name	SH3 and PX domain-containing protein 2B
Gene Name	SH3PXD2B
Organism	Homo sapiens (Human).
Sequence Length	911
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 (By similarity)..
Protein Sequence	MPPRRSIVEVKVLDVQKRRVPNKHYVYIIRVTWSSGSTEAIYRRYSKFFDLQMQMLDKFPMEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLIPIDEYCKALIQLPPYISQCDEVLQFFETRPEDLNPPKEEHIGKKKSGGDQTSVDPMVLEQYVVVANYQKQESSEISLSVGQVVDIIEKNESGWWFVSTAEEQGWVPATCLEGQDGVQDEFSLQPEEEEKYTVIYPYTARDQDEMNLERGAVVEVIQKNLEGWWKIRYQGKEGWAPASYLKKNSGEPLPPKPGPGSPSHPGALDLDGVSRQQNAVGREKELLSSQRDGRFEGRPVPDGDAKQRSPKMRQRPPPRRDMTIPRGLNLPKPPIPPQVEEEYYTIAEFQTTIPDGISFQAGLKVEVIEKNLSGWWYIQIEDKEGWAPATFIDKYKKTSNASRPNFLAPLPHEVTQLRLGEAAALENNTGSEATGPSRPLPDAPHGVMDSGLPWSKDWKGSKDVLRKASSDMSASAGYEEISDPDMEEKPSLPPRKESIIKSEGELLERERERQRTEQLRGPTPKPPGVILPMMPAKHIPPARDSRRPEPKPDKSRLFQLKNDMGLECGHKVLAKEVKKPNLRPISKSKTDLPEEKPDATPQNPFLKSRPQVRPKPAPSPKTEPPQGEDQVDICNLRSKLRPAKSQDKSLLDGEGPQAVGGQDVAFSRSFLPGEGPGRAQDRTGKQDGLSPKEISCRAPPRPAKTTDPVSKSVPVPLQEAPQQRPVVPPRRPPPPKKTSSSSRPLPEVRGPQCEGHESRAAPTPGRALLVPPKAKPFLSNSLGGQDDTRGKGSLGPWGTGKIGENREKAAAASVPNADGLKDSLYVAVADFEGDKDTSSFQEGTVFEVREKNSSGWWFCQVLSGAPSWEGWIPSNYLRKKP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MPPRRSIVEVKVL --CCCCCCEEEEEEE	32.06	24719451
17	Acetylation	VKVLDVQKRRVPNKH EEEEEECCCCCCCCE	41.86	20167786
25	Phosphorylation	RRVPNKHYVYIIRVT CCCCCCEEEEEEEEE	9.14	19060867
27	Phosphorylation	VPNKHYVYIIRVTWS CCCCEEEEEEEEEEC	5.40	-
32	Phosphorylation	YVYIIRVTWSSGSTE EEEEEEEEECCCCHH	15.13	27251275
34	Phosphorylation	YIIRVTWSSGSTEAI EEEEEEECCCCHHHH	18.56	27251275
35	Phosphorylation	IIRVTWSSGSTEAIY EEEEEECCCCHHHHH	28.46	27251275
37	Phosphorylation	RVTWSSGSTEAIYRR EEEECCCCHHHHHHH	25.64	24719451
38	Phosphorylation	VTWSSGSTEAIYRRY EEECCCCHHHHHHHH	32.72	27251275
42	Phosphorylation	SGSTEAIYRRYSKFF CCCHHHHHHHHHHHH	8.97	-
45	Phosphorylation	TEAIYRRYSKFFDLQ HHHHHHHHHHHHHHH	13.76	28509920
46	Phosphorylation	EAIYRRYSKFFDLQM HHHHHHHHHHHHHHH	22.60	28509920
79	Ubiquitination	IIPFLPGKILFRRSH EECCCCCCEEEECHH	34.01	21890473
85	Phosphorylation	GKILFRRSHIRDVAV CCEEEECHHHHHHHH	21.00	24719451
142	Phosphorylation	EHIGKKKSGGDQTSV HHCCCCCCCCCCCCC	57.81	21712546
147	Phosphorylation	KKSGGDQTSVDPMVL CCCCCCCCCCCHHHH	35.14	21712546
226	Phosphorylation	QPEEEEKYTVIYPYT CCCCHHCEEEEEEEC	14.98	28102081
227	Phosphorylation	PEEEEKYTVIYPYTA CCCHHCEEEEEEECC	16.11	28102081
230	Phosphorylation	EEKYTVIYPYTARDQ HHCEEEEEEECCCCC	5.95	-
232	Phosphorylation	KYTVIYPYTARDQDE CEEEEEEECCCCCHH	8.96	-
276	Ubiquitination	WAPASYLKKNSGEPL CCCHHHCCCCCCCCC	41.49	-
279	Phosphorylation	ASYLKKNSGEPLPPK HHHCCCCCCCCCCCC	54.11	29978859
291	Phosphorylation	PPKPGPGSPSHPGAL CCCCCCCCCCCCCCC	26.77	29255136
293	Phosphorylation	KPGPGSPSHPGALDL CCCCCCCCCCCCCCC	43.97	30266825
304	Phosphorylation	ALDLDGVSRQQNAVG CCCCCCCCCCCCCCH	29.87	24732914
318	Phosphorylation	GREKELLSSQRDGRF HHHHHHHHHCCCCCC	36.73	23312004
319	Phosphorylation	REKELLSSQRDGRFE HHHHHHHHCCCCCCC	29.24	28857561
339	Phosphorylation	DGDAKQRSPKMRQRP CCCHHHCCHHHHCCC	26.78	24719451
353	Phosphorylation	PPPRRDMTIPRGLNL CCCCCCCCCCCCCCC	31.92	20068231
373	Phosphorylation	PPQVEEEYYTIAEFQ CCCCCCEEEEEEEEE	14.80	-
374	Phosphorylation	PQVEEEYYTIAEFQT CCCCCEEEEEEEEEC	8.58	-
428	Phosphorylation	FIDKYKKTSNASRPN HHHHHHCCCCCCCCC	24.06	28348404
429	Phosphorylation	IDKYKKTSNASRPNF HHHHHCCCCCCCCCC	39.00	28348404
432	Phosphorylation	YKKTSNASRPNFLAP HHCCCCCCCCCCCCC	53.15	28348404
491	Phosphorylation	WSKDWKGSKDVLRKA CCCCCCCCHHHHHHH	23.19	24719451
499	Phosphorylation	KDVLRKASSDMSASA HHHHHHHHHCCCHHC	29.88	26133373
500	Phosphorylation	DVLRKASSDMSASAG HHHHHHHHCCCHHCC	42.04	26657352
503	Phosphorylation	RKASSDMSASAGYEE HHHHHCCCHHCCCCC	24.86	26657352
505	Phosphorylation	ASSDMSASAGYEEIS HHHCCCHHCCCCCCC	18.21	26657352
508	Phosphorylation	DMSASAGYEEISDPD CCCHHCCCCCCCCCC	15.31	26657352
512	Phosphorylation	SAGYEEISDPDMEEK HCCCCCCCCCCCCCC	46.50	28985074
521	Phosphorylation	PDMEEKPSLPPRKES CCCCCCCCCCCCHHH	65.65	24719451
528	Phosphorylation	SLPPRKESIIKSEGE CCCCCHHHHHCCHHH	32.42	30266825
531	Sumoylation	PRKESIIKSEGELLE CCHHHHHCCHHHHHH	40.56	-
531	Sumoylation	PRKESIIKSEGELLE CCHHHHHCCHHHHHH	40.56	-
532	Phosphorylation	RKESIIKSEGELLER CHHHHHCCHHHHHHH	40.19	30266825
546	Phosphorylation	RERERQRTEQLRGPT HHHHHHHHHHHCCCC	21.53	27251275
553	Phosphorylation	TEQLRGPTPKPPGVI HHHHCCCCCCCCCEE	46.93	24719451
601	Acetylation	MGLECGHKVLAKEVK CCCCCCHHHHHHHHC	24.99	26051181
618	Phosphorylation	NLRPISKSKTDLPEE CCCCCCCCCCCCCCC	33.72	28857561
619	Methylation	LRPISKSKTDLPEEK CCCCCCCCCCCCCCC	50.20	24129315
620	Phosphorylation	RPISKSKTDLPEEKP CCCCCCCCCCCCCCC	50.27	28857561
630	Phosphorylation	PEEKPDATPQNPFLK CCCCCCCCCCCCCCC	32.55	25159151
649	Phosphorylation	VRPKPAPSPKTEPPQ CCCCCCCCCCCCCCC	40.93	30576142
652	Phosphorylation	KPAPSPKTEPPQGED CCCCCCCCCCCCCCC	58.05	30576142
675	Phosphorylation	SKLRPAKSQDKSLLD HHCCCCCCCCCCCCC	45.80	23927012
679	Phosphorylation	PAKSQDKSLLDGEGP CCCCCCCCCCCCCCC	42.32	25159151
697	Phosphorylation	GGQDVAFSRSFLPGE CCEEEEEECCCCCCC	19.78	23312004
699	Phosphorylation	QDVAFSRSFLPGEGP EEEEEECCCCCCCCC	29.91	24173317
713	Phosphorylation	PGRAQDRTGKQDGLS CCCCCCCCCCCCCCC	57.95	23403867
720	Phosphorylation	TGKQDGLSPKEISCR CCCCCCCCHHHCCCC	39.18	21815630
735	Phosphorylation	APPRPAKTTDPVSKS CCCCCCCCCCCCCCC	38.24	24275569
768	Phosphorylation	RPPPPKKTSSSSRPL CCCCCCCCCCCCCCC	39.71	30576142
769	Phosphorylation	PPPPKKTSSSSRPLP CCCCCCCCCCCCCCC	36.78	26699800
770	Phosphorylation	PPPKKTSSSSRPLPE CCCCCCCCCCCCCCC	37.25	26657352
771	Phosphorylation	PPKKTSSSSRPLPEV CCCCCCCCCCCCCCC	30.08	26699800
772	Phosphorylation	PKKTSSSSRPLPEVR CCCCCCCCCCCCCCC	39.61	26699800
788	Phosphorylation	PQCEGHESRAAPTPG CCCCCCCCCCCCCCC	22.88	21406692
805	Malonylation	LLVPPKAKPFLSNSL EECCCCCCCCCCCCC	42.29	26320211
805	Acetylation	LLVPPKAKPFLSNSL EECCCCCCCCCCCCC	42.29	26051181
809	Phosphorylation	PKAKPFLSNSLGGQD CCCCCCCCCCCCCCC	25.42	26657352
811	Phosphorylation	AKPFLSNSLGGQDDT CCCCCCCCCCCCCCC	25.64	26657352
818	Phosphorylation	SLGGQDDTRGKGSLG CCCCCCCCCCCCCCC	50.00	29255136
821	Methylation	GQDDTRGKGSLGPWG CCCCCCCCCCCCCCC	41.87	115981265
823	Phosphorylation	DDTRGKGSLGPWGTG CCCCCCCCCCCCCCC	33.37	28857561
829	Phosphorylation	GSLGPWGTGKIGENR CCCCCCCCCCCCCCH	31.28	-
843	Phosphorylation	REKAAAASVPNADGL HHHHHHHCCCCCCCC	33.12	-
853	Phosphorylation	NADGLKDSLYVAVAD CCCCCCCCEEEEEEC	21.73	27251275
855	Phosphorylation	DGLKDSLYVAVADFE CCCCCCEEEEEECCC	7.13	27251275

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
508	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPD2B_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SPD2B_HUMAN !!

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
249420	Frank-Ter Haar syndrome (FTHS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SPD2B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25, AND MASSSPECTROMETRY.	18083107 [Abstract]