dbPTM

SHCBP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SHCBP_HUMAN
UniProt AC	Q8NEM2
Protein Name	SHC SH2 domain-binding protein 1
Gene Name	SHCBP1
Organism	Homo sapiens (Human).
Sequence Length	672
Subcellular Localization	Midbody . Cytoplasm, cytoskeleton, spindle . Displays weak localization to the spindle midzone in some early telophase cells and is concentrated at the midbody in late cytokinesis.
Protein Description	May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc. Acts as a positive regulator of FGF signaling in neural progenitor cells..
Protein Sequence	MADGSLTGGGLEAAAMAPERMGWAVEQELASLEKGLFQDEDSCSDCSYRDKPGSSLQSFMPEGKTFFPEIFQTNQLLFYERFRAYQDYILADCKASEVQEFTAEFLEKVLEPSGWRAVWHTNVFKVLVEITDVDFAALKAVVRLAEPYLCDSQVSTFTMECMKELLDLKEHRLPLQELWVVFDDSGVFDQTALAIEHVRFFYQNIWRSWDEEEEDEYDYFVRCVEPRLRLHYDILEDRVPSGLIVDYHNLLSQCEESYRKFLNLRSSLSNCNSDSEQENISMVEGLKLYSEMEQLKQKLKLIENPLLRYVFGYQKNSNIQAKGVRSSGQKITHVVSSTMMAGLLRSLLTDRLCQEPGEEEREIQFHSDPLSAINACFEGDTVIVCPGHYVVHGTFSIADSIELEGYGLPDDIVIEKRGKGDTFVDCTGADIKISGIKFVQHDAVEGILIVHRGKTTLENCVLQCETTGVTVRTSAEFLMKNSDLYGAKGAGIEIYPGSQCTLSDNGIHHCKEGILIKDFLDEHYDIPKISMVNNIIHNNEGYGVVLVKPTIFSDLQENAEDGTEENKALKIQTSGEPDVAERVDLEELIECATGKMELCARTDPSEQVEGNCEIVNELIAASTQKGQIKKKRLSELGITQADDNLMSQEMFVGIVGNQFKWNGKGSFGTFLF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADGSLTGG ------CCCCCCCCC	29.85	22223895
5	Phosphorylation	---MADGSLTGGGLE ---CCCCCCCCCHHH	24.25	25159151
7	Phosphorylation	-MADGSLTGGGLEAA -CCCCCCCCCHHHHH	35.16	20068231
31	Phosphorylation	AVEQELASLEKGLFQ HHHHHHHHHHCCCCC	50.08	18669648
42	Phosphorylation	GLFQDEDSCSDCSYR CCCCCCCCCCCCCCC	17.30	22167270
44	Phosphorylation	FQDEDSCSDCSYRDK CCCCCCCCCCCCCCC	45.67	30266825
47	Phosphorylation	EDSCSDCSYRDKPGS CCCCCCCCCCCCCCC	28.35	30266825
48	Phosphorylation	DSCSDCSYRDKPGSS CCCCCCCCCCCCCCC	29.21	23927012
51	Ubiquitination	SDCSYRDKPGSSLQS CCCCCCCCCCCCHHH	42.13	21890473
54	Phosphorylation	SYRDKPGSSLQSFMP CCCCCCCCCHHHHCC	36.08	25159151
55	Phosphorylation	YRDKPGSSLQSFMPE CCCCCCCCHHHHCCC	36.02	25159151
58	Phosphorylation	KPGSSLQSFMPEGKT CCCCCHHHHCCCCCC	28.89	23663014
64	Sumoylation	QSFMPEGKTFFPEIF HHHCCCCCCCCHHHH	40.26	-
85	Phosphorylation	FYERFRAYQDYILAD HHHHHHHHCHHHHHC	9.54	-
88	Phosphorylation	RFRAYQDYILADCKA HHHHHCHHHHHCCCH	5.15	-
94	Ubiquitination	DYILADCKASEVQEF HHHHHCCCHHHHHHH	56.33	-
96	Phosphorylation	ILADCKASEVQEFTA HHHCCCHHHHHHHHH	24.64	20068231
102	Phosphorylation	ASEVQEFTAEFLEKV HHHHHHHHHHHHHHH	25.23	20068231
108	Ubiquitination	FTAEFLEKVLEPSGW HHHHHHHHHHCCCCC	55.02	-
139	Ubiquitination	DVDFAALKAVVRLAE CCCHHHHHHHHHHHC	34.11	21890473
148	Phosphorylation	VVRLAEPYLCDSQVS HHHHHCCCCCCCHHH	16.09	30177828
152	Phosphorylation	AEPYLCDSQVSTFTM HCCCCCCCHHHHHHH	31.33	30177828
155	Phosphorylation	YLCDSQVSTFTMECM CCCCCHHHHHHHHHH	15.34	30177828
156	Phosphorylation	LCDSQVSTFTMECMK CCCCHHHHHHHHHHH	25.03	30177828
158	Phosphorylation	DSQVSTFTMECMKEL CCHHHHHHHHHHHHH	16.49	30177828
169	Ubiquitination	MKELLDLKEHRLPLQ HHHHHHHHHHCCCHH	51.66	-
217	Phosphorylation	DEEEEDEYDYFVRCV CHHHCCCCCCHHHHH	28.41	22817900
219	Phosphorylation	EEEDEYDYFVRCVEP HHCCCCCCHHHHHCC	11.76	22817900
260	Ubiquitination	QCEESYRKFLNLRSS HCHHHHHHHHHHHHH	46.07	-
266	Phosphorylation	RKFLNLRSSLSNCNS HHHHHHHHHHHCCCC	38.50	30278072
267	Phosphorylation	KFLNLRSSLSNCNSD HHHHHHHHHHCCCCC	29.41	23663014
269	Phosphorylation	LNLRSSLSNCNSDSE HHHHHHHHCCCCCCH	41.08	30266825
273	Phosphorylation	SSLSNCNSDSEQENI HHHHCCCCCCHHHHH	44.72	30266825
275	Phosphorylation	LSNCNSDSEQENISM HHCCCCCCHHHHHHH	40.79	30266825
281	Phosphorylation	DSEQENISMVEGLKL CCHHHHHHHHHHHHH	28.49	29396449
287	Ubiquitination	ISMVEGLKLYSEMEQ HHHHHHHHHHHHHHH	57.12	-
289	Phosphorylation	MVEGLKLYSEMEQLK HHHHHHHHHHHHHHH	10.86	-
296	Ubiquitination	YSEMEQLKQKLKLIE HHHHHHHHHHHHHHH	45.11	21890473
300	Ubiquitination	EQLKQKLKLIENPLL HHHHHHHHHHHCHHH	55.22	21890473
313	Phosphorylation	LLRYVFGYQKNSNIQ HHHHHHCCCCCCCCC	12.59	19413330
315	Ubiquitination	RYVFGYQKNSNIQAK HHHHCCCCCCCCCEE	54.59	21890473
322	Ubiquitination	KNSNIQAKGVRSSGQ CCCCCCEECCCCCCC	41.38	-
326	Phosphorylation	IQAKGVRSSGQKITH CCEECCCCCCCCCHH	36.09	24719451
332	Phosphorylation	RSSGQKITHVVSSTM CCCCCCCHHHHHHHH	18.69	24719451
336	Phosphorylation	QKITHVVSSTMMAGL CCCHHHHHHHHHHHH	21.00	24043423
337	Phosphorylation	KITHVVSSTMMAGLL CCHHHHHHHHHHHHH	14.54	24043423
338	Phosphorylation	ITHVVSSTMMAGLLR CHHHHHHHHHHHHHH	11.94	24043423
349	Phosphorylation	GLLRSLLTDRLCQEP HHHHHHHHHHHCCCC	25.11	24719451
406	Phosphorylation	DSIELEGYGLPDDIV CEEEEECCCCCCCEE	13.20	16094384
419	Ubiquitination	IVIEKRGKGDTFVDC EEEEECCCCCEEEEC	58.61	21890473
432	Ubiquitination	DCTGADIKISGIKFV ECCCCCEEECCEEEE	31.22	-
434	Phosphorylation	TGADIKISGIKFVQH CCCCEEECCEEEEEE	29.48	23532336
454	Ubiquitination	ILIVHRGKTTLENCV EEEEECCEECHHCCE	37.99	-
474	Phosphorylation	TGVTVRTSAEFLMKN CCCEEECCHHHHHHC	18.42	16964243
480	Ubiquitination	TSAEFLMKNSDLYGA CCHHHHHHCCCCCCC	56.28	-
488	Ubiquitination	NSDLYGAKGAGIEIY CCCCCCCCCCCCEEE	44.95	-
511	Ubiquitination	DNGIHHCKEGILIKD CCCCCCCCCCEEEHH	55.40	-
517	Ubiquitination	CKEGILIKDFLDEHY CCCCEEEHHHHHHCC	38.69	-
524	Phosphorylation	KDFLDEHYDIPKISM HHHHHHCCCCCCEEE	17.33	28796482
548	Ubiquitination	GYGVVLVKPTIFSDL CEEEEEECCCCCHHH	32.08	-
567	Sumoylation	EDGTEENKALKIQTS CCCCHHHCCEEEEEC	59.38	-
570	Ubiquitination	TEENKALKIQTSGEP CHHHCCEEEEECCCC	37.31	-
573	Phosphorylation	NKALKIQTSGEPDVA HCCEEEEECCCCCHH	42.02	18669648
574	Phosphorylation	KALKIQTSGEPDVAE CCEEEEECCCCCHHH	25.45	21815630
595	Ubiquitination	LIECATGKMELCART HHHHHCCCCEEEECC	25.50	-
622	Phosphorylation	VNELIAASTQKGQIK HHHHHHHHCCCCCCC	23.50	25159151
625	Ubiquitination	LIAASTQKGQIKKKR HHHHHCCCCCCCHHH	53.52	-
634	Phosphorylation	QIKKKRLSELGITQA CCCHHHHHHCCCCCC	34.50	25159151
639	Phosphorylation	RLSELGITQADDNLM HHHHCCCCCCCCCHH	18.86	27251275
647	Phosphorylation	QADDNLMSQEMFVGI CCCCCHHHCCCEEEE	26.59	22617229
664	Ubiquitination	NQFKWNGKGSFGTFL CCEEECCCCCCEECC	48.44	-

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
634	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ZUFSP_HUMAN	ZUFSP	physical	16189514

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SHCBP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-273, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-31; SER-42; SER-44;SER-47; SER-273 AND SER-634, AND MASS SPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.	15302935 [Abstract]