3BP5L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: 3BP5L_HUMAN
• UniProt AC: Q7L8J4
• Protein Name: SH3 domain-binding protein 5-like
• Gene Name: SH3BP5L
• Organism: Homo sapiens (Human).
• Sequence Length: 393
• Protein Sequence: MAELRQVPGGRETPQGELRPEVVEDEVPRSPVAEEPGGGGSSSSEAKLSPREEEELDPRIQEELEHLNQASEEINQVELQLDEARTTYRRILQESARKLNTQGSHLGSCIEKARPYYEARRLAKEAQQETQKAALRYERAVSMHNAAREMVFVAEQGVMADKNRLDPTWQEMLNHATCKVNEAEEERLRGEREHQRVTRLCQQAEARVQALQKTLRRAIGKSRPYFELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALRNLEQISEQIHARRRGGLPPHPLGPRRSSPVGAEAGPEDMEDGDSGIEGAEGAGLEEGSSLGPGPAPDTDTLSLLSLRTVASDLQKCDSVEHLRGLSDHVSLDGQELGTRSGGRRGSDGGARGGRHQRSVSL

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
13	Phosphorylation	QVPGGRETPQGELRP CCCCCCCCCCCCCCH	21.39	29255136
30	Phosphorylation	VEDEVPRSPVAEEPG HCCCCCCCCCCCCCC	20.04	30266825
41	Phosphorylation	EEPGGGGSSSSEAKL CCCCCCCCCCCCCCC	30.26	23663014
42	Phosphorylation	EPGGGGSSSSEAKLS CCCCCCCCCCCCCCC	40.95	23663014
43	Phosphorylation	PGGGGSSSSEAKLSP CCCCCCCCCCCCCCH	33.62	23663014
44	Phosphorylation	GGGGSSSSEAKLSPR CCCCCCCCCCCCCHH	43.45	23663014
49	Phosphorylation	SSSEAKLSPREEEEL CCCCCCCCHHHHHHC	22.62	29255136
112	Ubiquitination	HLGSCIEKARPYYEA CHHHHHHHHHHHHHH	29.77	-
142	Phosphorylation	LRYERAVSMHNAARE HHHHHHHHHHHHHHH	17.22	27251275
143	Sulfoxidation	RYERAVSMHNAAREM HHHHHHHHHHHHHHH	1.96	30846556
213	Ubiquitination	ARVQALQKTLRRAIG HHHHHHHHHHHHHHC	50.83	-
233	Phosphorylation	FELKAQFSQILEEHK HHHHHHHHHHHHHHH	12.30	28857561
254	Ubiquitination	EQQVAQAKTRYSVAL HHHHHHHHHHHHHHH	22.81	-
334	Phosphorylation	APDTDTLSLLSLRTV CCCCCHHHHHHHHHH	29.38	25921289
337	Phosphorylation	TDTLSLLSLRTVASD CCHHHHHHHHHHHHH	22.54	25921289
340	Phosphorylation	LSLLSLRTVASDLQK HHHHHHHHHHHHHHH	26.22	30266825
343	Phosphorylation	LSLRTVASDLQKCDS HHHHHHHHHHHHCCC	34.22	29255136
350	Phosphorylation	SDLQKCDSVEHLRGL HHHHHCCCHHHHCCC	38.58	23401153
358	Phosphorylation	VEHLRGLSDHVSLDG HHHHCCCCCCEEECC	28.61	29255136
362	Phosphorylation	RGLSDHVSLDGQELG CCCCCCEEECCCCCC	19.81	29255136
370	Phosphorylation	LDGQELGTRSGGRRG ECCCCCCCCCCCCCC	34.00	23927012
378	Phosphorylation	RSGGRRGSDGGARGG CCCCCCCCCCCCCCC	31.13	26699800
390	Phosphorylation	RGGRHQRSVSL---- CCCCCCCCCCC----	14.97	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of 3BP5L_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of 3BP5L_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of 3BP5L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BICD1_HUMAN	BICD1	physical	28514442
THG1_HUMAN	THG1L	physical	28514442
TNKS1_HUMAN	TNKS	physical	28514442
TNKS2_HUMAN	TNKS2	physical	28514442
FBW1A_HUMAN	BTRC	physical	28514442
MYPT1_HUMAN	PPP1R12A	physical	28514442
HEXI1_HUMAN	HEXIM1	physical	28514442
MIPO1_HUMAN	MIPOL1	physical	28514442
FBW1B_HUMAN	FBXW11	physical	28514442
CARM1_HUMAN	CARM1	physical	28514442
FL2D_HUMAN	WTAP	physical	28514442

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-362, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-343; SER-350 ANDSER-362, AND MASS SPECTROMETRY.
PubMed: 18669648