dbPTM

STALP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STALP_HUMAN
UniProt AC	Q96FJ0
Protein Name	AMSH-like protease
Gene Name	STAMBPL1
Organism	Homo sapiens (Human).
Sequence Length	436
Subcellular Localization
Protein Description	Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains..
Protein Sequence	MDQPFTVNSLKKLAAMPDHTDVSLSPEERVRALSKLGCNITISEDITPRRYFRSGVEMERMASVYLEEGNLENAFVLYNKFITLFVEKLPNHRDYQQCAVPEKQDIMKKLKEIAFPRTDELKNDLLKKYNVEYQEYLQSKNKYKAEILKKLEHQRLIEAERKRIAQMRQQQLESEQFLFFEDQLKKQELARGQMRSQQTSGLSEQIDGSALSCFSTHQNNSLLNVFADQPNKSDATNYASHSPPVNRALTPAATLSAVQNLVVEGLRCVVLPEDLCHKFLQLAESNTVRGIETCGILCGKLTHNEFTITHVIVPKQSAGPDYCDMENVEELFNVQDQHDLLTLGWIHTHPTQTAFLSSVDLHTHCSYQLMLPEAIAIVCSPKHKDTGIFRLTNAGMLEVSACKKKGFHPHTKEPRLFSICKHVLVKDIKIIVLDLR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDQPFTVN -------CCCCCCHH	11.02	22814378
6	Phosphorylation	--MDQPFTVNSLKKL --CCCCCCHHHHHHH	26.01	29255136
9	Phosphorylation	DQPFTVNSLKKLAAM CCCCCHHHHHHHHCC	36.91	29255136
12	Ubiquitination	FTVNSLKKLAAMPDH CCHHHHHHHHCCCCC	48.96	-
23	Phosphorylation	MPDHTDVSLSPEERV CCCCCCCCCCHHHHH	26.41	29255136
25	Phosphorylation	DHTDVSLSPEERVRA CCCCCCCCHHHHHHH	23.82	29255136
41	Phosphorylation	SKLGCNITISEDITP HHCCCCEEECCCCCH	12.40	-
47	Phosphorylation	ITISEDITPRRYFRS EEECCCCCHHHHCCC	24.06	25159151
111	Ubiquitination	QDIMKKLKEIAFPRT HHHHHHHHHHCCCCC	56.82	33845483
122	Ubiquitination	FPRTDELKNDLLKKY CCCCHHHHHHHHHHH	46.50	29967540
128	Ubiquitination	LKNDLLKKYNVEYQE HHHHHHHHHCHHHHH	41.86	-
129	Phosphorylation	KNDLLKKYNVEYQEY HHHHHHHHCHHHHHH	23.89	23828894
140	Ubiquitination	YQEYLQSKNKYKAEI HHHHHHCCCHHHHHH	44.49	29967540
142	Ubiquitination	EYLQSKNKYKAEILK HHHHCCCHHHHHHHH	52.44	-
144	Ubiquitination	LQSKNKYKAEILKKL HHCCCHHHHHHHHHH	40.95	-
233	Phosphorylation	FADQPNKSDATNYAS ECCCCCCCCCCCCCC	38.83	21945579
236	Phosphorylation	QPNKSDATNYASHSP CCCCCCCCCCCCCCC	33.48	21945579
238	Phosphorylation	NKSDATNYASHSPPV CCCCCCCCCCCCCCC	12.72	21945579
240	Phosphorylation	SDATNYASHSPPVNR CCCCCCCCCCCCCCC	17.71	21945579
242	Phosphorylation	ATNYASHSPPVNRAL CCCCCCCCCCCCCCC	28.53	22167270
250	Phosphorylation	PPVNRALTPAATLSA CCCCCCCCHHHHHHH	15.19	29496963
254	Phosphorylation	RALTPAATLSAVQNL CCCCHHHHHHHHHHH	24.29	26074081
256	Phosphorylation	LTPAATLSAVQNLVV CCHHHHHHHHHHHHH	23.26	27732954
278	Ubiquitination	LPEDLCHKFLQLAES CCHHHHHHHHHHHHC	46.93	-
386	Phosphorylation	CSPKHKDTGIFRLTN CCCCCCCCCEEEECC	36.66	29759185
392	Phosphorylation	DTGIFRLTNAGMLEV CCCEEEECCCCEEEE	20.83	20068231
400	Phosphorylation	NAGMLEVSACKKKGF CCCEEEEHHHHCCCC	20.69	20068231
412	Ubiquitination	KGFHPHTKEPRLFSI CCCCCCCCCCHHHHH	63.79	29967540
426	Ubiquitination	ICKHVLVKDIKIIVL HHHHHHHCCEEEEEE	49.96	29967540

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
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF2	Q9HAU4	PMID:22199232

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RU2A_HUMAN	SNRPA1	physical	19615732
UBE2N_HUMAN	UBE2N	physical	19615732
EPN4_HUMAN	CLINT1	physical	19615732
UBP49_HUMAN	USP49	physical	19615732
OTUB1_HUMAN	OTUB1	physical	19615732
HMX3_HUMAN	HMX3	physical	19615732
CLH1_HUMAN	CLTC	physical	16716190
UBC_HUMAN	UBC	physical	18758443
RNF32_HUMAN	RNF32	physical	21163940
GNPTA_HUMAN	GNPTAB	physical	25416956
INCA1_HUMAN	INCA1	physical	25416956
RAB2A_HUMAN	RAB2A	physical	21516116
HIP1R_HUMAN	HIP1R	physical	28514442
STABP_HUMAN	STAMBP	physical	28514442
P3C2A_HUMAN	PIK3C2A	physical	28514442
CLH2_HUMAN	CLTCL1	physical	28514442
GAK_HUMAN	GAK	physical	28514442
GTSE1_HUMAN	GTSE1	physical	28514442
BMP2K_HUMAN	BMP2K	physical	28514442
PICAL_HUMAN	PICALM	physical	28514442
SMAP2_HUMAN	SMAP2	physical	28514442
ZN106_HUMAN	ZNF106	physical	28514442
SI1L1_HUMAN	SIPA1L1	physical	28514442
EPS15_HUMAN	EPS15	physical	28514442
NUMB_HUMAN	NUMB	physical	28514442
REPS1_HUMAN	REPS1	physical	28514442
STX8_HUMAN	STX8	physical	28514442
VTI1B_HUMAN	VTI1B	physical	28514442
EPN4_HUMAN	CLINT1	physical	28514442
CLH1_HUMAN	CLTC	physical	28514442
GRIN1_HUMAN	GPRIN1	physical	28514442
WNK1_HUMAN	WNK1	physical	28514442
AP1B1_HUMAN	AP1B1	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.

Regulatory Network of STALP_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-25 AND SER-242, AND MASSSPECTROMETRY.	18669648 [Abstract]