dbPTM

STABP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STABP_HUMAN
UniProt AC	O95630
Protein Name	STAM-binding protein
Gene Name	STAMBP
Organism	Homo sapiens (Human).
Sequence Length	424
Subcellular Localization	Nucleus. Membrane Peripheral membrane protein. Cytoplasm. Early endosome.
Protein Description	Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization (By similarity). Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways..
Protein Sequence	MSDHGDVSLPPEDRVRALSQLGSAVEVNEDIPPRRYFRSGVEIIRMASIYSEEGNIEHAFILYNKYITLFIEKLPKHRDYKSAVIPEKKDTVKKLKEIAFPKAEELKAELLKRYTKEYTEYNEEKKKEAEELARNMAIQQELEKEKQRVAQQKQQQLEQEQFHAFEEMIRNQELEKERLKIVQEFGKVDPGLGGPLVPDLEKPSLDVFPTLTVSSIQPSDCHTTVRPAKPPVVDRSLKPGALSNSESIPTIDGLRHVVVPGRLCPQFLQLASANTARGVETCGILCGKLMRNEFTITHVLIPKQSAGSDYCNTENEEELFLIQDQQGLITLGWIHTHPTQTAFLSSVDLHTHCSYQMMLPESVAIVCSPKFQETGFFKLTDHGLEEISSCRQKGFHPHSKDPPLFCSCSHVTVVDRAVTITDLR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDHGDVSL ------CCCCCCCCC	38.01	30108239
19	Phosphorylation	EDRVRALSQLGSAVE HHHHHHHHHHCCCEE	23.52	30850117
39	Phosphorylation	PPRRYFRSGVEIIRM CCHHHCCCCCEEEEE	36.97	46163135
48	Phosphorylation	VEIIRMASIYSEEGN CEEEEEEECCCCCCC	16.83	28348404
50	Phosphorylation	IIRMASIYSEEGNIE EEEEEECCCCCCCEE	13.92	28122231
51	Phosphorylation	IRMASIYSEEGNIEH EEEEECCCCCCCEEE	27.74	28348404
81	Ubiquitination	LPKHRDYKSAVIPEK CCCCCCHHHCCCCCC	35.91	-
82	Phosphorylation	PKHRDYKSAVIPEKK CCCCCHHHCCCCCCH	22.87	27470641
88	Acetylation	KSAVIPEKKDTVKKL HHCCCCCCHHHHHHH	51.07	23749302
88	Ubiquitination	KSAVIPEKKDTVKKL HHCCCCCCHHHHHHH	51.07	-
96	Ubiquitination	KDTVKKLKEIAFPKA HHHHHHHHHHCCCCH	56.82	-
102	Sumoylation	LKEIAFPKAEELKAE HHHHCCCCHHHHHHH	63.07	-
102	Sumoylation	LKEIAFPKAEELKAE HHHHCCCCHHHHHHH	63.07	-
102	Ubiquitination	LKEIAFPKAEELKAE HHHHCCCCHHHHHHH	63.07	-
107	Ubiquitination	FPKAEELKAELLKRY CCCHHHHHHHHHHHH	42.99	21890473
107	Ubiquitination	FPKAEELKAELLKRY CCCHHHHHHHHHHHH	42.99	21890473
112	Ubiquitination	ELKAELLKRYTKEYT HHHHHHHHHHHHHHH	56.85	-
114	Phosphorylation	KAELLKRYTKEYTEY HHHHHHHHHHHHHHH	22.15	23403867
116	Ubiquitination	ELLKRYTKEYTEYNE HHHHHHHHHHHHHHH	39.53	-
118	Phosphorylation	LKRYTKEYTEYNEEK HHHHHHHHHHHHHHH	13.36	27642862
121	Phosphorylation	YTKEYTEYNEEKKKE HHHHHHHHHHHHHHH	21.77	27642862
136	Sulfoxidation	AEELARNMAIQQELE HHHHHHHHHHHHHHH	2.64	21406390
144	Ubiquitination	AIQQELEKEKQRVAQ HHHHHHHHHHHHHHH	80.82	-
153	Ubiquitination	KQRVAQQKQQQLEQE HHHHHHHHHHHHHHH	37.68	21890473
153	Ubiquitination	KQRVAQQKQQQLEQE HHHHHHHHHHHHHHH	37.68	21890473
153	Acetylation	KQRVAQQKQQQLEQE HHHHHHHHHHHHHHH	37.68	12650301
168	Sulfoxidation	QFHAFEEMIRNQELE HHHHHHHHHHCHHHH	2.48	30846556
176	Ubiquitination	IRNQELEKERLKIVQ HHCHHHHHHHHHHHH	61.84	-
180	Ubiquitination	ELEKERLKIVQEFGK HHHHHHHHHHHHHCC	47.23	-
187	Ubiquitination	KIVQEFGKVDPGLGG HHHHHHCCCCCCCCC	49.11	-
214	Phosphorylation	VFPTLTVSSIQPSDC CCCEEEECCCCHHHC	19.25	30631047
236	Phosphorylation	KPPVVDRSLKPGALS CCCCCCCCCCCCCCC	35.96	29978859
238	Ubiquitination	PVVDRSLKPGALSNS CCCCCCCCCCCCCCC	42.52	-
243	Phosphorylation	SLKPGALSNSESIPT CCCCCCCCCCCCCCC	37.46	21082442
245	Phosphorylation	KPGALSNSESIPTID CCCCCCCCCCCCCCC	29.37	21082442
247	Phosphorylation	GALSNSESIPTIDGL CCCCCCCCCCCCCCC	33.42	15314065
250	Phosphorylation	SNSESIPTIDGLRHV CCCCCCCCCCCCCEE	29.99	28450419
255	Methylation	IPTIDGLRHVVVPGR CCCCCCCCEEEECCC	26.53	-
295	Phosphorylation	KLMRNEFTITHVLIP HHHCCCCEEEEEEEC	20.84	24114839
297	Phosphorylation	MRNEFTITHVLIPKQ HCCCCEEEEEEECCC	11.68	24114839
378	Ubiquitination	FQETGFFKLTDHGLE CCCCCCEEECCCCHH	48.49	-
393	Ubiquitination	EISSCRQKGFHPHSK HHHHHHHCCCCCCCC	44.16	-
399	Phosphorylation	QKGFHPHSKDPPLFC HCCCCCCCCCCCCEE	43.11	46163141
400	Ubiquitination	KGFHPHSKDPPLFCS CCCCCCCCCCCCEEC	71.82	-
419	Phosphorylation	TVVDRAVTITDLR-- EEEECEEEEECCC--	19.71	26437602
424	Methylation	AVTITDLR------- EEEEECCC-------	47.51	-

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:14755250

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD6_HUMAN	SMAD6	physical	11483516
SMAD7_HUMAN	SMAD7	physical	11483516
GRAP2_HUMAN	GRAP2	physical	10224278
STAM1_HUMAN	STAM	physical	10383417
FETA_HUMAN	AFP	physical	19615732
CLCA_HUMAN	CLTA	physical	19615732
GRB2_HUMAN	GRB2	physical	19615732
P3C2A_HUMAN	PIK3C2A	physical	19615732
EPN4_HUMAN	CLINT1	physical	19615732
CHMP3_HUMAN	CHMP3	physical	19615732
OTUB1_HUMAN	OTUB1	physical	19615732
CHMP3_HUMAN	CHMP3	physical	17159328
CHM1A_HUMAN	CHMP1A	physical	16760479
CHM1B_HUMAN	CHMP1B	physical	16760479
CHM2A_HUMAN	CHMP2A	physical	16760479
CHMP3_HUMAN	CHMP3	physical	16760479
STAM1_HUMAN	STAM	physical	16760479
CLH1_HUMAN	CLTC	physical	16716190
STAM1_HUMAN	STAM	physical	15314065
CHM1A_HUMAN	CHMP1A	physical	17711858
CHM1B_HUMAN	CHMP1B	physical	17711858
CHMP3_HUMAN	CHMP3	physical	17711858
CHM4A_HUMAN	CHMP4A	physical	17711858
CHM4B_HUMAN	CHMP4B	physical	17711858
CHM4C_HUMAN	CHMP4C	physical	17711858
STAM1_HUMAN	STAM	physical	20159979
STAM2_HUMAN	STAM2	physical	20159979
GRB2_HUMAN	GRB2	physical	20159979
GRAP2_HUMAN	GRAP2	physical	20159979
STAM1_HUMAN	STAM	physical	16520378
UBC_HUMAN	UBC	physical	20622874
UBE2S_HUMAN	UBE2S	physical	20622874
TRAF6_HUMAN	TRAF6	physical	20622874
UBC_HUMAN	UBC	physical	19373254
STAM1_HUMAN	STAM	physical	12810066
GRB2_HUMAN	GRB2	physical	12810066
STAM1_HUMAN	STAM	physical	16431367
CLH1_HUMAN	CLTC	physical	16431367
CHMP3_HUMAN	CHMP3	physical	16431367
UBC_HUMAN	UBC	physical	16431367
GRAP2_HUMAN	GRAP2	physical	12176364
GRB2_HUMAN	GRB2	physical	16730941
GRAP2_HUMAN	GRAP2	physical	16730941
STAM1_HUMAN	STAM	physical	16730941
STAM2_HUMAN	STAM2	physical	16730941
CHMP3_HUMAN	CHMP3	physical	16730941
CHM1A_HUMAN	CHMP1A	physical	16730941
HEM1_HUMAN	ALAS1	physical	16730941
AMNLS_HUMAN	AMN	physical	16730941
UACA_HUMAN	UACA	physical	16730941
CTBL1_HUMAN	CTNNBL1	physical	16730941
MP2K5_HUMAN	MAP2K5	physical	16730941
CHM1B_HUMAN	CHMP1B	physical	16730941
CHM4B_HUMAN	CHMP4B	physical	16730941
STAM2_HUMAN	STAM2	physical	19060904
PCH2_HUMAN	TRIP13	physical	19060904
UBC_HUMAN	UBC	physical	23562397
UBC_HUMAN	UBC	physical	24151880
STAM1_HUMAN	STAM	physical	24151880
FPPS_HUMAN	FDPS	physical	22863883
SMUF2_HUMAN	SMURF2	physical	14755250
CHMP3_MOUSE	Chmp3	physical	16431367
M3K2_HUMAN	MAP3K2	physical	24975362
UBC_HUMAN	UBC	physical	24961813
TNR1A_HUMAN	TNFRSF1A	physical	24980434
CXA1_HUMAN	GJA1	physical	25070368
CHMP3_HUMAN	CHMP3	physical	25416956
CHM1B_HUMAN	CHMP1B	physical	25416956
CLH2_HUMAN	CLTCL1	physical	26186194
GRB2_HUMAN	GRB2	physical	26186194
CHMP3_HUMAN	CHMP3	physical	26186194
CHM1A_HUMAN	CHMP1A	physical	26186194
P3C2A_HUMAN	PIK3C2A	physical	26186194
GAK_HUMAN	GAK	physical	26186194
UBC_HUMAN	UBC	physical	25527291
PTN11_HUMAN	PTPN11	physical	26344197
UBC_HUMAN	UBC	physical	25752577
UBC_HUMAN	UBC	physical	26368668
UBC_HUMAN	UBC	physical	26601948
UBC_HUMAN	UBC	physical	26876099
P53_HUMAN	TP53	physical	27561390
CHMP3_HUMAN	CHMP3	physical	28514442
CLH2_HUMAN	CLTCL1	physical	28514442
P3C2A_HUMAN	PIK3C2A	physical	28514442
BMP2K_HUMAN	BMP2K	physical	28514442
GAK_HUMAN	GAK	physical	28514442
CHM1A_HUMAN	CHMP1A	physical	28514442
GTSE1_HUMAN	GTSE1	physical	28514442
RBP1_HUMAN	RALBP1	physical	28514442
AP2A1_HUMAN	AP2A1	physical	28514442
EPN4_HUMAN	CLINT1	physical	28514442
CHM2A_HUMAN	CHMP2A	physical	28514442
VTI1B_HUMAN	VTI1B	physical	28514442
UBC_HUMAN	UBC	physical	28319114
ILRL2_HUMAN	IL1RL2	physical	29176319

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614261	Microcephaly-capillary malformation syndrome (MICCAP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of STABP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Promoting bone morphogenetic protein signaling through negativeregulation of inhibitory Smads."; Itoh F., Asao H., Sugamura K., Heldin C.-H., ten Dijke P., Itoh S.; EMBO J. 20:4132-4142(2001). Cited for: FUNCTION, INTERACTION WITH SMAD6 AND SMAD7, SUBCELLULAR LOCATION, ANDPHOSPHORYLATION AT SER-2; SER-48; SER-243; SER-245 AND SER-247.	11483516 [Abstract]