SAV1_HUMAN - dbPTM
SAV1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAV1_HUMAN
UniProt AC Q9H4B6
Protein Name Protein salvador homolog 1
Gene Name SAV1
Organism Homo sapiens (Human).
Sequence Length 383
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. SAV1 is required for STK3/MST2 and STK4/MST1 activation and promotes cell-cycle exit and terminal differentiation in developing epithelial tissues. Plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with STK3/MST2, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation..
Protein Sequence MLSRKKTKNEVSKPAEVQGKYVKKETSPLLRNLMPSFIRHGPTIPRRTDICLPDSSPNAFSTSGDVVSRNQSFLRTPIQRTPHEIMRRESNRLSAPSYLARSLADVPREYGSSQSFVTEVSFAVENGDSGSRYYYSDNFFDGQRKRPLGDRAHEDYRYYEYNHDLFQRMPQNQGRHASGIGRVAATSLGNLTNHGSEDLPLPPGWSVDWTMRGRKYYIDHNTNTTHWSHPLEREGLPPGWERVESSEFGTYYVDHTNKKAQYRHPCAPSVPRYDQPPPVTYQPQQTERNQSLLVPANPYHTAEIPDWLQVYARAPVKYDHILKWELFQLADLDTYQGMLKLLFMKELEQIVKMYEAYRQALLTELENRKQRQQWYAQQHGKNF
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 Orthologous
Protein Cluster
26PhosphorylationGKYVKKETSPLLRNL
CCCCCCCCCHHHHHH		44.5230266825
27PhosphorylationKYVKKETSPLLRNLM
CCCCCCCCHHHHHHH		18.0330266825
36PhosphorylationLLRNLMPSFIRHGPT
HHHHHHHHHHHHCCC		21.2421944251
55PhosphorylationTDICLPDSSPNAFST
CCEECCCCCCCCCCC		45.8430576142
56PhosphorylationDICLPDSSPNAFSTS
CEECCCCCCCCCCCC		29.5621815630
61PhosphorylationDSSPNAFSTSGDVVS
CCCCCCCCCCCCHHH		21.1823898821
62PhosphorylationSSPNAFSTSGDVVSR
CCCCCCCCCCCHHHC		30.2130576142
72PhosphorylationDVVSRNQSFLRTPIQ
CHHHCCHHHCCCCCC		29.7821712546
75MethylationSRNQSFLRTPIQRTP
HCCHHHCCCCCCCCH		36.1254559095
76PhosphorylationRNQSFLRTPIQRTPH
CCHHHCCCCCCCCHH		27.2229214152
81PhosphorylationLRTPIQRTPHEIMRR
CCCCCCCCHHHHHHH		16.7828555341
90PhosphorylationHEIMRRESNRLSAPS
HHHHHHHHCCCCHHH		25.9921712546
94PhosphorylationRRESNRLSAPSYLAR
HHHHCCCCHHHHHHH		34.5930266825
97PhosphorylationSNRLSAPSYLARSLA
HCCCCHHHHHHHHHH		32.2830266825
98PhosphorylationNRLSAPSYLARSLAD
CCCCHHHHHHHHHHC		11.8823403867
102PhosphorylationAPSYLARSLADVPRE
HHHHHHHHHHCCCHH		23.4628060719
112PhosphorylationDVPREYGSSQSFVTE
CCCHHHCCCCCEEEE		25.0527251275
113PhosphorylationVPREYGSSQSFVTEV
CCHHHCCCCCEEEEE		26.0227251275
133PhosphorylationNGDSGSRYYYSDNFF
CCCCCCEEEECCCCC		14.4129978859
134PhosphorylationGDSGSRYYYSDNFFD
CCCCCEEEECCCCCC		8.7229978859
135PhosphorylationDSGSRYYYSDNFFDG
CCCCEEEECCCCCCC		10.7029978859
136PhosphorylationSGSRYYYSDNFFDGQ
CCCEEEECCCCCCCC		15.2322617229
156PhosphorylationGDRAHEDYRYYEYNH
CCCCCHHHHHHHCCC		9.4927642862
158PhosphorylationRAHEDYRYYEYNHDL
CCCHHHHHHHCCCCH		8.4029978859
159PhosphorylationAHEDYRYYEYNHDLF
CCHHHHHHHCCCCHH		11.7029978859
161PhosphorylationEDYRYYEYNHDLFQR
HHHHHHHCCCCHHHH		11.1527642862
168MethylationYNHDLFQRMPQNQGR
CCCCHHHHCCCCCCC		31.26115493375
186PhosphorylationGIGRVAATSLGNLTN
CHHHHHHHHHCCCCC		18.1023090842
187PhosphorylationIGRVAATSLGNLTNH
HHHHHHHHHCCCCCC		29.5623090842
192PhosphorylationATSLGNLTNHGSEDL
HHHHCCCCCCCCCCC		29.2123090842
196PhosphorylationGNLTNHGSEDLPLPP
CCCCCCCCCCCCCCC		22.0123090842
206PhosphorylationLPLPPGWSVDWTMRG
CCCCCCCEEEEEECC		19.0028270605
210PhosphorylationPGWSVDWTMRGRKYY
CCCEEEEEECCEEEE		7.7922817900
245PhosphorylationPGWERVESSEFGTYY
CCCEEEHHHCCEEEE		32.1030576142
246PhosphorylationGWERVESSEFGTYYV
CCEEEHHHCCEEEEE		24.3630576142
250PhosphorylationVESSEFGTYYVDHTN
EHHHCCEEEEEECCC		19.5925332170
251PhosphorylationESSEFGTYYVDHTNK
HHHCCEEEEEECCCC		11.2330576142
256PhosphorylationGTYYVDHTNKKAQYR
EEEEEECCCCEEECC		44.2425332170
258UbiquitinationYYVDHTNKKAQYRHP
EEEECCCCEEECCCC		51.12-
262PhosphorylationHTNKKAQYRHPCAPS
CCCCEEECCCCCCCC		18.7525332170
269PhosphorylationYRHPCAPSVPRYDQP
CCCCCCCCCCCCCCC		26.6521944251
281PhosphorylationDQPPPVTYQPQQTER
CCCCCCCCCCCCCCC		20.5927642862
357PhosphorylationIVKMYEAYRQALLTE
HHHHHHHHHHHHHHH		7.42-
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
26TPhosphorylationKinaseSTK3Q13188
GPS
27SPhosphorylationKinaseSTK3Q13188
GPS
36SPhosphorylationKinaseSTK3Q13188
GPS
269SPhosphorylationKinaseSTK3Q13188
GPS
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:25692647
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAV1_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 SAV1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RASF1_HUMANRASSF1physical
17379520
STK3_HUMANSTK3physical
17379520
LATS1_HUMANLATS1physical
17379520
STK3_HUMANSTK3physical
21988832
ALG13_HUMANALG13physical
24255178
AMOT_HUMANAMOTphysical
24255178
ATPG_HUMANATP5C1physical
24255178
CP131_HUMANCEP131physical
24255178
CC138_HUMANCCDC138physical
24255178
CEP72_HUMANCEP72physical
24255178
CEP85_HUMANCEP85physical
24255178
CNTRB_HUMANCNTROBphysical
24255178
CPEB4_HUMANCPEB4physical
24255178
KC1E_HUMANCSNK1Ephysical
24255178
4ET_HUMANEIF4ENIF1physical
24255178
FUBP3_HUMANFUBP3physical
24255178
GLMN_HUMANGLMNphysical
24255178
HDAC6_HUMANHDAC6physical
24255178
IF2B2_HUMANIGF2BP2physical
24255178
INADL_HUMANINADLphysical
24255178
IRS4_HUMANIRS4physical
24255178
MOONR_HUMANKIAA0753physical
24255178
KBP_HUMANKIAA1279physical
24255178
KIF7_HUMANKIF7physical
24255178
KIRR1_HUMANKIRRELphysical
24255178
LATS2_HUMANLATS2physical
24255178
TGO1_HUMANMIA3physical
24255178
MOB1A_HUMANMOB1Aphysical
24255178
NYNRI_HUMANNYNRINphysical
24255178
OFD1_HUMANOFD1physical
24255178
PCM1_HUMANPCM1physical
24255178
PIBF1_HUMANPIBF1physical
24255178
PKP4_HUMANPKP4physical
24255178
PTN14_HUMANPTPN14physical
24255178
PUM1_HUMANPUM1physical
24255178
SYQ_HUMANQARSphysical
24255178
RL36A_HUMANRPL36Aphysical
24255178
SC16A_HUMANSEC16Aphysical
24255178
SNTB1_HUMANSNTB1physical
24255178
SNTB2_HUMANSNTB2physical
24255178
SPTN1_HUMANSPTAN1physical
24255178
STK3_HUMANSTK3physical
24255178
STK4_HUMANSTK4physical
24255178
TNR6A_HUMANTNRC6Aphysical
24255178
TNR6B_HUMANTNRC6Bphysical
24255178
TBB6_HUMANTUBB6physical
24255178
GCP2_HUMANTUBGCP2physical
24255178
UNK_HUMANUNKphysical
24255178
UTRO_HUMANUTRNphysical
24255178
1433E_HUMANYWHAEphysical
24255178
1433F_HUMANYWHAHphysical
24255178
1433Z_HUMANYWHAZphysical
24255178
STK3_HUMANSTK3physical
26186194
STK4_HUMANSTK4physical
26186194
GRN_HUMANGRNphysical
26186194
YTHD1_HUMANYTHDF1physical
26186194
BAG1_HUMANBAG1physical
26186194
SEMG1_HUMANSEMG1physical
26186194
AJUBA_HUMANAJUBAphysical
20303269
WTIP_HUMANWTIPphysical
20303269
STK4_HUMANSTK4physical
24366813
STK3_HUMANSTK3physical
24366813
LATS2_HUMANLATS2physical
25670202
SKI_HUMANSKIphysical
25670202
NEDD4_HUMANNEDD4physical
25692647
STK4_HUMANSTK4physical
25692647
LATS2_HUMANLATS2physical
25692647
STK4_HUMANSTK4physical
28514442
STK3_HUMANSTK3physical
28514442
BAG1_HUMANBAG1physical
28514442
SEMG1_HUMANSEMG1physical
28514442
TIAR_HUMANTIAL1physical
28514442
GRN_HUMANGRNphysical
28514442
KIF3C_HUMANKIF3Cphysical
27173435
KIF3B_HUMANKIF3Bphysical
27173435
USP9X_HUMANUSP9Xphysical
28720576
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 SAV1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26; SER-27; SER-56;SER-90; SER-94; SER-136; THR-186 AND THR-210, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26, AND MASSSPECTROMETRY.

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