F10A1_HUMAN - dbPTM
F10A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F10A1_HUMAN
UniProt AC P50502
Protein Name Hsc70-interacting protein
Gene Name ST13
Organism Homo sapiens (Human).
Sequence Length 369
Subcellular Localization Cytoplasm.
Protein Description One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins (By similarity)..
Protein Sequence MDPRKVNELRAFVKMCKQDPSVLHTEEMRFLREWVESMGGKVPPATQKAKSEENTKEEKPDSKKVEEDLKADEPSSEESDLEIDKEGVIEPDTDAPQEMGDENAEITEEMMDQANDKKVAAIEALNDGELQKAIDLFTDAIKLNPRLAILYAKRASVFVKLQKPNAAIRDCDRAIEINPDSAQPYKWRGKAHRLLGHWEEAAHDLALACKLDYDEDASAMLKEVQPRAQKIAEHRRKYERKREEREIKERIERVKKAREEHERAQREEEARRQSGAQYGSFPGGFPGGMPGNFPGGMPGMGGGMPGMAGMPGLNEILSDPEVLAAMQDPEVMVAFQDVAQNPANMSKYQSNPKVMNLISKLSAKFGGQA
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
4Methylation----MDPRKVNELRA
----CCHHHHHHHHH		51.82115385797
10MethylationPRKVNELRAFVKMCK
HHHHHHHHHHHHHHH		21.57115390419
10DimethylationPRKVNELRAFVKMCK
HHHHHHHHHHHHHHH		21.57-
14AcetylationNELRAFVKMCKQDPS
HHHHHHHHHHHCCCC		31.9325953088
14UbiquitinationNELRAFVKMCKQDPS
HHHHHHHHHHHCCCC		31.9321890473
14MalonylationNELRAFVKMCKQDPS
HHHHHHHHHHHCCCC		31.9326320211
14UbiquitinationNELRAFVKMCKQDPS
HHHHHHHHHHHCCCC		31.9321890473
17UbiquitinationRAFVKMCKQDPSVLH
HHHHHHHHCCCCCCC		54.99-
17AcetylationRAFVKMCKQDPSVLH
HHHHHHHHCCCCCCC		54.9923236377
21PhosphorylationKMCKQDPSVLHTEEM
HHHHCCCCCCCHHHH		45.6724300666
25PhosphorylationQDPSVLHTEEMRFLR
CCCCCCCHHHHHHHH		29.4924300666
28SulfoxidationSVLHTEEMRFLREWV
CCCCHHHHHHHHHHH		2.7521406390
32MethylationTEEMRFLREWVESMG
HHHHHHHHHHHHHCC		32.78115478511
38SulfoxidationLREWVESMGGKVPPA
HHHHHHHCCCCCCHH		5.3330846556
41UbiquitinationWVESMGGKVPPATQK
HHHHCCCCCCHHHHH		45.9321890473
41UbiquitinationWVESMGGKVPPATQK
HHHHCCCCCCHHHHH		45.9321890473
48UbiquitinationKVPPATQKAKSEENT
CCCHHHHHHHCCCCC		54.12-
50UbiquitinationPPATQKAKSEENTKE
CHHHHHHHCCCCCCC		66.4921890473
51PhosphorylationPATQKAKSEENTKEE
HHHHHHHCCCCCCCC		55.8126091039
56UbiquitinationAKSEENTKEEKPDSK
HHCCCCCCCCCCCHH		75.3821890473
59UbiquitinationEENTKEEKPDSKKVE
CCCCCCCCCCHHHHH		56.0421890473
63UbiquitinationKEEKPDSKKVEEDLK
CCCCCCHHHHHHHHH		69.12-
64UbiquitinationEEKPDSKKVEEDLKA
CCCCCHHHHHHHHHC		59.85-
75PhosphorylationDLKADEPSSEESDLE
HHHCCCCCCCCCCCC		48.6229255136
76PhosphorylationLKADEPSSEESDLEI
HHCCCCCCCCCCCCC		56.9829255136
79PhosphorylationDEPSSEESDLEIDKE
CCCCCCCCCCCCCCC		43.3619664994
93PhosphorylationEGVIEPDTDAPQEMG
CCCCCCCCCCCHHHC		44.7930140170
107PhosphorylationGDENAEITEEMMDQA
CCCCHHHHHHHHHHH		19.8720363803
118UbiquitinationMDQANDKKVAAIEAL
HHHHCHHHHHHHHHC		39.71-
118MalonylationMDQANDKKVAAIEAL
HHHHCHHHHHHHHHC		39.7126320211
132UbiquitinationLNDGELQKAIDLFTD
CCCHHHHHHHHHHHH		60.99-
138PhosphorylationQKAIDLFTDAIKLNP
HHHHHHHHHHHHHCH		31.6421712546
142UbiquitinationDLFTDAIKLNPRLAI
HHHHHHHHHCHHHHH		43.8821890473
142UbiquitinationDLFTDAIKLNPRLAI
HHHHHHHHHCHHHHH		43.8821890473
151PhosphorylationNPRLAILYAKRASVF
CHHHHHHHHHHCCEE		12.1728152594
153MalonylationRLAILYAKRASVFVK
HHHHHHHHHCCEEEE		34.6326320211
153UbiquitinationRLAILYAKRASVFVK
HHHHHHHHHCCEEEE		34.6321890473
153UbiquitinationRLAILYAKRASVFVK
HHHHHHHHHCCEEEE		34.6321890473
153AcetylationRLAILYAKRASVFVK
HHHHHHHHHCCEEEE		34.6323236377
156PhosphorylationILYAKRASVFVKLQK
HHHHHHCCEEEECCC		21.8130266825
160UbiquitinationKRASVFVKLQKPNAA
HHCCEEEECCCCCHH		33.4621890473
160MalonylationKRASVFVKLQKPNAA
HHCCEEEECCCCCHH		33.4626320211
160UbiquitinationKRASVFVKLQKPNAA
HHCCEEEECCCCCHH		33.4621890473
160AcetylationKRASVFVKLQKPNAA
HHCCEEEECCCCCHH		33.4625953088
163UbiquitinationSVFVKLQKPNAAIRD
CEEEECCCCCHHHCC		51.1521890473
163UbiquitinationSVFVKLQKPNAAIRD
CEEEECCCCCHHHCC		51.1521890473
181PhosphorylationAIEINPDSAQPYKWR
CEECCCCCCCCCCCC		30.0225159151
185NitrationNPDSAQPYKWRGKAH
CCCCCCCCCCCCHHH		15.88-
186UbiquitinationPDSAQPYKWRGKAHR
CCCCCCCCCCCHHHH		36.7821890473
186UbiquitinationPDSAQPYKWRGKAHR
CCCCCCCCCCCHHHH		36.7821890473
186AcetylationPDSAQPYKWRGKAHR
CCCCCCCCCCCHHHH		36.7823236377
210AcetylationHDLALACKLDYDEDA
HHHHHHHCCCCCHHH		38.4925038526
210UbiquitinationHDLALACKLDYDEDA
HHHHHHHCCCCCHHH		38.49-
213PhosphorylationALACKLDYDEDASAM
HHHHCCCCCHHHHHH		31.50-
213NitrationALACKLDYDEDASAM
HHHHCCCCCHHHHHH		31.50-
218PhosphorylationLDYDEDASAMLKEVQ
CCCCHHHHHHHHHHH		26.9121712546
220SulfoxidationYDEDASAMLKEVQPR
CCHHHHHHHHHHHHH		5.2121406390
222UbiquitinationEDASAMLKEVQPRAQ
HHHHHHHHHHHHHHH		42.6321890473
230UbiquitinationEVQPRAQKIAEHRRK
HHHHHHHHHHHHHHH		42.79-
346PhosphorylationAQNPANMSKYQSNPK
HHCCCCHHHHHCCHH		28.1921728385
347UbiquitinationQNPANMSKYQSNPKV
HCCCCHHHHHCCHHH		36.22-
350PhosphorylationANMSKYQSNPKVMNL
CCHHHHHCCHHHHHH		52.5924719451
353AcetylationSKYQSNPKVMNLISK
HHHHCCHHHHHHHHH		59.3725953088
353UbiquitinationSKYQSNPKVMNLISK
HHHHCCHHHHHHHHH		59.3721890473
355SulfoxidationYQSNPKVMNLISKLS
HHCCHHHHHHHHHHH		4.1621406390
359PhosphorylationPKVMNLISKLSAKFG
HHHHHHHHHHHHHHC		30.6129514088
360MalonylationKVMNLISKLSAKFGG
HHHHHHHHHHHHHCC		39.1926320211
360UbiquitinationKVMNLISKLSAKFGG
HHHHHHHHHHHHHCC		39.19-
360AcetylationKVMNLISKLSAKFGG
HHHHHHHHHHHHHCC		39.1925953088
362PhosphorylationMNLISKLSAKFGGQA
HHHHHHHHHHHCCCC		32.9028450419
364UbiquitinationLISKLSAKFGGQA--
HHHHHHHHHCCCC--		40.9621890473
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
346SPhosphorylationKinaseGRK5P34947
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F10A1_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 F10A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAPK1_HUMANDAPK1physical
17324930
HSP7C_HUMANHSPA8physical
11687574
CUL2_HUMANCUL2physical
22863883
PLAK_HUMANJUPphysical
22863883
HS90A_HUMANHSP90AA1physical
10642522
HSP74_HUMANHSPA4physical
10642522
COF2_HUMANCFL2physical
26344197
CLIC1_HUMANCLIC1physical
26344197
DEST_HUMANDSTNphysical
26344197
HEAT3_HUMANHEATR3physical
26344197
PACN2_HUMANPACSIN2physical
26344197
PACN3_HUMANPACSIN3physical
26344197
TCP4_HUMANSUB1physical
26344197
HS90A_HUMANHSP90AA1physical
22504172
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of F10A1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-76 AND SER-79, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-76 AND SER-79,AND MASS SPECTROMETRY.
"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-75; SER-76; SER-79 ANDSER-181, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-76 AND SER-79,AND MASS SPECTROMETRY.
"G protein-coupled receptor kinase 5 phosphorylation of Hip regulatesinternalization of the chemokine receptor CXCR4.";
Barker B.L., Benovic J.L.;
Biochemistry 50:6933-6941(2011).
Cited for: PHOSPHORYLATION AT SER-346, AND INTERACTION WITH GRK5.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-76 AND SER-79,AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-79, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-76 AND SER-79,AND MASS SPECTROMETRY.

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