HSP7E_HUMAN - dbPTM
HSP7E_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP7E_HUMAN
UniProt AC Q0VDF9
Protein Name Heat shock 70 kDa protein 14
Gene Name HSPA14
Organism Homo sapiens (Human).
Sequence Length 509
Subcellular Localization Cytoplasm, cytosol .
Protein Description Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity..
Protein Sequence MAAIGVHLGCTSACVAVYKDGRAGVVANDAGDRVTPAVVAYSENEEIVGLAAKQSRIRNISNTVMKVKQILGRSSSDPQAQKYIAESKCLVIEKNGKLRYEIDTGEETKFVNPEDVARLIFSKMKETAHSVLGSDANDVVITVPFDFGEKQKNALGEAARAAGFNVLRLIHEPSAALLAYGIGQDSPTGKSNILVFKLGGTSLSLSVMEVNSGIYRVLSTNTDDNIGGAHFTETLAQYLASEFQRSFKHDVRGNARAMMKLTNSAEVAKHSLSTLGSANCFLDSLYEGQDFDCNVSRARFELLCSPLFNKCIEAIRGLLDQNGFTADDINKVVLCGGSSRIPKLQQLIKDLFPAVELLNSIPPDEVIPIGAAIEAGILIGKENLLVEDSLMIECSARDILVKGVDESGASRFTVLFPSGTPLPARRQHTLQAPGSISSVCLELYESDGKNSAKEETKFAQVVLQDLDKKENGLRDILAVLTMKRDGSLHVTCTDQETGKCEAISIEIAS
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
35PhosphorylationNDAGDRVTPAVVAYS
CCCCCCCCCEEEEEE
13.3621406692
41PhosphorylationVTPAVVAYSENEEIV
CCCEEEEEECCCCHH
12.6121406692
42PhosphorylationTPAVVAYSENEEIVG
CCEEEEEECCCCHHH
24.9821406692
53UbiquitinationEIVGLAAKQSRIRNI
CHHHHHHCHHHHHHH
43.10-
66UbiquitinationNISNTVMKVKQILGR
HHHHHHHHHHHHHCC
41.78-
68UbiquitinationSNTVMKVKQILGRSS
HHHHHHHHHHHCCCC
26.55-
74PhosphorylationVKQILGRSSSDPQAQ
HHHHHCCCCCCHHHH
32.1829978859
75PhosphorylationKQILGRSSSDPQAQK
HHHHCCCCCCHHHHH
37.0820068231
76PhosphorylationQILGRSSSDPQAQKY
HHHCCCCCCHHHHHH
55.3320068231
82AcetylationSSDPQAQKYIAESKC
CCCHHHHHHHHCCCE
41.4626051181
82UbiquitinationSSDPQAQKYIAESKC
CCCHHHHHHHHCCCE
41.46-
83PhosphorylationSDPQAQKYIAESKCL
CCHHHHHHHHCCCEE
8.0320068231
87PhosphorylationAQKYIAESKCLVIEK
HHHHHHCCCEEEEEE
21.4630576142
88UbiquitinationQKYIAESKCLVIEKN
HHHHHCCCEEEEEEC
24.08-
94UbiquitinationSKCLVIEKNGKLRYE
CCEEEEEECCEEEEE
60.93-
94AcetylationSKCLVIEKNGKLRYE
CCEEEEEECCEEEEE
60.9325953088
100PhosphorylationEKNGKLRYEIDTGEE
EECCEEEEEEECCCC
27.89-
109UbiquitinationIDTGEETKFVNPEDV
EECCCCCCCCCHHHH
51.07-
122PhosphorylationDVARLIFSKMKETAH
HHHHHHHHHHHHHHH
25.5024719451
123UbiquitinationVARLIFSKMKETAHS
HHHHHHHHHHHHHHH
43.15-
125UbiquitinationRLIFSKMKETAHSVL
HHHHHHHHHHHHHHH
56.50-
127PhosphorylationIFSKMKETAHSVLGS
HHHHHHHHHHHHHCC
24.9323917254
150UbiquitinationVPFDFGEKQKNALGE
EECCCCHHHHHHHHH
67.94-
152UbiquitinationFDFGEKQKNALGEAA
CCCCHHHHHHHHHHH
56.08-
180PhosphorylationPSAALLAYGIGQDSP
HHHHHHHHCCCCCCC
14.8326074081
186PhosphorylationAYGIGQDSPTGKSNI
HHCCCCCCCCCCCCE
19.2422617229
188PhosphorylationGIGQDSPTGKSNILV
CCCCCCCCCCCCEEE
62.2830108239
191PhosphorylationQDSPTGKSNILVFKL
CCCCCCCCCEEEEEE
30.3726074081
219PhosphorylationSGIYRVLSTNTDDNI
CCCEEECCCCCCCCC
19.43-
260AcetylationGNARAMMKLTNSAEV
HCHHHHHHHCCHHHH
38.7925953088
273PhosphorylationEVAKHSLSTLGSANC
HHHHHHHHHHHHCCC
25.3030576142
286PhosphorylationNCFLDSLYEGQDFDC
CCHHHHHHCCCCCCC
23.2030576142
296PhosphorylationQDFDCNVSRARFELL
CCCCCCCCHHHHHHH
13.2630576142
305PhosphorylationARFELLCSPLFNKCI
HHHHHHHHHHHHHHH
25.3021406692
310UbiquitinationLCSPLFNKCIEAIRG
HHHHHHHHHHHHHHH
29.29-
310AcetylationLCSPLFNKCIEAIRG
HHHHHHHHHHHHHHH
29.2926051181
331UbiquitinationFTADDINKVVLCGGS
CCHHHCCEEEECCCC
33.77-
331AcetylationFTADDINKVVLCGGS
CCHHHCCEEEECCCC
33.7726051181
343AcetylationGGSSRIPKLQQLIKD
CCCCHHHHHHHHHHH
57.4625953088
343UbiquitinationGGSSRIPKLQQLIKD
CCCCHHHHHHHHHHH
57.46-
402UbiquitinationSARDILVKGVDESGA
CHHHEEEEECCCCCC
50.17-
402AcetylationSARDILVKGVDESGA
CHHHEEEEECCCCCC
50.1726051181
413PhosphorylationESGASRFTVLFPSGT
CCCCCCEEEECCCCC
18.3923312004
418PhosphorylationRFTVLFPSGTPLPAR
CEEEECCCCCCCCCC
48.2228450419
420PhosphorylationTVLFPSGTPLPARRQ
EEECCCCCCCCCCCH
26.4521815630
456PhosphorylationKNSAKEETKFAQVVL
CCCHHHHHHHHHHHH
32.33-
457UbiquitinationNSAKEETKFAQVVLQ
CCHHHHHHHHHHHHH
41.82-
468UbiquitinationVVLQDLDKKENGLRD
HHHHHHHHCCCCHHH
70.09-
469AcetylationVLQDLDKKENGLRDI
HHHHHHHCCCCHHHH
56.9619814893
481PhosphorylationRDILAVLTMKRDGSL
HHHHHHEEECCCCCE
17.6620068231
487PhosphorylationLTMKRDGSLHVTCTD
EEECCCCCEEEEEEC
21.4223312004

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

Oops, there are no upstream regulatory protein records of HSP7E_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP7E_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 HSP7E_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAF1_HUMANPAF1physical
22939629

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 HSP7E_HUMAN

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Related Literatures of Post-Translational Modification

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