HS12B_HUMAN - dbPTM
HS12B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HS12B_HUMAN
UniProt AC Q96MM6
Protein Name Heat shock 70 kDa protein 12B
Gene Name HSPA12B
Organism Homo sapiens (Human).
Sequence Length 686
Subcellular Localization
Protein Description
Protein Sequence MLAVPEMGLQGLYIGSSPERSPVPSPPGSPRTQESCGIAPLTPSQSPKPEVRAPQQASFSVVVAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGAFHSFGYTARDYYHDLDPEEARDWLYFEKFKMKIHSATDLTLKTQLEAVNGKTMPALEVFAHALRFFREHALQELREQSPSLPEKDTVRWVLTVPAIWKQPAKQFMREAAYLAGLVSRENAEQLLIALEPEAASVYCRKLRLHQLLDLSGRAPGGGRLGERRSIDSSFRQAREQLRRSRHSRTFLVESGVGELWAEMQAGDRYVVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIATFKRQRPAAWVDLTIAFEARKRTAGPHRAGALNISLPFSFIDFYRKQRGHNVETALRRSSVNFVKWSSQGMLRMSCEAMNELFQPTVSGIIQHIEALLARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARGLRVVVPHDVGLTILKGAVLFGQAPGVVRVRRSPLTYGVGVLNRFVPGRHPPEKLLVRDGRRWCTDVFERFVAAEQSVALGEEVRRSYCPARPGQRRVLINLYCCAAEDARFITDPGVRKCGALSLELEPADCGQDTAGAPPGRREIRAAMQFGDTEIKVTAVDVSTNRSVRASIDFLSN
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
13PhosphorylationEMGLQGLYIGSSPER
CCCCCEEECCCCCCC
15.2924043423
16PhosphorylationLQGLYIGSSPERSPV
CCEEECCCCCCCCCC
32.9128857561
17PhosphorylationQGLYIGSSPERSPVP
CEEECCCCCCCCCCC
26.1028857561
21PhosphorylationIGSSPERSPVPSPPG
CCCCCCCCCCCCCCC
28.7026657352
25PhosphorylationPERSPVPSPPGSPRT
CCCCCCCCCCCCCCC
43.9224670416
29PhosphorylationPVPSPPGSPRTQESC
CCCCCCCCCCCCCCC
19.5823911959
32PhosphorylationSPPGSPRTQESCGIA
CCCCCCCCCCCCCCC
39.8223403867
35PhosphorylationGSPRTQESCGIAPLT
CCCCCCCCCCCCCCC
14.0723403867
42PhosphorylationSCGIAPLTPSQSPKP
CCCCCCCCCCCCCCC
21.6026657352
44PhosphorylationGIAPLTPSQSPKPEV
CCCCCCCCCCCCCCC
37.7526657352
46PhosphorylationAPLTPSQSPKPEVRA
CCCCCCCCCCCCCCC
38.9523911959
200PhosphorylationPSLPEKDTVRWVLTV
CCCCCCCCEEEEEEH
24.04-
206PhosphorylationDTVRWVLTVPAIWKQ
CCEEEEEEHHHHHCC
18.15-
262PhosphorylationLHQLLDLSGRAPGGG
HHHHHHHCCCCCCCC
26.37-
276PhosphorylationGRLGERRSIDSSFRQ
CCCCCCCCCCHHHHH
36.6523911959
279PhosphorylationGERRSIDSSFRQARE
CCCCCCCHHHHHHHH
29.7023403867
280PhosphorylationERRSIDSSFRQAREQ
CCCCCCHHHHHHHHH
22.2424702127
397PhosphorylationAFEARKRTAGPHRAG
EHHHHHCCCCCCCCC
38.71-
433PhosphorylationVETALRRSSVNFVKW
HHHHHHHHCCCEEEE
32.0023663014
434PhosphorylationETALRRSSVNFVKWS
HHHHHHHCCCEEEEC
21.1923663014
442PhosphorylationVNFVKWSSQGMLRMS
CCEEEECCHHHHHHH
29.6428857561
662PhosphorylationAAMQFGDTEIKVTAV
HHHHHCCCEEEEEEE
39.7323403867
667PhosphorylationGDTEIKVTAVDVSTN
CCCEEEEEEEECCCC
18.8918187866

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 HS12B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HS12B_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 HS12B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1C40_HUMANKRT40physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956

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 HS12B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, AND MASSSPECTROMETRY.

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