Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Heat shock 70 kDa protein 1A/1B  

UniProtKB / Swiss-Prot ID :  HSP71_HUMAN

Gene Name (Synonyms) : 
HSPA1A, HSPA1
HSPA1B  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. 

Protein Function :  In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. 

Protein Sequence MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDA...
Predicted Secondary Structure CCCCCEEEEEECCCCEEEEEEECCEEEEEECCCCCEECCEEEEECCCCEEECCHHHHHHHCCCCHHHHHH...
Protein Variant
LocationDescription
95I -> V. VAR_032152
110E -> D (in dbSNP:rs17856061 anddbSNP:rs562047).
467A -> V. VAR_032153
499N -> S (in dbSNP:rs17855850 anddbSNP:rs483638).
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAKAAA
---CCCCCE
15.36UniProtKB
Link
41PhosphotyrosineTTPSYVAFT
ECCEEEEEC
9.30PhosphoELM
Link
41Phosphotyrosine.TTPSYVAFT
ECCEEEEEC
9.30UniProtKB
Link
106PhosphoserineKVQVSYKGE
EEEEEEECC
12.20HPRD
Link
106Phosphoserine.KVQVSYKGE
EEEEEEECC
12.20UniProtKB
Link
107PhosphotyrosineVQVSYKGET
EEEEEECCC
24.93HPRD
Link
107Phosphotyrosine.VQVSYKGET
EEEEEECCC
24.93UniProtKB
Link
108N6-acetyllysineQVSYKGETK
EEEEECCCC
42.64HPRD
Link
108N6-acetyllysine.QVSYKGETK
EEEEECCCC
42.64UniProtKB
Link
222PhosphothreonineEVKATAGDT
EEEEECCCC
26.00HPRD
Link
246N6-acetyllysineVEEFKRKHK
HHHHHHHHC
64.91HPRD
Link
246N6-acetyllysine.VEEFKRKHK
HHHHHHHHC
64.91UniProtKB
Link
319N6-acetyllysineEPVEKALRD
HHHHHHHHH
53.61HPRD
Link
348N6-acetyllysinePKVQKLLQD
HHHHHHHHH
54.90HPRD
Link
348N6-acetyllysine.PKVQKLLQD
HHHHHHHHH
54.90UniProtKB
Link
362PhosphoserineDLNKSINPD
CCCCCCCHH
26.90PhosphoELM
Link
371PhosphotyrosineEAVAYGAAV
HHHHHHHHH
10.74PhosphoELM
Link
500N6-acetyllysineGKANKITIT
CCEEEEEEE
46.19HPRD
Link-
507Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ITNDKGRLS
EECCCCCCC
48.26UbiProtDB
Link-
524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QEAEKYKAE
HHHHHHHHH
60.13UbiProtDB
Link-
525PhosphotyrosineEAEKYKAED
HHHHHHHHH
13.61PhosphoELM
Link-
608PhosphoserineNPIISGLYQ
HHHHHHHHH
24.38HPRD
Link-
611PhosphotyrosineISGLYQGAG
HHHHHHHCC
14.39HPRD
Link-
611PhosphotyrosineISGLYQGAG
HHHHHHHCC
14.39PhosphoELM
Link-
611Phosphotyrosine.ISGLYQGAG
HHHHHHHCC
14.39UniProtKB
Link-
631PhosphoserinePKGGSGSGP
CCCCCCCCC
38.15HPRD
Link-
631PhosphoserinePKGGSGSGP
CCCCCCCCC
38.15PhosphoELM
Link-
631PhosphoserinePKGGSGSGP
CCCCCCCCC
38.15SysPTM
Link-
631Phosphoserine.PKGGSGSGP
CCCCCCCCC
38.15UniProtKB
Link-
633PhosphoserineGGSGSGPTI
CCCCCCCCC
43.21HPRD
Link-
636PhosphothreonineGSGPTIEEV
CCCCCCCCC
44.54HPRD
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NQO1_HUMANphysical interactionMINT-18206MINT11821413
1433B_HUMANphysical interactionMINT-50346MINT15324660
STIP1_HUMANphysical interactionMINT-17766MINT10786835
ATX1_HUMANphysical interactionMINT-2859843MINT16713569
RD23A_HUMANphysical interactionMINT-2791462MINT16712842
1433G_HUMANphysical interactionMINT-50819MINT15324660
FANCC_HUMANphysical interactionMINT-16948MINT11500375
FANCC_HUMANphysical interactionMINT-16949MINT11500375
DNJC3_HUMANphysical interactionMINT-15378MINT9920933
BAG1_HUMANphysical interactionMINT-45859MINT11231577
BAG1_HUMANphysical interactionMINT-45860MINT11231577
HPBP1_HUMANphysical interactionMINT-2871494MINT16713569
CH60_HUMANphysical interactionDIP:824EDIP8776728
AIFM1_HUMANin vitro
in vivo
HPRD:06784HPRD11533664
- top -

Disease Reference
Drug Reference
- top -
Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-106 AND TYR-107, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246 AND LYS-348,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-631, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41, AND MASSSPECTROMETRY.
"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 TYR-611, AND MASSSPECTROMETRY.
"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 SER-631, AND MASSSPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-106 AND TYR-107, AND MASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures