HS74L_MOUSE - dbPTM
HS74L_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HS74L_MOUSE
UniProt AC P48722
Protein Name Heat shock 70 kDa protein 4L
Gene Name Hspa4l
Organism Mus musculus (Mouse).
Sequence Length 838
Subcellular Localization Cytoplasm. Nucleus. May translocate to the nucleus after heat shock..
Protein Description Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase..
Protein Sequence MSVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTPACISLGSRTRAIGNAAKSQIVTNVRNTIHGFKKLHGRSFDDPIVQTERIRLPYELQKMPNGSTGVKVRYLEEERPFAIEQVTGMLLAKLKETSENALKKPVADCVISIPSFFTDAERRSVMAAAQVAGLNCLRLMNETTAVALAYGIYKQDLPSLDEKPRNVVFIDMGHSAYQVSVCAFNKGKLKVLATTFDPYLGGRNFDEALVDYFCDEFKTKYKINVKENSRALLRLYQECEKLKKLMSANASDLPLNIECFMNDLDVSSKMNRAQFEQLCASLLARVEPPLKSVMDQANLQREDINSIEIVGGATRIPAVKEQVTRFFLKDISTTLNADEAVARGCALQCAILSPAFKVREFSITDLVPYSVTLRWKTSFEEGTGECEVFSKNHPAPFSKVITFHKKEPFELEAFYTNLHEVPYPDPRIGNFTIQNVFPQSDGDSSKVKVKVRINIHGIFSVASASVIEKQNLEGDHNDAAMETEAPKSEGKEDVDKMQVDQEEGGHQKCHAEHTPEEEIDHTGAKAKAPPSDKQDRINQTIKKGKIKSIDLPIQSSLYRQLTQDLLNSYIENEGKMIMQDKLEKERNDAKNAVEEYVYDFRDKLGTVYEKFITPEDMNKLSAMLEDTENWLYEEGEDQPKQVYVDRLQELKKYGQPIQMKYVEHEERPKALNDLGKKIQLVLKVIEAHRNKDERYDHLDPAEMERVEKYISDSMNWLNSKMNAQNKLSLTQDPVVKVSEIVTKSKELDNFCNPIVYKPKPKVEAPEDKAKTGSEHNGPMDGQSGSETSPDPPKGSSQHTDSGEMEVD
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
20PhosphorylationCYIAVARSGGIETIA
HHEEHHHCCCHHHHH		31.4728066266
53AcetylationRAIGNAAKSQIVTNV
HHCHHHHHHHHHHHH		40.25-
58PhosphorylationAAKSQIVTNVRNTIH
HHHHHHHHHHHHHHH		29.6221454597
74PhosphorylationFKKLHGRSFDDPIVQ
HHHHHCCCCCCCCCE		37.3025521595
89PhosphorylationTERIRLPYELQKMPN
EEECCCCHHHHCCCC		33.59-
93UbiquitinationRLPYELQKMPNGSTG
CCCHHHHCCCCCCCC		69.7922790023
98PhosphorylationLQKMPNGSTGVKVRY
HHCCCCCCCCCEEEE		28.7329109428
134UbiquitinationETSENALKKPVADCV
HHCHHHHCCCHHHHE		53.2527667366
194UbiquitinationDLPSLDEKPRNVVFI
CCCCCCCCCCCEEEE		49.2822790023
221UbiquitinationAFNKGKLKVLATTFD
EEECCCEEEEEEECC		38.3922790023
272MalonylationRLYQECEKLKKLMSA
HHHHHHHHHHHHHHC		76.8126320211
278PhosphorylationEKLKKLMSANASDLP
HHHHHHHHCCCCCCC		28.8923567750
282PhosphorylationKLMSANASDLPLNIE
HHHHCCCCCCCCEEH		39.2123567750
322UbiquitinationARVEPPLKSVMDQAN
HHCCCCHHHHHHHHC		46.9422790023
351UbiquitinationATRIPAVKEQVTRFF
CCCCHHHHHHHHHHH		44.5322790023
376S-nitrosylationDEAVARGCALQCAIL
HHHHHHHHHHHHHHH		2.5922588120
380S-nitrosylationARGCALQCAILSPAF
HHHHHHHHHHHCCCE		2.3722588120
384PhosphorylationALQCAILSPAFKVRE
HHHHHHHCCCEEEEE		14.2026745281
388UbiquitinationAILSPAFKVREFSIT
HHHCCCEEEEEEECC		42.35-
393PhosphorylationAFKVREFSITDLVPY
CEEEEEEECCCCCCE		21.5929899451
408PhosphorylationSVTLRWKTSFEEGTG
EEEEEEEECCCCCCC		31.5225521595
409PhosphorylationVTLRWKTSFEEGTGE
EEEEEEECCCCCCCE		27.2529899451
414PhosphorylationKTSFEEGTGECEVFS
EECCCCCCCEEEEEE		32.8429899451
430AcetylationNHPAPFSKVITFHKK
CCCCCCEEEEEEECC		37.73-
519PhosphorylationMETEAPKSEGKEDVD
HHCCCCCCCCCCCHH		50.9929899451
545PhosphorylationQKCHAEHTPEEEIDH
CCCCCCCCCHHHCCC		24.7325521595
553PhosphorylationPEEEIDHTGAKAKAP
CHHHCCCCCCCCCCC		34.7825619855
571PhosphorylationKQDRINQTIKKGKIK
HHHHHHHHHHCCCCC		30.2128494245
573AcetylationDRINQTIKKGKIKSI
HHHHHHHHCCCCCCC		59.887616659
578UbiquitinationTIKKGKIKSIDLPIQ
HHHCCCCCCCCCCCC		44.8622790023
579PhosphorylationIKKGKIKSIDLPIQS
HHCCCCCCCCCCCCH		25.4725521595
586PhosphorylationSIDLPIQSSLYRQLT
CCCCCCCHHHHHHHH		24.0326643407
587PhosphorylationIDLPIQSSLYRQLTQ
CCCCCCHHHHHHHHH		17.0326643407
589PhosphorylationLPIQSSLYRQLTQDL
CCCCHHHHHHHHHHH		9.7726643407
593PhosphorylationSSLYRQLTQDLLNSY
HHHHHHHHHHHHHHH		16.2325521595
599PhosphorylationLTQDLLNSYIENEGK
HHHHHHHHHHHHHCC		27.7026643407
600PhosphorylationTQDLLNSYIENEGKM
HHHHHHHHHHHHCCC		15.9228066266
634UbiquitinationYVYDFRDKLGTVYEK
HHHHHHHHHCCHHHH		44.5522790023
641UbiquitinationKLGTVYEKFITPEDM
HHCCHHHHCCCHHHH		25.1222790023
663PhosphorylationEDTENWLYEEGEDQP
HHHCCHHHHCCCCCC		11.98-
682AcetylationVDRLQELKKYGQPIQ
HHHHHHHHHHCCCCC		43.10-
692PhosphorylationGQPIQMKYVEHEERP
CCCCCEEECCHHHCC		13.0126026062
757UbiquitinationSKMNAQNKLSLTQDP
HHHCCCCCCCCCCCC		27.6322790023
759PhosphorylationMNAQNKLSLTQDPVV
HCCCCCCCCCCCCCE		30.86-
761PhosphorylationAQNKLSLTQDPVVKV
CCCCCCCCCCCCEEH		27.7917525332
776MethylationSEIVTKSKELDNFCN
HHHHHCCHHHHCCCC		64.94-
814PhosphorylationNGPMDGQSGSETSPD
CCCCCCCCCCCCCCC		50.2223984901
816PhosphorylationPMDGQSGSETSPDPP
CCCCCCCCCCCCCCC		42.8423984901
818PhosphorylationDGQSGSETSPDPPKG
CCCCCCCCCCCCCCC		47.4525521595
819PhosphorylationGQSGSETSPDPPKGS
CCCCCCCCCCCCCCC		24.2126643407
826PhosphorylationSPDPPKGSSQHTDSG
CCCCCCCCCCCCCCC		32.7121743459
827PhosphorylationPDPPKGSSQHTDSGE
CCCCCCCCCCCCCCC		34.3521743459
830PhosphorylationPKGSSQHTDSGEMEV
CCCCCCCCCCCCCCC		24.9921743459
832PhosphorylationGSSQHTDSGEMEVD-
CCCCCCCCCCCCCC-		37.5022324799
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 HS74L_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HS74L_MOUSE !!
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 HS74L_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HS74L_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HS74L_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-761, AND MASSSPECTROMETRY.

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