HS74L_HUMAN - dbPTM
HS74L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HS74L_HUMAN
UniProt AC O95757
Protein Name Heat shock 70 kDa protein 4L
Gene Name HSPA4L
Organism Homo sapiens (Human).
Sequence Length 839
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 MSVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTPACISLGSRTRAIGNAAKSQIVTNVRNTIHGFKKLHGRSFDDPIVQTERIRLPYELQKMPNGSAGVKVRYLEEERPFAIEQVTGMLLAKLKETSENALKKPVADCVISIPSFFTDAERRSVMAAAQVAGLNCLRLMNETTAVALAYGIYKQDLPPLDEKPRNVVFIDMGHSAYQVLVCAFNKGKLKVLATTFDPYLGGRNFDEALVDYFCDEFKTKYKINVKENSRALLRLYQECEKLKKLMSANASDLPLNIECFMNDLDVSSKMNRAQFEQLCASLLARVEPPLKAVMEQANLQREDISSIEIVGGATRIPAVKEQITKFFLKDISTTLNADEAVARGCALQCAILSPAFKVREFSITDLVPYSITLRWKTSFEDGSGECEVFCKNHPAPFSKVITFHKKEPFELEAFYTNLHEVPYPDARIGSFTIQNVFPQSDGDSSKVKVKVRVNIHGIFSVASASVIEKQNLEGDHSDAPMETETSFKNENKDNMDKMQVDQEEGHQKCHAEHTPEEEIDHTGAKTKSAVSDKQDRLNQTLKKGKVKSIDLPIQSSLCRQLGQDLLNSYIENEGKMIMQDKLEKERNDAKNAVEEYVYDFRDRLGTVYEKFITPEDLSKLSAVLEDTENWLYEDGEDQPKQVYVDKLQELKKYGQPIQMKYMEHEERPKALNDLGKKIQLVMKVIEAYRNKDERYDHLDPTEMEKVEKCISDAMSWLNSKMNAQNKLSLTQDPVVKVSEIVAKSKELDNFCNPIIYKPKPKAEVPEDKPKANSEHNGPMDGQSGTETKSDSTKDSSQHTKSSGEMEVD
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
2Phosphorylation------MSVVGIDLG
------CCEEEEEHH
26.0524043423
14PhosphorylationDLGFLNCYIAVARSG
EHHHHHHHEEHHHCC
7.2824043423
20PhosphorylationCYIAVARSGGIETIA
HHEEHHHCCCHHHHH
31.4722617229
25PhosphorylationARSGGIETIANEYSD
HHCCCHHHHHHHCCC
24.38-
30PhosphorylationIETIANEYSDRCTPA
HHHHHHHCCCCCCHH
18.71-
31PhosphorylationETIANEYSDRCTPAC
HHHHHHCCCCCCHHH
16.64-
33MethylationIANEYSDRCTPACIS
HHHHCCCCCCHHHHC
21.92115479937
43PhosphorylationPACISLGSRTRAIGN
HHHHCCCHHHHHCHH
35.4528857561
51PhosphorylationRTRAIGNAAKSQIVT
HHHHCHHHHHHHHHH
15.85-
53AcetylationRAIGNAAKSQIVTNV
HHCHHHHHHHHHHHH
40.2525953088
53UbiquitinationRAIGNAAKSQIVTNV
HHCHHHHHHHHHHHH
40.2521906983
54PhosphorylationAIGNAAKSQIVTNVR
HCHHHHHHHHHHHHH
22.03-
56PhosphorylationGNAAKSQIVTNVRNT
HHHHHHHHHHHHHHH
5.50-
64MethylationVTNVRNTIHGFKKLH
HHHHHHHHHHHHHHH
3.23-
68UbiquitinationRNTIHGFKKLHGRSF
HHHHHHHHHHHCCCC
60.04-
74PhosphorylationFKKLHGRSFDDPIVQ
HHHHHCCCCCCCCCE
37.3023401153
82PhosphorylationFDDPIVQTERIRLPY
CCCCCCEEEECCCCH
19.1428857561
84UbiquitinationDPIVQTERIRLPYEL
CCCCEEEECCCCHHH
23.79-
86MethylationIVQTERIRLPYELQK
CCEEEECCCCHHHHC
35.5197804701
89PhosphorylationTERIRLPYELQKMPN
EEECCCCHHHHCCCC
33.59-
99UbiquitinationQKMPNGSAGVKVRYL
HCCCCCCCCCEEEEC
28.35-
102UbiquitinationPNGSAGVKVRYLEEE
CCCCCCCEEEECCCC
21.78-
105PhosphorylationSAGVKVRYLEEERPF
CCCCEEEECCCCCCC
22.81-
117MethylationRPFAIEQVTGMLLAK
CCCCHHHHHHHHHHH
3.03-
118PhosphorylationPFAIEQVTGMLLAKL
CCCHHHHHHHHHHHH
19.3020068231
124UbiquitinationVTGMLLAKLKETSEN
HHHHHHHHHHHHCHH
61.12-
133UbiquitinationKETSENALKKPVADC
HHHCHHHHCCCHHHH
12.66-
157UbiquitinationDAERRSVMAAAQVAG
HHHHHHHHHHHHHHC
1.90-
194UbiquitinationDLPPLDEKPRNVVFI
CCCCCCCCCCCEEEE
49.2821890473
219AcetylationVCAFNKGKLKVLATT
HHHHCCCCEEEEEEE
46.9020167786
221AcetylationAFNKGKLKVLATTFD
HHCCCCEEEEEEECC
38.3920167786
221UbiquitinationAFNKGKLKVLATTFD
HHCCCCEEEEEEECC
38.39-
225PhosphorylationGKLKVLATTFDPYLG
CCEEEEEEECCHHCC
24.6820068231
225UbiquitinationGKLKVLATTFDPYLG
CCEEEEEEECCHHCC
24.68-
226PhosphorylationKLKVLATTFDPYLGG
CEEEEEEECCHHCCC
22.0420068231
230PhosphorylationLATTFDPYLGGRNFD
EEEECCHHCCCCCHH
21.5920068231
249AcetylationDYFCDEFKTKYKINV
HHHCHHHCCCEEEEC
41.9025038526
249UbiquitinationDYFCDEFKTKYKINV
HHHCHHHCCCEEEEC
41.9021906983
250AcetylationYFCDEFKTKYKINVK
HHCHHHCCCEEEECC
44.95-
252AcetylationCDEFKTKYKINVKEN
CHHHCCCEEEECCHH
23.49-
257SuccinylationTKYKINVKENSRALL
CCEEEECCHHHHHHH
46.8423954790
261PhosphorylationINVKENSRALLRLYQ
EECCHHHHHHHHHHH
40.6220068231
265MethylationENSRALLRLYQECEK
HHHHHHHHHHHHHHH
32.00-
272AcetylationRLYQECEKLKKLMSA
HHHHHHHHHHHHHHC
76.8119608861
272UbiquitinationRLYQECEKLKKLMSA
HHHHHHHHHHHHHHC
76.81-
274AcetylationYQECEKLKKLMSANA
HHHHHHHHHHHHCCC
55.7325953088
278PhosphorylationEKLKKLMSANASDLP
HHHHHHHHCCCCCCC
28.89-
280UbiquitinationLKKLMSANASDLPLN
HHHHHHCCCCCCCCE
32.44-
288UbiquitinationASDLPLNIECFMNDL
CCCCCCEEHHHHHCC
6.85-
290GlutathionylationDLPLNIECFMNDLDV
CCCCEEHHHHHCCCH
3.2922555962
296MethylationECFMNDLDVSSKMNR
HHHHHCCCHHHHCCH
40.91-
298PhosphorylationFMNDLDVSSKMNRAQ
HHHCCCHHHHCCHHH
24.7322210691
299PhosphorylationMNDLDVSSKMNRAQF
HHCCCHHHHCCHHHH
35.4522210691
303AcetylationDVSSKMNRAQFEQLC
CHHHHCCHHHHHHHH
26.68-
303UbiquitinationDVSSKMNRAQFEQLC
CHHHHCCHHHHHHHH
26.68-
306UbiquitinationSKMNRAQFEQLCASL
HHCCHHHHHHHHHHH
6.70-
310GlutathionylationRAQFEQLCASLLARV
HHHHHHHHHHHHHHC
2.1222555962
312PhosphorylationQFEQLCASLLARVEP
HHHHHHHHHHHHCCH
23.9524719451
336PhosphorylationNLQREDISSIEIVGG
CCCCCCCCCEEEECC
37.2725332170
337PhosphorylationLQREDISSIEIVGGA
CCCCCCCCEEEECCC
25.2820860994
345PhosphorylationIEIVGGATRIPAVKE
EEEECCCCCCHHHHH
32.1925332170
351UbiquitinationATRIPAVKEQITKFF
CCCCHHHHHHHHHHH
46.11-
356UbiquitinationAVKEQITKFFLKDIS
HHHHHHHHHHHHHHH
35.4321890473
360UbiquitinationQITKFFLKDISTTLN
HHHHHHHHHHHHCCC
48.1121906983
365PhosphorylationFLKDISTTLNADEAV
HHHHHHHCCCHHHHH
15.95-
376GlutathionylationDEAVARGCALQCAIL
HHHHHHHHHHHHHHH
2.5922555962
376S-palmitoylationDEAVARGCALQCAIL
HHHHHHHHHHHHHHH
2.5929575903
380S-palmitoylationARGCALQCAILSPAF
HHHHHHHHHHHCCCE
2.3729575903
382UbiquitinationGCALQCAILSPAFKV
HHHHHHHHHCCCEEE
5.28-
384PhosphorylationALQCAILSPAFKVRE
HHHHHHHCCCEEEEE
14.2025159151
387UbiquitinationCAILSPAFKVREFSI
HHHHCCCEEEEEEEC
9.49-
388UbiquitinationAILSPAFKVREFSIT
HHHCCCEEEEEEECC
42.3521890473
388AcetylationAILSPAFKVREFSIT
HHHCCCEEEEEEECC
42.3525953088
388MethylationAILSPAFKVREFSIT
HHHCCCEEEEEEECC
42.358009857
388UbiquitinationAILSPAFKVREFSIT
HHHCCCEEEEEEECC
42.3521906983
391UbiquitinationSPAFKVREFSITDLV
CCCEEEEEEECCCCE
46.89-
393PhosphorylationAFKVREFSITDLVPY
CEEEEEEECCCCEEE
21.5921406692
395PhosphorylationKVREFSITDLVPYSI
EEEEEECCCCEEEEE
23.2921406692
400PhosphorylationSITDLVPYSITLRWK
ECCCCEEEEEEEEEE
12.7721406692
401PhosphorylationITDLVPYSITLRWKT
CCCCEEEEEEEEEEE
11.7421406692
403PhosphorylationDLVPYSITLRWKTSF
CCEEEEEEEEEEEEC
12.3421406692
407UbiquitinationYSITLRWKTSFEDGS
EEEEEEEEEECCCCC
28.0521890473
408PhosphorylationSITLRWKTSFEDGSG
EEEEEEEEECCCCCC
31.5221406692
409PhosphorylationITLRWKTSFEDGSGE
EEEEEEEECCCCCCC
23.9421406692
414PhosphorylationKTSFEDGSGECEVFC
EEECCCCCCCEEEEE
43.6821406692
415PhosphorylationTSFEDGSGECEVFCK
EECCCCCCCEEEEEC
49.45-
417GlutathionylationFEDGSGECEVFCKNH
CCCCCCCEEEEECCC
6.5322555962
419MethylationDGSGECEVFCKNHPA
CCCCCEEEEECCCCC
11.74-
419UbiquitinationDGSGECEVFCKNHPA
CCCCCEEEEECCCCC
11.74-
422AcetylationGECEVFCKNHPAPFS
CCEEEEECCCCCCCC
46.9926051181
429PhosphorylationKNHPAPFSKVITFHK
CCCCCCCCEEEEEEC
25.5921406692
430AcetylationNHPAPFSKVITFHKK
CCCCCCCEEEEEECC
37.7326051181
436AcetylationSKVITFHKKEPFELE
CEEEEEECCCCEEEE
55.4225038526
453UbiquitinationYTNLHEVPYPDARIG
EECCCCCCCCCCCCE
31.77-
461PhosphorylationYPDARIGSFTIQNVF
CCCCCCEEEEEEEEC
19.4928857561
461UbiquitinationYPDARIGSFTIQNVF
CCCCCCEEEEEEEEC
19.49-
468UbiquitinationSFTIQNVFPQSDGDS
EEEEEEECCCCCCCC
6.29-
494PhosphorylationHGIFSVASASVIEKQ
EEEEEEEEHHHHHHC
20.9425693802
496PhosphorylationIFSVASASVIEKQNL
EEEEEEHHHHHHCCC
22.5725693802
508PhosphorylationQNLEGDHSDAPMETE
CCCCCCCCCCCCCCC
39.9620873877
508UbiquitinationQNLEGDHSDAPMETE
CCCCCCCCCCCCCCC
39.96-
512SulfoxidationGDHSDAPMETETSFK
CCCCCCCCCCCCCCC
12.1821406390
514PhosphorylationHSDAPMETETSFKNE
CCCCCCCCCCCCCCC
38.0125159151
516PhosphorylationDAPMETETSFKNENK
CCCCCCCCCCCCCCC
47.0525159151
517PhosphorylationAPMETETSFKNENKD
CCCCCCCCCCCCCCC
28.1725159151
519AcetylationMETETSFKNENKDNM
CCCCCCCCCCCCCCC
64.2226051181
539PhosphorylationDQEEGHQKCHAEHTP
CHHHHHHHCCCCCCC
23.47-
540GlutathionylationQEEGHQKCHAEHTPE
HHHHHHHCCCCCCCH
2.7122555962
545PhosphorylationQKCHAEHTPEEEIDH
HHCCCCCCCHHHCCC
24.7322167270
548PhosphorylationHAEHTPEEEIDHTGA
CCCCCCHHHCCCCCC
62.55-
571PhosphorylationKQDRLNQTLKKGKVK
HHHHHHHHHHCCCCC
39.2025159151
576PhosphorylationNQTLKKGKVKSIDLP
HHHHHCCCCCCCCCC
56.20-
579PhosphorylationLKKGKVKSIDLPIQS
HHCCCCCCCCCCCCH
25.0725159151
586PhosphorylationSIDLPIQSSLCRQLG
CCCCCCCHHHHHHHC
26.4620873877
587PhosphorylationIDLPIQSSLCRQLGQ
CCCCCCHHHHHHHCH
18.3420873877
589GlutathionylationLPIQSSLCRQLGQDL
CCCCHHHHHHHCHHH
2.5522555962
599PhosphorylationLGQDLLNSYIENEGK
HCHHHHHHHHHHHCC
27.7025159151
600PhosphorylationGQDLLNSYIENEGKM
CHHHHHHHHHHHCCC
15.9223403867
602PhosphorylationDLLNSYIENEGKMIM
HHHHHHHHHHCCCHH
40.7818212344
604UbiquitinationLNSYIENEGKMIMQD
HHHHHHHHCCCHHHH
47.61-
610PhosphorylationNEGKMIMQDKLEKER
HHCCCHHHHHHHHHH
33.49-
612AcetylationGKMIMQDKLEKERND
CCCHHHHHHHHHHHH
41.4723236377
612UbiquitinationGKMIMQDKLEKERND
CCCHHHHHHHHHHHH
41.4721890473
615AcetylationIMQDKLEKERNDAKN
HHHHHHHHHHHHHHH
72.8525953088
618PhosphorylationDKLEKERNDAKNAVE
HHHHHHHHHHHHHHH
55.47-
627PhosphorylationAKNAVEEYVYDFRDR
HHHHHHHHHHHHHHH
7.2728674151
629PhosphorylationNAVEEYVYDFRDRLG
HHHHHHHHHHHHHHC
14.4126356563
630PhosphorylationAVEEYVYDFRDRLGT
HHHHHHHHHHHHHCC
23.2820068231
631PhosphorylationVEEYVYDFRDRLGTV
HHHHHHHHHHHHCCC
4.85-
641AcetylationRLGTVYEKFITPEDL
HHCCCHHHCCCHHHH
25.1226051181
643UbiquitinationGTVYEKFITPEDLSK
CCCHHHCCCHHHHHH
10.46-
644PhosphorylationTVYEKFITPEDLSKL
CCHHHCCCHHHHHHH
24.6128634298
649PhosphorylationFITPEDLSKLSAVLE
CCCHHHHHHHHHHHH
43.8228634298
652PhosphorylationPEDLSKLSAVLEDTE
HHHHHHHHHHHHHHC
21.7728634298
652UbiquitinationPEDLSKLSAVLEDTE
HHHHHHHHHHHHHHC
21.77-
658PhosphorylationLSAVLEDTENWLYED
HHHHHHHHCCCCCCC
23.11-
663PhosphorylationEDTENWLYEDGEDQP
HHHCCCCCCCCCCCC
12.0022817900
671AcetylationEDGEDQPKQVYVDKL
CCCCCCCCEEEHHHH
46.9223236377
672UbiquitinationDGEDQPKQVYVDKLQ
CCCCCCCEEEHHHHH
38.16-
682AcetylationVDKLQELKKYGQPIQ
HHHHHHHHHHCCCCH
43.10-
684PhosphorylationKLQELKKYGQPIQMK
HHHHHHHHCCCCHHH
21.2920068231
692PhosphorylationGQPIQMKYMEHEERP
CCCCHHHCCCHHHCH
11.4620068231
702UbiquitinationHEERPKALNDLGKKI
HHHCHHHHHHHHHHH
6.82-
707AcetylationKALNDLGKKIQLVMK
HHHHHHHHHHHHHHH
54.7425953088
713SulfoxidationGKKIQLVMKVIEAYR
HHHHHHHHHHHHHHC
3.7921406390
715PhosphorylationKIQLVMKVIEAYRNK
HHHHHHHHHHHHCCC
2.3020068231
723PhosphorylationIEAYRNKDERYDHLD
HHHHCCCCCCCCCCC
49.5120068231
726PhosphorylationYRNKDERYDHLDPTE
HCCCCCCCCCCCHHH
12.9824275569
732PhosphorylationRYDHLDPTEMEKVEK
CCCCCCHHHHHHHHH
47.8628258704
736AcetylationLDPTEMEKVEKCISD
CCHHHHHHHHHHHHH
55.1525038526
757PhosphorylationSKMNAQNKLSLTQDP
HHHCCCCCCCCCCCC
27.63-
759PhosphorylationMNAQNKLSLTQDPVV
HCCCCCCCCCCCCCC
30.86-
761PhosphorylationAQNKLSLTQDPVVKV
CCCCCCCCCCCCCCH
27.7917525332
767UbiquitinationLTQDPVVKVSEIVAK
CCCCCCCCHHHHHHC
40.03-
769O-linked_GlycosylationQDPVVKVSEIVAKSK
CCCCCCHHHHHHCCH
18.8523301498
770UbiquitinationDPVVKVSEIVAKSKE
CCCCCHHHHHHCCHH
44.46-
774UbiquitinationKVSEIVAKSKELDNF
CHHHHHHCCHHHHCC
51.68-
776MethylationSEIVAKSKELDNFCN
HHHHHCCHHHHCCCC
62.68-
788AcetylationFCNPIIYKPKPKAEV
CCCCCCCCCCCCCCC
35.8427452117
788UbiquitinationFCNPIIYKPKPKAEV
CCCCCCCCCCCCCCC
35.84-
792PhosphorylationIIYKPKPKAEVPEDK
CCCCCCCCCCCCCCC
64.4017525332
804PhosphorylationEDKPKANSEHNGPMD
CCCCCCCCCCCCCCC
45.1323186163
814PhosphorylationNGPMDGQSGTETKSD
CCCCCCCCCCCCCCC
53.8925159151
816PhosphorylationPMDGQSGTETKSDST
CCCCCCCCCCCCCCC
45.8123186163
819UbiquitinationGQSGTETKSDSTKDS
CCCCCCCCCCCCCCC
46.14-
831AcetylationKDSSQHTKSSGEMEV
CCCCCCCCCCCCCCC
40.2626051181
845PhosphorylationVD-------------
CC-------------
-

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HS74L_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 HS74L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NU188_HUMANNUP188physical
22939629
VP26A_HUMANVPS26Aphysical
22939629
NUBP2_HUMANNUBP2physical
22939629
IPO7_HUMANIPO7physical
22863883
PUS7_HUMANPUS7physical
22863883
DNJA1_HUMANDNAJA1physical
26344197
DNJA2_HUMANDNAJA2physical
26344197
DNJA4_HUMANDNAJA4physical
26344197
DNJB1_HUMANDNAJB1physical
26344197
DJC10_HUMANDNAJC10physical
26344197
DNJC9_HUMANDNAJC9physical
26344197
HINT1_HUMANHINT1physical
26344197
PAIP1_HUMANPAIP1physical
26344197
PP1RB_HUMANPPP1R11physical
26344197
TAGL2_HUMANTAGLN2physical
26344197
TAGL3_HUMANTAGLN3physical
26344197
TTC4_HUMANTTC4physical
26344197

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 HS74L_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-272, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-571, 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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