DHX57_HUMAN - dbPTM
DHX57_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHX57_HUMAN
UniProt AC Q6P158
Protein Name Putative ATP-dependent RNA helicase DHX57
Gene Name DHX57
Organism Homo sapiens (Human).
Sequence Length 1386
Subcellular Localization
Protein Description Probable ATP-binding RNA helicase..
Protein Sequence MSSSVRRKGKPGKGGGKGSSRGGRGGRSHASKSHGSGGGGGGGGGGGGGNRKASSRIWDDGDDFCIFSESRRPSRPSNSNISKGESRPKWKPKAKVPLQTLHMTSENQEKVKALLRDLQEQDADAGSERGLSGEEEDDEPDCCNDERYWPAGQEPSLVPDLDPLEYAGLASVEPYVPEFTVSPFAVQKLSRYGFNTERCQAVLRMCDGDVGASLEHLLTQCFSETFGERMKISEAVNQISLDECMEQRQEEAFALKSICGEKFIERIQNRVWTIGLELEYLTSRFRKSKPKESTKNVQENSLEICKFYLKGNCKFGSKCRFKHEVPPNQIVGRIERSVDDSHLNAIEDASFLYELEIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYDKALTFAETSEPVVYSLITLLEEESEIVKLLTNTHHKYSDPPVNFLPVPSRTRINNPACHKTVIPNNSFVSNQIPEVEKASESEESDEDDGPAPVIVENESYVNLKKKISKRYDWQAKSVHAENGKICKQFRMKQASRQFQSILQERQSLPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSATLNAELFSDYFNSCPVITIPGRTFPVDQFFLEDAIAVTRYVLQDGSPYMRSMKQISKEKLKARRNRTAFEEVEEDLRLSLHLQDQDSVKDAVPDQQLDFKQLLARYKGVSKSVIKTMSIMDFEKVNLELIEALLEWIVDGKHSYPPGAILVFLPGLAEIKMLYEQLQSNSLFNNRRSNRCVIHPLHSSLSSEEQQAVFVKPPAGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDASKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNHQLLKQQLPEIQRVPLEQLCLRIKILEMFSAHNLQSVFSRLIEPPHTDSLRASKIRLRDLGALTPDERLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFVSPWDKKEEANQKKLEFAFANSDYLALLQAYKGWQLSTKEGVRASYNYCRQNFLSGRVLQEMASLKRQFTELLSDIGFAREGLRAREIEKRAQGGDGVLDATGEEANSNAENPKLISAMLCAALYPNVVQVKSPEGKFQKTSTGAVRMQPKSAELKFVTKNDGYVHIHPSSVNYQVRHFDSPYLLYHEKIKTSRVFIRDCSMVSVYPLVLFGGGQVNVQLQRGEFVVSLDDGWIRFVAASHQVAELVKELRCELDQLLQDKIKNPSIDLCTCPRGSRIISTIVKLVTTQ
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
25PhosphorylationGSSRGGRGGRSHASK
CCCCCCCCCCCCCCC
38.8633259812
25 (in isoform 1)Phosphorylation-38.86-
28PhosphorylationRGGRGGRSHASKSHG
CCCCCCCCCCCCCCC
27.0423090842
30 (in isoform 1)Phosphorylation-21.65-
31PhosphorylationRGGRSHASKSHGSGG
CCCCCCCCCCCCCCC
29.3020363803
33PhosphorylationGRSHASKSHGSGGGG
CCCCCCCCCCCCCCC
30.5023090842
36PhosphorylationHASKSHGSGGGGGGG
CCCCCCCCCCCCCCC
28.9223090842
51MethylationGGGGGGNRKASSRIW
CCCCCCCCCCCCCCC
38.91-
54PhosphorylationGGGNRKASSRIWDDG
CCCCCCCCCCCCCCC
24.1622210691
74PhosphorylationFSESRRPSRPSNSNI
EECCCCCCCCCCCCC
55.8223927012
77PhosphorylationSRRPSRPSNSNISKG
CCCCCCCCCCCCCCC
52.3529496963
79PhosphorylationRPSRPSNSNISKGES
CCCCCCCCCCCCCCC
39.6223927012
82PhosphorylationRPSNSNISKGESRPK
CCCCCCCCCCCCCCC
38.5727251275
104PhosphorylationPLQTLHMTSENQEKV
CCCEEECCCCCHHHH
23.3428348404
105PhosphorylationLQTLHMTSENQEKVK
CCEEECCCCCHHHHH
27.2928857561
127PhosphorylationEQDADAGSERGLSGE
HHHCCCCCCCCCCCC
26.3329255136
132PhosphorylationAGSERGLSGEEEDDE
CCCCCCCCCCCCCCC
47.1623401153
154UbiquitinationRYWPAGQEPSLVPDL
CCCCCCCCCCCCCCC
35.6229967540
190PhosphorylationPFAVQKLSRYGFNTE
HHHHHHHHHCCCCHH
30.4124719451
193UbiquitinationVQKLSRYGFNTERCQ
HHHHHHCCCCHHHHH
14.2832015554
256UbiquitinationQEEAFALKSICGEKF
HHHHHHHHHHHCHHH
34.0529967540
273PhosphorylationRIQNRVWTIGLELEY
HHHHHHHHHHHHHHH
11.4327732954
280PhosphorylationTIGLELEYLTSRFRK
HHHHHHHHHHHHHHH
28.0927732954
282PhosphorylationGLELEYLTSRFRKSK
HHHHHHHHHHHHHCC
19.5627732954
283PhosphorylationLELEYLTSRFRKSKP
HHHHHHHHHHHHCCC
27.1627732954
293PhosphorylationRKSKPKESTKNVQEN
HHCCCCHHCCCCHHC
51.3026270265
294PhosphorylationKSKPKESTKNVQENS
HCCCCHHCCCCHHCH
27.9426270265
295UbiquitinationSKPKESTKNVQENSL
CCCCHHCCCCHHCHH
65.4832015554
301PhosphorylationTKNVQENSLEICKFY
CCCCHHCHHHHHHHH
26.9926270265
373 (in isoform 1)Phosphorylation-12.82-
375 (in isoform 1)Phosphorylation-12.59-
377PhosphorylationPLVAFYSTNENLPLA
CEEEEEECCCCCCCH
34.86-
378 (in isoform 1)Phosphorylation-30.16-
396UbiquitinationISEFLYDKALTFAET
HHHHHHHHHHHHHHC
31.57-
444PhosphorylationVNFLPVPSRTRINNP
CCCCCCCCCCCCCCC
46.6626552605
456PhosphorylationNNPACHKTVIPNNSF
CCCCCCCCCCCCCCC
10.4521406692
462PhosphorylationKTVIPNNSFVSNQIP
CCCCCCCCCHHCCCC
33.3921406692
465PhosphorylationIPNNSFVSNQIPEVE
CCCCCCHHCCCCCHH
22.4721406692
475PhosphorylationIPEVEKASESEESDE
CCCHHHCCCCCCCCC
53.3617081983
477PhosphorylationEVEKASESEESDEDD
CHHHCCCCCCCCCCC
44.1425159151
480PhosphorylationKASESEESDEDDGPA
HCCCCCCCCCCCCCC
42.1025159151
495PhosphorylationPVIVENESYVNLKKK
CEEEECCCEECHHHH
46.0621406692
496PhosphorylationVIVENESYVNLKKKI
EEEECCCEECHHHHH
6.2821406692
512MethylationKRYDWQAKSVHAENG
HCCCCHHCCHHHHCC
37.60-
533UbiquitinationRMKQASRQFQSILQE
HHHHHHHHHHHHHHH
37.9324816145
536PhosphorylationQASRQFQSILQERQS
HHHHHHHHHHHHHHC
26.9328857561
552PhosphorylationPAWEERETILNLLRK
CCHHHHHHHHHHHHH
36.6720068231
605PhosphorylationCTQPRRISAISVAER
ECCCCHHHHHHHHHH
20.1028450419
608PhosphorylationPRRISAISVAERVAK
CCHHHHHHHHHHHHH
18.2628450419
635UbiquitinationQIRLESVKSSATRLL
EEEHHHHHCCHHHHH
48.2324816145
639PhosphorylationESVKSSATRLLYCTT
HHHHCCHHHHHHHHH
24.65-
688UbiquitinationLLVLKDIVSQRPGLQ
HHHHHHHHHCCCCHH
5.9832015554
699UbiquitinationPGLQVILMSATLNAE
CCHHHEEEECCCCHH
1.4329967540
741PhosphorylationDAIAVTRYVLQDGSP
HHHHHHHHHHHCCCH
8.99-
747PhosphorylationRYVLQDGSPYMRSMK
HHHHHCCCHHHHHHH
22.5820068231
749PhosphorylationVLQDGSPYMRSMKQI
HHHCCCHHHHHHHHH
13.5720068231
752PhosphorylationDGSPYMRSMKQISKE
CCCHHHHHHHHHCHH
17.5020068231
757PhosphorylationMRSMKQISKEKLKAR
HHHHHHHCHHHHHHH
32.0626074081
790UbiquitinationLQDQDSVKDAVPDQQ
ECCCCHHHHCCCHHH
43.8732015554
801UbiquitinationPDQQLDFKQLLARYK
CHHHCCHHHHHHHHC
39.4429967540
813PhosphorylationRYKGVSKSVIKTMSI
HHCCCCHHHHHHHCC
22.9029083192
817PhosphorylationVSKSVIKTMSIMDFE
CCHHHHHHHCCCCHH
12.6722210691
819PhosphorylationKSVIKTMSIMDFEKV
HHHHHHHCCCCHHHC
21.7222210691
869PhosphorylationMLYEQLQSNSLFNNR
HHHHHHHHCCCCCCC
36.6624043423
871PhosphorylationYEQLQSNSLFNNRRS
HHHHHHCCCCCCCCC
39.3224043423
1002UbiquitinationQRVPLEQLCLRIKIL
HCCCHHHHHHHHHHH
1.8529967540
1030PhosphorylationRLIEPPHTDSLRASK
HHCCCCCCCCCCHHH
32.8122817900
1032PhosphorylationIEPPHTDSLRASKIR
CCCCCCCCCCHHHCC
22.4022817900
1034UbiquitinationPPHTDSLRASKIRLR
CCCCCCCCHHHCCHH
40.5432015554
1036PhosphorylationHTDSLRASKIRLRDL
CCCCCCHHHCCHHHH
23.3722817900
1104MalonylationFVSPWDKKEEANQKK
CCCCCCHHHHHHHHH
59.3126320211
1104AcetylationFVSPWDKKEEANQKK
CCCCCCHHHHHHHHH
59.3126051181
1104UbiquitinationFVSPWDKKEEANQKK
CCCCCCHHHHHHHHH
59.3129967540
1135UbiquitinationYKGWQLSTKEGVRAS
HCCCCCCCHHHHHHH
41.5329967540
1136UbiquitinationKGWQLSTKEGVRASY
CCCCCCCHHHHHHHH
49.4432015554
1142PhosphorylationTKEGVRASYNYCRQN
CHHHHHHHHHHHHHH
11.89-
1152PhosphorylationYCRQNFLSGRVLQEM
HHHHHCCCHHHHHHH
22.0324719451
11632-HydroxyisobutyrylationLQEMASLKRQFTELL
HHHHHHHHHHHHHHH
41.48-
1237UbiquitinationSPEGKFQKTSTGAVR
CCCCCCEECCCCCEE
47.8029967540
1256UbiquitinationSAELKFVTKNDGYVH
CEEEEEEECCCCEEE
27.5429967540
1261PhosphorylationFVTKNDGYVHIHPSS
EEECCCCEEEECHHH
7.54-
1267PhosphorylationGYVHIHPSSVNYQVR
CEEEECHHHCCEEEE
32.53-
1271PhosphorylationIHPSSVNYQVRHFDS
ECHHHCCEEEECCCC
13.26-
1358UbiquitinationLDQLLQDKIKNPSID
HHHHHHHHHHCCCCC
42.4929967540
1373PhosphorylationLCTCPRGSRIISTIV
CCCCCCCHHHHHHHH
22.9128509920
1377PhosphorylationPRGSRIISTIVKLVT
CCCHHHHHHHHHHHH
15.0928509920
1378PhosphorylationRGSRIISTIVKLVTT
CCHHHHHHHHHHHHC
21.2728509920
1384PhosphorylationSTIVKLVTTQ-----
HHHHHHHHCC-----
29.8928509920
1385PhosphorylationTIVKLVTTQ------
HHHHHHHCC------
25.4628509920

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 DHX57_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHX57_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 DHX57_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
SESN2_HUMANSESN2physical
28514442
APOD_HUMANAPODphysical
28514442
ZDH17_HUMANZDHHC17physical
28514442
CLUS_HUMANCLUphysical
28514442
RS2_HUMANRPS2physical
28514442
RSSA_HUMANRPSAphysical
28514442
TTL12_HUMANTTLL12physical
28514442
ACTBL_HUMANACTBL2physical
28514442
SRC_HUMANSRCphysical
28514442
H14_HUMANHIST1H1Ephysical
28514442
HSP7C_HUMANHSPA8physical
28514442
EF1A2_HUMANEEF1A2physical
28514442
UBB_HUMANUBBphysical
28514442
GLMN_HUMANGLMNphysical
28514442
RS14_HUMANRPS14physical
28514442
MUCL1_HUMANMUCL1physical
28514442

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 DHX57_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-132, ANDMASS SPECTROMETRY.
"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 SER-127; SER-132; SER-475;SER-477 AND SER-480, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND MASSSPECTROMETRY.
"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-127; SER-475; SER-477AND SER-480, AND MASS SPECTROMETRY.

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