KIN17_HUMAN - dbPTM
KIN17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIN17_HUMAN
UniProt AC O60870
Protein Name DNA/RNA-binding protein KIN17
Gene Name KIN {ECO:0000312|HGNC:HGNC:6327}
Organism Homo sapiens (Human).
Sequence Length 393
Subcellular Localization Nucleus . Cytoplasm . During S phase, strongly associated with the nuclear matrix, and to chromosomal DNA in the presence of DNA damage. Also shows cytoplasmic localization in elongated spermatids.
Protein Description Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro..
Protein Sequence MGKSDFLTPKAIANRIKSKGLQKLRWYCQMCQKQCRDENGFKCHCMSESHQRQLLLASENPQQFMDYFSEEFRNDFLELLRRRFGTKRVHNNIVYNEYISHREHIHMNATQWETLTDFTKWLGREGLCKVDETPKGWYIQYIDRDPETIRRQLELEKKKKQDLDDEEKTAKFIEEQVRRGLEGKEQEVPTFTELSRENDEEKVTFNLSKGACSSSGATSSKSSTLGPSALKTIGSSASVKRKESSQSSTQSKEKKKKKSALDEIMEIEEEKKRTARTDYWLQPEIIVKIITKKLGEKYHKKKAIVKEVIDKYTAVVKMIDSGDKLKLDQTHLETVIPAPGKRILVLNGGYRGNEGTLESINEKTFSATIVIETGPLKGRRVEGIQYEDISKLA
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
3Methylation-----MGKSDFLTPK
-----CCCCCCCCHH		45.62115972153
3Ubiquitination-----MGKSDFLTPK
-----CCCCCCCCHH		45.6224816145
4Phosphorylation----MGKSDFLTPKA
----CCCCCCCCHHH		28.0625159151
8PhosphorylationMGKSDFLTPKAIANR
CCCCCCCCHHHHHHH		23.8021815630
10UbiquitinationKSDFLTPKAIANRIK
CCCCCCHHHHHHHHH		47.3829967540
23MethylationIKSKGLQKLRWYCQM
HHHCCHHHHHHHHHH		45.09116251909
27PhosphorylationGLQKLRWYCQMCQKQ
CHHHHHHHHHHHHHH		2.6528258704
36MethylationQMCQKQCRDENGFKC
HHHHHHHHCCCCCEE		52.3530760179
78UbiquitinationEFRNDFLELLRRRFG
HHHHHHHHHHHHHHC		45.8324816145
135"N6,N6,N6-trimethyllysine"CKVDETPKGWYIQYI
CCCCCCCCCEEEEEE		70.29-
135MethylationCKVDETPKGWYIQYI
CCCCCCCCCEEEEEE		70.2923349634
135MethylationCKVDETPKGWYIQYI
CCCCCCCCCEEEEEE		70.29-
138PhosphorylationDETPKGWYIQYIDRD
CCCCCCEEEEEECCC		6.19-
148PhosphorylationYIDRDPETIRRQLEL
EECCCHHHHHHHHHH		25.7724719451
184UbiquitinationVRRGLEGKEQEVPTF
HHHHCCCCCCCCCCC		47.0124816145
204PhosphorylationENDEEKVTFNLSKGA
CCCCCCEEEEECCCC		20.2022798277
209MethylationKVTFNLSKGACSSSG
CEEEEECCCCCCCCC		54.41115972135
213PhosphorylationNLSKGACSSSGATSS
EECCCCCCCCCCCCC		27.31-
221MethylationSSGATSSKSSTLGPS
CCCCCCCCCCCCCHH		48.47115972141
222PhosphorylationSGATSSKSSTLGPSA
CCCCCCCCCCCCHHH		30.4221406692
223PhosphorylationGATSSKSSTLGPSAL
CCCCCCCCCCCHHHH		31.2421406692
224PhosphorylationATSSKSSTLGPSALK
CCCCCCCCCCHHHHH		42.7121406692
228PhosphorylationKSSTLGPSALKTIGS
CCCCCCHHHHHHHCC		44.4221406692
231AcetylationTLGPSALKTIGSSAS
CCCHHHHHHHCCCCC		37.5025953088
231MethylationTLGPSALKTIGSSAS
CCCHHHHHHHCCCCC		37.50115972147
232PhosphorylationLGPSALKTIGSSASV
CCHHHHHHHCCCCCC		31.27-
235PhosphorylationSALKTIGSSASVKRK
HHHHHHCCCCCCCCH		20.9124732914
236PhosphorylationALKTIGSSASVKRKE
HHHHHCCCCCCCCHH		21.2524732914
238PhosphorylationKTIGSSASVKRKESS
HHHCCCCCCCCHHHC		30.0723401153
2402-HydroxyisobutyrylationIGSSASVKRKESSQS
HCCCCCCCCHHHCCC		56.08-
244PhosphorylationASVKRKESSQSSTQS
CCCCCHHHCCCCHHC		36.39-
247PhosphorylationKRKESSQSSTQSKEK
CCHHHCCCCHHCHHH		36.9822817900
248PhosphorylationRKESSQSSTQSKEKK
CHHHCCCCHHCHHHH		23.8722817900
249PhosphorylationKESSQSSTQSKEKKK
HHHCCCCHHCHHHHH		41.95-
251PhosphorylationSSQSSTQSKEKKKKK
HCCCCHHCHHHHHHH		42.76-
254AcetylationSSTQSKEKKKKKSAL
CCHHCHHHHHHHHHH		73.8819814685
259PhosphorylationKEKKKKKSALDEIME
HHHHHHHHHHHHHHH		42.8328555341
265SulfoxidationKSALDEIMEIEEEKK
HHHHHHHHHHHHHHH		3.9021406390
279PhosphorylationKRTARTDYWLQPEII
HHHCCCCCCCCHHHH		13.86-
288UbiquitinationLQPEIIVKIITKKLG
CCHHHHHHHHHHHHH		20.2733845483
292UbiquitinationIIVKIITKKLGEKYH
HHHHHHHHHHHHHHH		35.28-
292UbiquitinationIIVKIITKKLGEKYH
HHHHHHHHHHHHHHH		35.28-
302MethylationGEKYHKKKAIVKEVI
HHHHHHCHHHHHHHH		48.4223644510
302MethylationGEKYHKKKAIVKEVI
HHHHHHCHHHHHHHH		48.42-
306MethylationHKKKAIVKEVIDKYT
HHCHHHHHHHHHHHH		39.90-
306MethylationHKKKAIVKEVIDKYT
HHCHHHHHHHHHHHH		39.9023644510
311AcetylationIVKEVIDKYTAVVKM
HHHHHHHHHHHHEEE		33.1226051181
311UbiquitinationIVKEVIDKYTAVVKM
HHHHHHHHHHHHEEE		33.1229967540
324UbiquitinationKMIDSGDKLKLDQTH
EECCCCCCEEEECCC		51.5529967540
326AcetylationIDSGDKLKLDQTHLE
CCCCCCEEEECCCCE		56.627987669
391UbiquitinationIQYEDISKLA-----
CCHHHHHHCC-----		49.0929967540
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 KIN17_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIN17_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 KIN17_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFA2_HUMANRPA2physical
12754299
RFA1_HUMANRPA1physical
12754299
RFA1_HUMANRPA1physical
15831485
PCNA_HUMANPCNAphysical
15831485
DJC17_HUMANDNAJC17physical
26344197
EIF2D_HUMANEIF2Dphysical
26344197
RECQ5_HUMANRECQL5physical
26344197
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIN17_HUMAN

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Related Literatures of Post-Translational Modification

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