CLP1_HUMAN - dbPTM
CLP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLP1_HUMAN
UniProt AC Q92989
Protein Name Polyribonucleotide 5'-hydroxyl-kinase Clp1 {ECO:0000255|HAMAP-Rule:MF_03035}
Gene Name CLP1 {ECO:0000255|HAMAP-Rule:MF_03035}
Organism Homo sapiens (Human).
Sequence Length 425
Subcellular Localization Nucleus .
Protein Description Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), double-stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA is phosphorylated more efficiently than dsDNA, and the RNA component of a DNA:RNA hybrid is phosphorylated more efficiently than the DNA component. Plays a key role in both tRNA splicing and mRNA 3'-end formation. Component of the tRNA splicing endonuclease complex: phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA splicing; this phosphorylation event is a prerequisite for the subsequent ligation of the two exon halves and the production of a mature tRNA. [PubMed: 24766809]
Protein Sequence MGEEANDDKKPTTKFELERETELRFEVEASQSVQLELLTGMAEIFGTELTRNKKFTFDAGAKVAVFTWHGCSVQLSGRTEVAYVSKDTPMLLYLNTHTALEQMRRQAEKEEERGPRVMVVGPTDVGKSTVCRLLLNYAVRLGRRPTYVELDVGQGSVSIPGTMGALYIERPADVEEGFSIQAPLVYHFGSTTPGTNIKLYNKITSRLADVFNQRCEVNRRASVSGCVINTCGWVKGSGYQALVHAASAFEVDVVVVLDQERLYNELKRDLPHFVRTVLLPKSGGVVERSKDFRRECRDERIREYFYGFRGCFYPHAFNVKFSDVKIYKVGAPTIPDSCLPLGMSQEDNQLKLVPVTPGRDMVHHLLSVSTAEGTEENLSETSVAGFIVVTSVDLEHQVFTVLSPAPRPLPKNFLLIMDIRFMDLK
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
9UbiquitinationGEEANDDKKPTTKFE
CCCCCCCCCCCCCEE
64.6124816145
12PhosphorylationANDDKKPTTKFELER
CCCCCCCCCCEEEEE
52.0429759185
13PhosphorylationNDDKKPTTKFELERE
CCCCCCCCCEEEEEE
42.1129759185
30PhosphorylationLRFEVEASQSVQLEL
EEEEEEECHHHHHHH
14.96-
32PhosphorylationFEVEASQSVQLELLT
EEEEECHHHHHHHHH
14.88-
54UbiquitinationTELTRNKKFTFDAGA
CCCCCCCCEEECCCC
53.8629967540
79PhosphorylationSVQLSGRTEVAYVSK
EEEECCCEEEEEEEC
38.0321406692
83PhosphorylationSGRTEVAYVSKDTPM
CCCEEEEEEECCCCE
15.4921406692
85PhosphorylationRTEVAYVSKDTPMLL
CEEEEEEECCCCEEE
16.4921406692
88PhosphorylationVAYVSKDTPMLLYLN
EEEEECCCCEEEEEE
17.8424275569
93PhosphorylationKDTPMLLYLNTHTAL
CCCCEEEEEEHHHHH
8.2424275569
118SulfoxidationEERGPRVMVVGPTDV
HHHCCCEEEECCCCC
1.8221406390
127UbiquitinationVGPTDVGKSTVCRLL
ECCCCCCHHHHHHHH
42.6821963094
202UbiquitinationTNIKLYNKITSRLAD
CCHHHHHHHHHHHHH
33.5329967540
203UbiquitinationNIKLYNKITSRLADV
CHHHHHHHHHHHHHH
3.6327667366
217UbiquitinationVFNQRCEVNRRASVS
HHHHCCCCCCCCCCC
8.4833845483
222PhosphorylationCEVNRRASVSGCVIN
CCCCCCCCCCCEEEE
18.2727251275
224PhosphorylationVNRRASVSGCVINTC
CCCCCCCCCEEEECC
24.7927251275
256UbiquitinationFEVDVVVVLDQERLY
CCCEEEEEECHHHHH
3.0933845483
261UbiquitinationVVVLDQERLYNELKR
EEEECHHHHHHHHHH
36.5233845483
263PhosphorylationVLDQERLYNELKRDL
EECHHHHHHHHHHHC
16.8928152594
264UbiquitinationLDQERLYNELKRDLP
ECHHHHHHHHHHHCC
53.3622817900
267AcetylationERLYNELKRDLPHFV
HHHHHHHHHHCCHHH
37.3725953088
267UbiquitinationERLYNELKRDLPHFV
HHHHHHHHHHCCHHH
37.3727667366
281UbiquitinationVRTVLLPKSGGVVER
HEEEEECCCCCCEEC
62.8021906983
282PhosphorylationRTVLLPKSGGVVERS
EEEEECCCCCCEECC
38.5530576142
287UbiquitinationPKSGGVVERSKDFRR
CCCCCCEECCHHHHH
49.1621963094
289PhosphorylationSGGVVERSKDFRREC
CCCCEECCHHHHHHH
24.0730576142
313PhosphorylationYGFRGCFYPHAFNVK
HCCCCCCCCEEEEEE
9.74-
320AcetylationYPHAFNVKFSDVKIY
CCEEEEEECCCCEEE
40.0126051181
320UbiquitinationYPHAFNVKFSDVKIY
CCEEEEEECCCCEEE
40.0133845483
325UbiquitinationNVKFSDVKIYKVGAP
EEECCCCEEEEECCC
45.3622817900
328UbiquitinationFSDVKIYKVGAPTIP
CCCCEEEEECCCCCC
37.3522817900
344PhosphorylationSCLPLGMSQEDNQLK
CCCCCCCCCCCCCEE
28.7225159151
351UbiquitinationSQEDNQLKLVPVTPG
CCCCCCEEEEECCCC
37.3621963094
356PhosphorylationQLKLVPVTPGRDMVH
CEEEEECCCCHHHHH
17.6023312004

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 CLP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLP1_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 CLP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEN2_HUMANTSEN2physical
15109492
SEN54_HUMANTSEN54physical
15109492
SEN34_HUMANTSEN34physical
15109492
CPSF5_HUMANNUDT21physical
11060040
CPSF2_HUMANCPSF2physical
11060040
CPSF6_HUMANCPSF6physical
11060040
CPSF7_HUMANCPSF7physical
11060040
CREB3_HUMANCREB3physical
11384994
A4_HUMANAPPphysical
21832049

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615803Pontocerebellar hypoplasia 10 (PCH10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CLP1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP