PRP17_HUMAN - dbPTM
PRP17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRP17_HUMAN
UniProt AC O60508
Protein Name Pre-mRNA-processing factor 17
Gene Name CDC40
Organism Homo sapiens (Human).
Sequence Length 579
Subcellular Localization Nucleus .
Protein Description Associates with the spliceosome late in the splicing pathway and may function in the second step of pre-mRNA splicing..
Protein Sequence MSAAIAALAASYGSGSGSESDSDSESSRCPLPAADSLMHLTKSPSSKPSLAVAVDSAPEVAVKEDLETGVHLDPAVKEVQYNPTYETMFAPEFGPENPFRTQQMAAPRNMLSGYAEPAHINDFMFEQQRRTFATYGYALDPSLDNHQVSAKYIGSVEEAEKNQGLTVFETGQKKTEKRKKFKENDASNIDGFLGPWAKYVDEKDVAKPSEEEQKELDEITAKRQKKGKQEEEKPGEEKTILHVKEMYDYQGRSYLHIPQDVGVNLRSTMPPEKCYLPKKQIHVWSGHTKGVSAVRLFPLSGHLLLSCSMDCKIKLWEVYGERRCLRTFIGHSKAVRDICFNTAGTQFLSAAYDRYLKLWDTETGQCISRFTNRKVPYCVKFNPDEDKQNLFVAGMSDKKIVQWDIRSGEIVQEYDRHLGAVNTIVFVDENRRFVSTSDDKSLRVWEWDIPVDFKYIAEPSMHSMPAVTLSPNGKWLACQSMDNQILIFGAQNRFRLNKKKIFKGHMVAGYACQVDFSPDMSYVISGDGNGKLNIWDWKTTKLYSRFKAHDKVCIGAVWHPHETSKVITCGWDGLIKLWD
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------MSAAIAALA
------CHHHHHHHH
26.8020068231
11PhosphorylationAIAALAASYGSGSGS
HHHHHHHHHCCCCCC
25.1530108239
12PhosphorylationIAALAASYGSGSGSE
HHHHHHHHCCCCCCC
15.5830108239
14PhosphorylationALAASYGSGSGSESD
HHHHHHCCCCCCCCC
22.8924043423
16PhosphorylationAASYGSGSGSESDSD
HHHHCCCCCCCCCCC
40.6224043423
18PhosphorylationSYGSGSGSESDSDSE
HHCCCCCCCCCCCCC
35.3124043423
20PhosphorylationGSGSGSESDSDSESS
CCCCCCCCCCCCCCC
44.0824043423
22PhosphorylationGSGSESDSDSESSRC
CCCCCCCCCCCCCCC
52.9224043423
24PhosphorylationGSESDSDSESSRCPL
CCCCCCCCCCCCCCC
43.2430108239
26PhosphorylationESDSDSESSRCPLPA
CCCCCCCCCCCCCCH
27.3430108239
27PhosphorylationSDSDSESSRCPLPAA
CCCCCCCCCCCCCHH
33.5730108239
36PhosphorylationCPLPAADSLMHLTKS
CCCCHHHHHHHHHCC
23.9026074081
41PhosphorylationADSLMHLTKSPSSKP
HHHHHHHHCCCCCCC
18.1326074081
43PhosphorylationSLMHLTKSPSSKPSL
HHHHHHCCCCCCCCE
25.4429255136
45PhosphorylationMHLTKSPSSKPSLAV
HHHHCCCCCCCCEEE
59.0729255136
46PhosphorylationHLTKSPSSKPSLAVA
HHHCCCCCCCCEEEE
52.5529255136
47AcetylationLTKSPSSKPSLAVAV
HHCCCCCCCCEEEEE
42.8526051181
49PhosphorylationKSPSSKPSLAVAVDS
CCCCCCCCEEEEECC
32.4730278072
56PhosphorylationSLAVAVDSAPEVAVK
CEEEEECCCCCEEEC
38.8425159151
81PhosphorylationPAVKEVQYNPTYETM
HHHCEEECCCCCCCC
28.43-
84PhosphorylationKEVQYNPTYETMFAP
CEEECCCCCCCCCCC
30.2828796482
85PhosphorylationEVQYNPTYETMFAPE
EEECCCCCCCCCCCC
15.6228796482
87PhosphorylationQYNPTYETMFAPEFG
ECCCCCCCCCCCCCC
13.7428796482
114PhosphorylationPRNMLSGYAEPAHIN
CCCHHHCCCCCHHHC
12.3827642862
131PhosphorylationMFEQQRRTFATYGYA
HHHHHHHHHHHCCEE
21.5828555341
134PhosphorylationQQRRTFATYGYALDP
HHHHHHHHCCEECCC
17.1829978859
135PhosphorylationQRRTFATYGYALDPS
HHHHHHHCCEECCCC
12.5229978859
137PhosphorylationRTFATYGYALDPSLD
HHHHHCCEECCCCCC
8.1229978859
142PhosphorylationYGYALDPSLDNHQVS
CCEECCCCCCCCCCC
48.2828555341
170PhosphorylationQGLTVFETGQKKTEK
CCCEEEECCCCHHHH
33.1928555341
175PhosphorylationFETGQKKTEKRKKFK
EECCCCHHHHHHHHC
54.5028555341
187PhosphorylationKFKENDASNIDGFLG
HHCCCCCCCCCCCHH
36.8620068231
198UbiquitinationGFLGPWAKYVDEKDV
CCHHHHHHHCCHHHC
41.7729967540
222UbiquitinationELDEITAKRQKKGKQ
HHHHHHHHHHHCCCC
46.8732015554
226AcetylationITAKRQKKGKQEEEK
HHHHHHHCCCCCCCC
64.107910527
228AcetylationAKRQKKGKQEEEKPG
HHHHHCCCCCCCCCC
64.517910537
244UbiquitinationEKTILHVKEMYDYQG
CCEEEEEEEEECCCC
26.4732015554
268PhosphorylationVGVNLRSTMPPEKCY
CCCCCCCCCCHHHCC
27.5430576142
307S-palmitoylationSGHLLLSCSMDCKIK
CCCEEHHEECCCEEE
3.8429575903
311S-palmitoylationLLSCSMDCKIKLWEV
EHHEECCCEEEEEEE
3.5329575903
314AcetylationCSMDCKIKLWEVYGE
EECCCEEEEEEECCH
32.8025953088
380UbiquitinationRKVPYCVKFNPDEDK
CCCCEEEECCCCHHH
35.5429967540
387UbiquitinationKFNPDEDKQNLFVAG
ECCCCHHHCCEEEEE
38.7529967540
399AcetylationVAGMSDKKIVQWDIR
EEECCCCEEEEEECC
53.7718585733
435PhosphorylationDENRRFVSTSDDKSL
ECCCCEEECCCCCCE
21.3421406692
436PhosphorylationENRRFVSTSDDKSLR
CCCCEEECCCCCCEE
30.7621406692
440UbiquitinationFVSTSDDKSLRVWEW
EEECCCCCCEEEEEE
57.2824816145
541AcetylationIWDWKTTKLYSRFKA
EEEECCHHHHHHHHH
51.1425953088
544PhosphorylationWKTTKLYSRFKAHDK
ECCHHHHHHHHHCCC
41.5024719451

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 PRP17_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRP17_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 PRP17_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRP19_HUMANPRPF19physical
22365833
CCD12_HUMANCCDC12physical
26344197
CRNL1_HUMANCRNKL1physical
26344197
U5S1_HUMANEFTUD2physical
26344197
ISY1_HUMANISY1physical
26344197
SF3B3_HUMANSF3B3physical
26344197
SNW1_HUMANSNW1physical
26344197
SRPK3_HUMANSRPK3physical
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 PRP17_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-14; SER-16; SER-18;SER-20; SER-22 AND SER-24, AND MASS SPECTROMETRY.

TOP