PRP31_HUMAN - dbPTM
PRP31_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRP31_HUMAN
UniProt AC Q8WWY3
Protein Name U4/U6 small nuclear ribonucleoprotein Prp31
Gene Name PRPF31
Organism Homo sapiens (Human).
Sequence Length 499
Subcellular Localization Nucleus . Nucleus speckle . Nucleus, Cajal body . Predominantly found in speckles and in Cajal bodies.
Protein Description Involved in pre-mRNA splicing as component of the spliceosome. [PubMed: 11867543]
Protein Sequence MSLADELLADLEEAAEEEEGGSYGEEEEEPAIEDVQEETQLDLSGDSVKTIAKLWDSKMFAEIMMKIEEYISKQAKASEVMGPVEAAPEYRVIVDANNLTVEIENELNIIHKFIRDKYSKRFPELESLVPNALDYIRTVKELGNSLDKCKNNENLQQILTNATIMVVSVTASTTQGQQLSEEELERLEEACDMALELNASKHRIYEYVESRMSFIAPNLSIIIGASTAAKIMGVAGGLTNLSKMPACNIMLLGAQRKTLSGFSSTSVLPHTGYIYHSDIVQSLPPDLRRKAARLVAAKCTLAARVDSFHESTEGKVGYELKDEIERKFDKWQEPPPVKQVKPLPAPLDGQRKKRGGRRYRKMKERLGLTEIRKQANRMSFGEIEEDAYQEDLGFSLGHLGKSGSGRVRQTQVNEATKARISKTLQRTLQKQSVVYGGKSTIRDRSSGTASSVAFTPLQGLEIVNPQAAEKKVAEANQKYFSSMAEFLKVKGEKSGLMST
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------MSLADELLA
------CCHHHHHHH
32.0628464451
23PhosphorylationEEEEGGSYGEEEEEP
HHHCCCCCCCCCCCC
31.6528464451
532-HydroxyisobutyrylationDSVKTIAKLWDSKMF
CHHHHHHHHHCCHHH
46.38-
53UbiquitinationDSVKTIAKLWDSKMF
CHHHHHHHHHCCHHH
46.38-
58UbiquitinationIAKLWDSKMFAEIMM
HHHHHCCHHHHHHHH
35.2532015554
70PhosphorylationIMMKIEEYISKQAKA
HHHHHHHHHHHHCHH
9.56-
73UbiquitinationKIEEYISKQAKASEV
HHHHHHHHHCHHHHH
44.7227667366
73AcetylationKIEEYISKQAKASEV
HHHHHHHHHCHHHHH
44.7225953088
76UbiquitinationEYISKQAKASEVMGP
HHHHHHCHHHHHCCC
50.37-
81SulfoxidationQAKASEVMGPVEAAP
HCHHHHHCCCCCCCC
4.3921406390
90PhosphorylationPVEAAPEYRVIVDAN
CCCCCCCEEEEEECC
14.77-
140UbiquitinationLDYIRTVKELGNSLD
HHHHHHHHHHHHHHH
46.7629967540
1402-HydroxyisobutyrylationLDYIRTVKELGNSLD
HHHHHHHHHHHHHHH
46.76-
145PhosphorylationTVKELGNSLDKCKNN
HHHHHHHHHHHHCCC
35.8327067055
148UbiquitinationELGNSLDKCKNNENL
HHHHHHHHHCCCHHH
53.0229967540
201UbiquitinationALELNASKHRIYEYV
HHHHCCCHHHHHHHH
34.2029901268
205PhosphorylationNASKHRIYEYVESRM
CCCHHHHHHHHHHHH
10.9327273156
207PhosphorylationSKHRIYEYVESRMSF
CHHHHHHHHHHHHCH
7.7928152594
210PhosphorylationRIYEYVESRMSFIAP
HHHHHHHHHHCHHCC
24.2028152594
239PhosphorylationMGVAGGLTNLSKMPA
HCHHCCCCCHHCCCC
37.0721406692
242PhosphorylationAGGLTNLSKMPACNI
HCCCCCHHCCCCCCE
29.0421406692
273PhosphorylationSVLPHTGYIYHSDIV
CCCCCCCEEECHHHH
10.2417360941
275PhosphorylationLPHTGYIYHSDIVQS
CCCCCEEECHHHHHH
6.1822817900
298UbiquitinationAARLVAAKCTLAARV
HHHHHHHHHHHHHCC
20.29-
298SumoylationAARLVAAKCTLAARV
HHHHHHHHHHHHHCC
20.29-
298UbiquitinationAARLVAAKCTLAARV
HHHHHHHHHHHHHCC
20.2929967540
298AcetylationAARLVAAKCTLAARV
HHHHHHHHHHHHHCC
20.2925953088
298SumoylationAARLVAAKCTLAARV
HHHHHHHHHHHHHCC
20.29-
307PhosphorylationTLAARVDSFHESTEG
HHHHCCCCCHHCCCC
26.1629507054
321UbiquitinationGKVGYELKDEIERKF
CCCCCCCHHHHHHHH
41.1829967540
321UbiquitinationGKVGYELKDEIERKF
CCCCCCCHHHHHHHH
41.18-
321SumoylationGKVGYELKDEIERKF
CCCCCCCHHHHHHHH
41.18-
321SumoylationGKVGYELKDEIERKF
CCCCCCCHHHHHHHH
41.18-
327SumoylationLKDEIERKFDKWQEP
CHHHHHHHHCCCCCC
45.16-
327SumoylationLKDEIERKFDKWQEP
CHHHHHHHHCCCCCC
45.16-
330UbiquitinationEIERKFDKWQEPPPV
HHHHHHCCCCCCCCC
54.6429967540
338UbiquitinationWQEPPPVKQVKPLPA
CCCCCCCCCCCCCCC
55.9633845483
338SumoylationWQEPPPVKQVKPLPA
CCCCCCCCCCCCCCC
55.96-
338SumoylationWQEPPPVKQVKPLPA
CCCCCCCCCCCCCCC
55.96-
341AcetylationPPPVKQVKPLPAPLD
CCCCCCCCCCCCCCC
38.0423236377
341AcetylationPPPVKQVKPLPAPLD
CCCCCCCCCCCCCCC
38.04-
369PhosphorylationMKERLGLTEIRKQAN
HHHHHCCHHHHHHHH
27.8028555341
379PhosphorylationRKQANRMSFGEIEED
HHHHHHCCCHHCCCH
27.1921712546
388PhosphorylationGEIEEDAYQEDLGFS
HHCCCHHHHHHHCCC
25.4228674151
395PhosphorylationYQEDLGFSLGHLGKS
HHHHHCCCHHHCCCC
31.4826074081
401UbiquitinationFSLGHLGKSGSGRVR
CCHHHCCCCCCCCCC
58.9932015554
402PhosphorylationSLGHLGKSGSGRVRQ
CHHHCCCCCCCCCCH
36.0726074081
404PhosphorylationGHLGKSGSGRVRQTQ
HHCCCCCCCCCCHHH
30.4326074081
410PhosphorylationGSGRVRQTQVNEATK
CCCCCCHHHHHHHHH
24.7426074081
416PhosphorylationQTQVNEATKARISKT
HHHHHHHHHHHHHHH
21.0321406692
417UbiquitinationTQVNEATKARISKTL
HHHHHHHHHHHHHHH
42.59-
417SumoylationTQVNEATKARISKTL
HHHHHHHHHHHHHHH
42.59-
417 (in isoform 1)Ubiquitination-42.5921890473
417SumoylationTQVNEATKARISKTL
HHHHHHHHHHHHHHH
42.59-
417UbiquitinationTQVNEATKARISKTL
HHHHHHHHHHHHHHH
42.5922817900
417AcetylationTQVNEATKARISKTL
HHHHHHHHHHHHHHH
42.5925953088
421PhosphorylationEATKARISKTLQRTL
HHHHHHHHHHHHHHH
17.6522798277
422SumoylationATKARISKTLQRTLQ
HHHHHHHHHHHHHHH
51.38-
422SumoylationATKARISKTLQRTLQ
HHHHHHHHHHHHHHH
51.38-
422UbiquitinationATKARISKTLQRTLQ
HHHHHHHHHHHHHHH
51.3822817900
423PhosphorylationTKARISKTLQRTLQK
HHHHHHHHHHHHHHH
22.7222798277
430 (in isoform 1)Ubiquitination-47.8821890473
430SumoylationTLQRTLQKQSVVYGG
HHHHHHHHCCEEECC
47.88-
430UbiquitinationTLQRTLQKQSVVYGG
HHHHHHHHCCEEECC
47.8822817900
430UbiquitinationTLQRTLQKQSVVYGG
HHHHHHHHCCEEECC
47.88-
430SumoylationTLQRTLQKQSVVYGG
HHHHHHHHCCEEECC
47.88-
432PhosphorylationQRTLQKQSVVYGGKS
HHHHHHCCEEECCCC
22.1523927012
435PhosphorylationLQKQSVVYGGKSTIR
HHHCCEEECCCCEEE
20.2920164059
438MethylationQSVVYGGKSTIRDRS
CCEEECCCCEEECCC
39.8130591561
438AcetylationQSVVYGGKSTIRDRS
CCEEECCCCEEECCC
39.8125953088
438UbiquitinationQSVVYGGKSTIRDRS
CCEEECCCCEEECCC
39.8132015554
439PhosphorylationSVVYGGKSTIRDRSS
CEEECCCCEEECCCC
32.1323401153
440PhosphorylationVVYGGKSTIRDRSSG
EEECCCCEEECCCCC
24.4223401153
445PhosphorylationKSTIRDRSSGTASSV
CCEEECCCCCCCCEE
37.0923927012
446PhosphorylationSTIRDRSSGTASSVA
CEEECCCCCCCCEEE
40.8523927012
448PhosphorylationIRDRSSGTASSVAFT
EECCCCCCCCEEEEE
25.8923927012
450PhosphorylationDRSSGTASSVAFTPL
CCCCCCCCEEEEEEC
25.7823927012
451PhosphorylationRSSGTASSVAFTPLQ
CCCCCCCEEEEEECC
18.2723927012
455PhosphorylationTASSVAFTPLQGLEI
CCCEEEEEECCCCEE
17.2223927012
470AcetylationVNPQAAEKKVAEANQ
CCHHHHHHHHHHHHH
48.0625953088
470UbiquitinationVNPQAAEKKVAEANQ
CCHHHHHHHHHHHHH
48.0632015554
471UbiquitinationNPQAAEKKVAEANQK
CHHHHHHHHHHHHHH
37.88-
471SumoylationNPQAAEKKVAEANQK
CHHHHHHHHHHHHHH
37.8828112733
478 (in isoform 1)Ubiquitination-48.3321890473
478UbiquitinationKVAEANQKYFSSMAE
HHHHHHHHHHHHHHH
48.3322817900
478SumoylationKVAEANQKYFSSMAE
HHHHHHHHHHHHHHH
48.3328112733
478SumoylationKVAEANQKYFSSMAE
HHHHHHHHHHHHHHH
48.33-
478UbiquitinationKVAEANQKYFSSMAE
HHHHHHHHHHHHHHH
48.33-
479PhosphorylationVAEANQKYFSSMAEF
HHHHHHHHHHHHHHH
10.0320068231
481PhosphorylationEANQKYFSSMAEFLK
HHHHHHHHHHHHHHH
19.0020068231
482PhosphorylationANQKYFSSMAEFLKV
HHHHHHHHHHHHHHH
16.4720068231
488UbiquitinationSSMAEFLKVKGEKSG
HHHHHHHHHHCCCCC
47.4232015554
490UbiquitinationMAEFLKVKGEKSGLM
HHHHHHHHCCCCCCC
60.82-
493UbiquitinationFLKVKGEKSGLMST-
HHHHHCCCCCCCCC-
59.50-
494PhosphorylationLKVKGEKSGLMST--
HHHHCCCCCCCCC--
32.6224732914
498PhosphorylationGEKSGLMST------
CCCCCCCCC------
35.6924732914
499PhosphorylationEKSGLMST-------
CCCCCCCC-------
28.7624732914

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 PRP31_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRP31_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 PRP31_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTBL1_HUMANCTNNBL1physical
21385873
IMA1_HUMANKPNA2physical
21385873
IMA5_HUMANKPNA1physical
21385873
NH2L1_HUMANNHP2L1physical
16723661
PPIH_HUMANPPIHphysical
16723661
PRPF3_HUMANPRPF3physical
16723661
PRP4_HUMANPRPF4physical
16723661
PRP31_HUMANPRPF31physical
16723661
PRP6_HUMANPRPF6physical
16723661
PRP6_HUMANPRPF6physical
22939629
SNUT1_HUMANSART1physical
22939629
SF3B1_HUMANSF3B1physical
22939629
SF3B3_HUMANSF3B3physical
22939629
SYF1_HUMANXAB2physical
22939629
SF3A1_HUMANSF3A1physical
22939629
SF3A3_HUMANSF3A3physical
22939629
RU2A_HUMANSNRPA1physical
22939629
RU2B_HUMANSNRPB2physical
22939629
SF3A2_HUMANSF3A2physical
22939629
TFDP1_HUMANTFDP1physical
22939629
RENT2_HUMANUPF2physical
22939629
STRN3_HUMANSTRN3physical
22939629
RBM25_HUMANRBM25physical
22365833
PHF5A_HUMANPHF5Aphysical
22365833
PRP6_HUMANPRPF6physical
22365833
RBM4_HUMANRBM4physical
22365833
HNRH2_HUMANHNRNPH2physical
22365833
RACK1_HUMANGNB2L1physical
22365833
CDA7L_HUMANCDCA7Lphysical
25416956
ZN250_HUMANZNF250physical
25416956
CC136_HUMANCCDC136physical
25416956
CEP70_HUMANCEP70physical
25416956
TSG10_HUMANTSGA10physical
25416956
ZN587_HUMANZNF587physical
25416956
C1QT1_HUMANC1QTNF1physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
K1C40_HUMANKRT40physical
25416956
PRIC1_HUMANPRICKLE1physical
25416956
MIPO1_HUMANMIPOL1physical
25416956
RBY1F_HUMANRBMY1Fphysical
25416956
KCTD6_HUMANKCTD6physical
25416956
KHDR2_HUMANKHDRBS2physical
25416956
CCD57_HUMANCCDC57physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
LURA1_HUMANLURAP1physical
25416956
CD2B2_HUMANCD2BP2physical
26344197
DDX23_HUMANDDX23physical
26344197
U5S1_HUMANEFTUD2physical
26344197
PRP4_HUMANPRPF4physical
26344197
PRP8_HUMANPRPF8physical
26344197
SNUT1_HUMANSART1physical
26344197
U520_HUMANSNRNP200physical
26344197
SART3_HUMANSART3physical
28514442
DIEXF_HUMANDIEXFphysical
28514442
ZN622_HUMANZNF622physical
28514442
STPAP_HUMANTUT1physical
28514442
FBRS_HUMANFBRSphysical
28514442
PRP4_HUMANPRPF4physical
28514442
MTHR_HUMANMTHFRphysical
28514442
SUFU_HUMANSUFUphysical
28514442
WBP4_HUMANWBP4physical
28514442
ARI1_HUMANARIH1physical
28514442
MEPCE_HUMANMEPCEphysical
28514442
RUXG_HUMANSNRPGphysical
27173435
SMD1_HUMANSNRPD1physical
27173435
RSMB_HUMANSNRPBphysical
27173435
SMD2_HUMANSNRPD2physical
27173435
RS19_HUMANRPS19physical
27173435
OSBL1_HUMANOSBPL1Aphysical
27173435
SMD3_HUMANSNRPD3physical
27173435
TT21B_HUMANTTC21Bphysical
27173435
IFT46_HUMANIFT46physical
27173435
UBE2N_HUMANUBE2Nphysical
27173435
RANB9_HUMANRANBP9physical
27173435
NH2L1_HUMANNHP2L1physical
26275778
ZNHI3_HUMANZNHIT3physical
26275778
NUFP1_HUMANNUFIP1physical
26275778
RUVB1_HUMANRUVBL1physical
26275778
SMN_HUMANSMN1physical
26275778

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600138Retinitis pigmentosa 11 (RP11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRP31_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379 AND THR-455, 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 THR-448 AND THR-455, ANDMASS SPECTROMETRY.

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