PR40B_HUMAN - dbPTM
PR40B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PR40B_HUMAN
UniProt AC Q6NWY9
Protein Name Pre-mRNA-processing factor 40 homolog B
Gene Name PRPF40B
Organism Homo sapiens (Human).
Sequence Length 871
Subcellular Localization Nucleus speckle .
Protein Description May be involved in pre-mRNA splicing..
Protein Sequence MMPPPFMPPPGIPPPFPPMGLPPMSQRPPAIPPMPPGILPPMLPPMGAPPPLTQIPGMVPPMMPGMLMPAVPVTAATAPGADTASSAVAGTGPPRALWSEHVAPDGRIYYYNADDKQSVWEKPSVLKSKAELLLSQCPWKEYKSDTGKPYYYNNQSKESRWTRPKDLDDLEVLVKQEAAGKQQQQLPQTLQPQPPQPQPDPPPVPPGPTPVPTGLLEPEPGGSEDCDVLEATQPLEQGFLQQLEEGPSSSGQHQPQQEEEESKPEPERSGLSWSNREKAKQAFKELLRDKAVPSNASWEQAMKMVVTDPRYSALPKLSEKKQAFNAYKAQREKEEKEEARLRAKEAKQTLQHFLEQHERMTSTTRYRRAEQTFGELEVWAVVPERDRKEVYDDVLFFLAKKEKEQAKQLRRRNIQALKSILDGMSSVNFQTTWSQAQQYLMDNPSFAQDHQLQNMDKEDALICFEEHIRALEREEEEERERARLRERRQQRKNREAFQTFLDELHETGQLHSMSTWMELYPAVSTDVRFANMLGQPGSTPLDLFKFYVEELKARFHDEKKIIKDILKDRGFCVEVNTAFEDFAHVISFDKRAAALDAGNIKLTFNSLLEKAEAREREREKEEARRMRRREAAFRSMLRQAVPALELGTAWEEVRERFVCDSAFEQITLESERIRLFREFLQVLEQTECQHLHTKGRKHGRKGKKHHHKRSHSPSGSESEEEELPPPSLRPPKRRRRNPSESGSEPSSSLDSVESGGAALGGRGSPSSHLLGADHGLRKAKKPKKKTKKRRHKSNSPESETDPEEKAGKESDEKEQEQDKDRELQQAELPNRSPGFGIKKEKTGWDTSESELSEGELERRRRTLLQQLDDHQ
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
95 (in isoform 4)Phosphorylation-45.5030206219
97 (in isoform 4)Phosphorylation-5.6630206219
98 (in isoform 4)Phosphorylation-10.7330206219
101 (in isoform 4)Phosphorylation-18.6130206219
104 (in isoform 4)Phosphorylation-43.4230206219
105 (in isoform 4)Phosphorylation-49.6330206219
138 (in isoform 4)Phosphorylation-37.2223663014
139 (in isoform 4)Phosphorylation-17.4623663014
141 (in isoform 4)Phosphorylation-55.0923663014
142 (in isoform 2)Acetylation-16.44-
142AcetylationSQCPWKEYKSDTGKP
HCCCCHHCCCCCCCC		16.4419608861
143 (in isoform 4)Phosphorylation-42.8423663014
144 (in isoform 4)Phosphorylation-39.2323663014
148AcetylationEYKSDTGKPYYYNNQ
HCCCCCCCCCCCCCC		31.7519608861
148 (in isoform 4)Phosphorylation-31.7523663014
149 (in isoform 4)Phosphorylation-24.5723663014
150 (in isoform 4)Phosphorylation-23.2823663014
170AcetylationRPKDLDDLEVLVKQE
CCCCHHHHHHHHHHH		4.97-
175SumoylationDDLEVLVKQEAAGKQ
HHHHHHHHHHHCCHH		37.9628112733
316AcetylationPRYSALPKLSEKKQA
CCCCCCCHHHHHHHH		66.5525825284
318PhosphorylationYSALPKLSEKKQAFN
CCCCCHHHHHHHHHH		54.2025332170
338AcetylationREKEEKEEARLRAKE
HHHHHHHHHHHHHHH		50.59-
547PhosphorylationPLDLFKFYVEELKAR
CHHHHHHHHHHHHHH		13.9328331001
563AcetylationHDEKKIIKDILKDRG
CCHHHHHHHHHHHCC		42.0422636967
585AcetylationAFEDFAHVISFDKRA
CCHHHHHHHCCCHHH		3.34-
606PhosphorylationNIKLTFNSLLEKAEA
CEEEEHHHHHHHHHH		30.0924719451
741PhosphorylationRRRNPSESGSEPSSS
CCCCCCCCCCCCCCC		52.5428985074
751 (in isoform 2)Phosphorylation-32.83-
751PhosphorylationEPSSSLDSVESGGAA
CCCCCCCCHHHCCCC		32.8319651622
763 (in isoform 3)Phosphorylation-47.3821406692
764PhosphorylationAALGGRGSPSSHLLG
CCCCCCCCCCHHHCC		21.9029255136
765 (in isoform 3)Phosphorylation-42.5521406692
766PhosphorylationLGGRGSPSSHLLGAD
CCCCCCCCHHHCCCH		31.8930266825
767PhosphorylationGGRGSPSSHLLGADH
CCCCCCCHHHCCCHH		22.8730278072
785PhosphorylationKAKKPKKKTKKRRHK
HCCCCCHHCCCCCCC		72.24-
788PhosphorylationKPKKKTKKRRHKSNS
CCCHHCCCCCCCCCC		60.95-
793PhosphorylationTKKRRHKSNSPESET
CCCCCCCCCCCCCCC		36.0927732954
795PhosphorylationKRRHKSNSPESETDP
CCCCCCCCCCCCCCH		36.8225159151
797 (in isoform 2)Phosphorylation-62.11-
798PhosphorylationHKSNSPESETDPEEK
CCCCCCCCCCCHHHH		49.5327732954
800PhosphorylationSNSPESETDPEEKAG
CCCCCCCCCHHHHCC		67.1627732954
810PhosphorylationEEKAGKESDEKEQEQ
HHHCCCCCHHHHHHH		55.3326657352
816PhosphorylationESDEKEQEQDKDREL
CCHHHHHHHHHHHHH		62.94-
819 (in isoform 2)Phosphorylation-59.38-
821MethylationEQEQDKDRELQQAEL
HHHHHHHHHHHHHHC		52.8718939025
821DimethylationEQEQDKDRELQQAEL
HHHHHHHHHHHHHHC		52.87-
831PhosphorylationQQAELPNRSPGFGIK
HHHHCCCCCCCCCCC		42.14-
831 (in isoform 3)Phosphorylation-42.1421406692
832PhosphorylationQAELPNRSPGFGIKK
HHHCCCCCCCCCCCC		35.6922167270
836 (in isoform 2)Phosphorylation-36.40-
838SumoylationRSPGFGIKKEKTGWD
CCCCCCCCCCCCCCC		56.0828112733
839 (in isoform 2)Phosphorylation-63.62-
842PhosphorylationFGIKKEKTGWDTSES
CCCCCCCCCCCCCHH		44.5922617229
846PhosphorylationKEKTGWDTSESELSE
CCCCCCCCCHHHCCH		28.0825159151
847PhosphorylationEKTGWDTSESELSEG
CCCCCCCCHHHCCHH		36.3325159151
849PhosphorylationTGWDTSESELSEGEL
CCCCCCHHHCCHHHH		43.5430108239
852PhosphorylationDTSESELSEGELERR
CCCHHHCCHHHHHHH		39.2325159151
853PhosphorylationTSESELSEGELERRR
CCHHHCCHHHHHHHH		70.1232645325
868PhosphorylationRTLLQQLDDHQ----
HHHHHHHHCCC----		47.19-
870PhosphorylationLLQQLDDHQ------
HHHHHHCCC------		34.61-
873PhosphorylationQLDDHQ---------
HHHCCC---------		-
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 PR40B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PR40B_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 PR40B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HD_HUMANHTTphysical
9700202
SRRM2_HUMANSRRM2physical
26344197
RGS9_HUMANRGS9physical
28514442
GNB5_HUMANGNB5physical
28514442
RBM25_HUMANRBM25physical
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 PR40B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148 AND LYS-563, AND MASSSPECTROMETRY.
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-832, AND MASSSPECTROMETRY.

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