SLU7_HUMAN - dbPTM
SLU7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLU7_HUMAN
UniProt AC O95391
Protein Name Pre-mRNA-splicing factor SLU7
Gene Name SLU7
Organism Homo sapiens (Human).
Sequence Length 586
Subcellular Localization Nucleus. Cytoplasm. Predominantly nuclear. Shuttling between the nucleus and the cytoplasm is regulated by the CCHC-type zinc finger. Upon UV-C stress stimulus, the nuclear concentration of the protein decreases, affecting alternative splicing. Trans
Protein Description Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation..
Protein Sequence MSATVVDAVNAAPLSGSKEMSLEEPKKMTREDWRKKKELEEQRKLGNAPAEVDEEGKDINPHIPQYISSVPWYIDPSKRPTLKHQRPQPEKQKQFSSSGEWYKRGVKENSIITKYRKGACENCGAMTHKKKDCFERPRRVGAKFTGTNIAPDEHVQPQLMFDYDGKRDRWNGYNPEEHMKIVEEYAKVDLAKRTLKAQKLQEELASGKLVEQANSPKHQWGEEEPNSQMEKDHNSEDEDEDKYADDIDMPGQNFDSKRRITVRNLRIREDIAKYLRNLDPNSAYYDPKTRAMRENPYANAGKNPDEVSYAGDNFVRYTGDTISMAQTQLFAWEAYDKGSEVHLQADPTKLELLYKSFKVKKEDFKEQQKESILEKYGGQEHLDAPPAELLLAQTEDYVEYSRHGTVIKGQERAVACSKYEEDVKIHNHTHIWGSYWKEGRWGYKCCHSFFKYSYCTGEAGKEIVNSEECIINEITGEESVKKPQTLMELHQEKLKEEKKKKKKKKKKHRKSSSDSDDEEKKHEKLKKALNAEEARLLHVKETMQIDERKRPYNSMYETREPTEEEMEAYRMKRQRPDDPMASFLGQ
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
2Acetylation------MSATVVDAV
------CCCEEECHH		32.4219413330
15PhosphorylationAVNAAPLSGSKEMSL
HHHHCCCCCCCCCCC		39.7120068231
17PhosphorylationNAAPLSGSKEMSLEE
HHCCCCCCCCCCCCC		23.2820068231
18UbiquitinationAAPLSGSKEMSLEEP
HCCCCCCCCCCCCCC		62.0524816145
28UbiquitinationSLEEPKKMTREDWRK
CCCCCCCCCHHHHHH		5.5024816145
44SumoylationKELEEQRKLGNAPAE
HHHHHHHHHCCCCCC		61.51-
44SumoylationKELEEQRKLGNAPAE
HHHHHHHHHCCCCCC		61.51-
78UbiquitinationPWYIDPSKRPTLKHQ
CCEECCCCCCCCCCC		68.7229967540
83UbiquitinationPSKRPTLKHQRPQPE
CCCCCCCCCCCCCHH		39.9229967540
93UbiquitinationRPQPEKQKQFSSSGE
CCCHHHHHCCCCCHH		65.4629967540
96PhosphorylationPEKQKQFSSSGEWYK
HHHHHCCCCCHHHHH		22.5428450419
97PhosphorylationEKQKQFSSSGEWYKR
HHHHCCCCCHHHHHH		43.5828450419
98PhosphorylationKQKQFSSSGEWYKRG
HHHCCCCCHHHHHHH		39.2628450419
102PhosphorylationFSSSGEWYKRGVKEN
CCCCHHHHHHHCHHC		6.11-
103UbiquitinationSSSGEWYKRGVKENS
CCCHHHHHHHCHHCC		43.6929967540
107UbiquitinationEWYKRGVKENSIITK
HHHHHHCHHCCHHHH		54.7429967540
110O-linked_GlycosylationKRGVKENSIITKYRK
HHHCHHCCHHHHHHC		19.2330379171
110PhosphorylationKRGVKENSIITKYRK
HHHCHHCCHHHHHHC		19.2319413330
131UbiquitinationGAMTHKKKDCFERPR
CCCCCCCCCCCCCCC		65.61-
143AcetylationRPRRVGAKFTGTNIA
CCCCCCCCCCCCCCC		37.2125953088
163PhosphorylationQPQLMFDYDGKRDRW
CCCEEECCCCCCCCC		18.48-
166UbiquitinationLMFDYDGKRDRWNGY
EEECCCCCCCCCCCC		48.5022505724
176UbiquitinationRWNGYNPEEHMKIVE
CCCCCCHHHHHHHHH		57.8222505724
180UbiquitinationYNPEEHMKIVEEYAK
CCHHHHHHHHHHHHH		45.5723503661
187SumoylationKIVEEYAKVDLAKRT
HHHHHHHHHHHHHHH		35.07-
187UbiquitinationKIVEEYAKVDLAKRT
HHHHHHHHHHHHHHH		35.0723503661
187SumoylationKIVEEYAKVDLAKRT
HHHHHHHHHHHHHHH		35.07-
190UbiquitinationEEYAKVDLAKRTLKA
HHHHHHHHHHHHHHH		7.2923503661
192UbiquitinationYAKVDLAKRTLKAQK
HHHHHHHHHHHHHHH		53.8923503661
197UbiquitinationLAKRTLKAQKLQEEL
HHHHHHHHHHHHHHH		18.1723503661
199SumoylationKRTLKAQKLQEELAS
HHHHHHHHHHHHHHH		57.93-
199SumoylationKRTLKAQKLQEELAS
HHHHHHHHHHHHHHH		57.93-
199UbiquitinationKRTLKAQKLQEELAS
HHHHHHHHHHHHHHH		57.9329967540
199AcetylationKRTLKAQKLQEELAS
HHHHHHHHHHHHHHH		57.9325953088
202UbiquitinationLKAQKLQEELASGKL
HHHHHHHHHHHHCCH		66.4723503661
208UbiquitinationQEELASGKLVEQANS
HHHHHHCCHHHHCCC		47.0329967540
208AcetylationQEELASGKLVEQANS
HHHHHHCCHHHHCCC		47.0326051181
215PhosphorylationKLVEQANSPKHQWGE
CHHHHCCCCCCCCCC		38.0429255136
227PhosphorylationWGEEEPNSQMEKDHN
CCCCCCCCHHCCCCC		41.4420363803
235PhosphorylationQMEKDHNSEDEDEDK
HHCCCCCCCCCCHHH		42.9023927012
243PhosphorylationEDEDEDKYADDIDMP
CCCCHHHHHCCCCCC		27.8223401153
256PhosphorylationMPGQNFDSKRRITVR
CCCCCCCCCCCEEEE		24.7520873877
257UbiquitinationPGQNFDSKRRITVRN
CCCCCCCCCCEEEEE		47.7629967540
257SumoylationPGQNFDSKRRITVRN
CCCCCCCCCCEEEEE		47.76-
257SumoylationPGQNFDSKRRITVRN
CCCCCCCCCCEEEEE		47.76-
261PhosphorylationFDSKRRITVRNLRIR
CCCCCCEEEEEHHHH		16.17-
273UbiquitinationRIREDIAKYLRNLDP
HHHHHHHHHHHCCCC		45.19-
282PhosphorylationLRNLDPNSAYYDPKT
HHCCCCCCCCCCHHH		24.0424719451
284PhosphorylationNLDPNSAYYDPKTRA
CCCCCCCCCCHHHHH		14.2821552520
285PhosphorylationLDPNSAYYDPKTRAM
CCCCCCCCCHHHHHH		26.0324719451
288UbiquitinationNSAYYDPKTRAMREN
CCCCCCHHHHHHHHC		47.9824816145
297PhosphorylationRAMRENPYANAGKNP
HHHHHCCCCCCCCCC		24.8628796482
298UbiquitinationAMRENPYANAGKNPD
HHHHCCCCCCCCCCC		10.7224816145
302UbiquitinationNPYANAGKNPDEVSY
CCCCCCCCCCCCCCC		64.0021906983
302AcetylationNPYANAGKNPDEVSY
CCCCCCCCCCCCCCC		64.0023749302
308PhosphorylationGKNPDEVSYAGDNFV
CCCCCCCCCCCCCCC		13.7628152594
309PhosphorylationKNPDEVSYAGDNFVR
CCCCCCCCCCCCCCE		21.5625627689
312UbiquitinationDEVSYAGDNFVRYTG
CCCCCCCCCCCEECC		36.9021963094
349SumoylationHLQADPTKLELLYKS
EEECCHHHHHHHHHH		45.4028112733
349UbiquitinationHLQADPTKLELLYKS
EEECCHHHHHHHHHH		45.4029967540
354PhosphorylationPTKLELLYKSFKVKK
HHHHHHHHHHHCCCH		19.7428674419
355UbiquitinationTKLELLYKSFKVKKE
HHHHHHHHHHCCCHH		49.7622817900
358UbiquitinationELLYKSFKVKKEDFK
HHHHHHHCCCHHHHH		61.3022817900
360UbiquitinationLYKSFKVKKEDFKEQ
HHHHHCCCHHHHHHH		51.5422817900
365UbiquitinationKVKKEDFKEQQKESI
CCCHHHHHHHHHHHH		67.9221890473
368UbiquitinationKEDFKEQQKESILEK
HHHHHHHHHHHHHHH		53.2022817900
369UbiquitinationEDFKEQQKESILEKY
HHHHHHHHHHHHHHH		53.80-
370UbiquitinationDFKEQQKESILEKYG
HHHHHHHHHHHHHHC		38.3822817900
371PhosphorylationFKEQQKESILEKYGG
HHHHHHHHHHHHHCC		39.2424719451
375UbiquitinationQKESILEKYGGQEHL
HHHHHHHHHCCHHCC		45.8329967540
397PhosphorylationLLAQTEDYVEYSRHG
HHEECCHHHCHHCCC		6.7527642862
400PhosphorylationQTEDYVEYSRHGTVI
ECCHHHCHHCCCCEE		10.8527642862
408UbiquitinationSRHGTVIKGQERAVA
HCCCCEECCCHHHEE		50.6429967540
408SumoylationSRHGTVIKGQERAVA
HCCCCEECCCHHHEE		50.6428112733
418SumoylationERAVACSKYEEDVKI
HHHEECCCCCCCCEE		57.47-
418SumoylationERAVACSKYEEDVKI
HHHEECCCCCCCCEE		57.47-
466PhosphorylationAGKEIVNSEECIINE
CCCEEECCCCCEEEE		24.7127067055
482SumoylationTGEESVKKPQTLMEL
CCHHHCCCCHHHHHH		39.95-
482SumoylationTGEESVKKPQTLMEL
CCHHHCCCCHHHHHH		39.95-
482UbiquitinationTGEESVKKPQTLMEL
CCHHHCCCCHHHHHH		39.9529967540
493UbiquitinationLMELHQEKLKEEKKK
HHHHHHHHHHHHHHH		59.2829967540
511PhosphorylationKKKKHRKSSSDSDDE
HHHHHHCCCCCCCHH		34.7226657352
513PhosphorylationKKHRKSSSDSDDEEK
HHHHCCCCCCCHHHH		48.5026657352
515PhosphorylationHRKSSSDSDDEEKKH
HHCCCCCCCHHHHHH		49.2426657352
526UbiquitinationEKKHEKLKKALNAEE
HHHHHHHHHHHCHHH		47.2522505724
527UbiquitinationKKHEKLKKALNAEEA
HHHHHHHHHHCHHHH		69.4222505724
536UbiquitinationLNAEEARLLHVKETM
HCHHHHHHHHHHHHH		5.1022505724
537UbiquitinationNAEEARLLHVKETMQ
CHHHHHHHHHHHHHC		3.4822505724
540AcetylationEARLLHVKETMQIDE
HHHHHHHHHHHCCCC		36.4012432345
540UbiquitinationEARLLHVKETMQIDE
HHHHHHHHHHHCCCC		36.4029967540
552PhosphorylationIDERKRPYNSMYETR
CCCCCCCCCCCCCCC		24.7329759185
554PhosphorylationERKRPYNSMYETREP
CCCCCCCCCCCCCCC		19.5229759185
556PhosphorylationKRPYNSMYETREPTE
CCCCCCCCCCCCCCH		17.6129759185
582PhosphorylationRPDDPMASFLGQ---
CCCCHHHHHCCC---		18.1021712546
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 SLU7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLU7_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 SLU7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
PPIL3_HUMANPPIL3physical
16189514
TCPE_HUMANCCT5physical
22939629
SF3B2_HUMANSF3B2physical
22365833
PRP8_HUMANPRPF8physical
22365833
PRPF3_HUMANPRPF3physical
22365833
PPIL3_HUMANPPIL3physical
22365833
PPIG_HUMANPPIGphysical
22365833
PCBP2_HUMANPCBP2physical
22365833
BAG2_HUMANBAG2physical
22365833
ZCH10_HUMANZCCHC10physical
22365833
NSD3_HUMANWHSC1L1physical
23455924
KDM1A_HUMANKDM1Aphysical
23455924
JMJD6_HUMANJMJD6physical
23455924
ANM5_HUMANPRMT5physical
23455924
ANM6_HUMANPRMT6physical
23455924
PPIL3_HUMANPPIL3physical
25416956
THAP1_HUMANTHAP1physical
25416956
CEP70_HUMANCEP70physical
25416956
LZTS2_HUMANLZTS2physical
25416956
K1C40_HUMANKRT40physical
25416956
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 SLU7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASSSPECTROMETRY.
"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-215, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-243, AND MASSSPECTROMETRY.

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