SMU1_HUMAN - dbPTM
SMU1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMU1_HUMAN
UniProt AC Q2TAY7
Protein Name WD40 repeat-containing protein SMU1
Gene Name SMU1
Organism Homo sapiens (Human).
Sequence Length 513
Subcellular Localization Cytoplasm . Nucleus . Nucleus speckle . Colocalizes with SRSF1 in nuclear speckles.
Protein Description Auxiliary spliceosomal protein that regulates selection of alternative splice sites in a small set of target pre-mRNA species (Probable). Regulates alternative splicing of the HSPG2 pre-mRNA (By similarity). Required for normal mitotic spindle assembly and normal progress through mitosis. [PubMed: 15878348 Required for normal accumulation of IK]
Protein Sequence MSIEIESSDVIRLIMQYLKENSLHRALATLQEETTVSLNTVDSIESFVADINSGHWDTVLQAIQSLKLPDKTLIDLYEQVVLELIELRELGAARSLLRQTDPMIMLKQTQPERYIHLENLLARSYFDPREAYPDGSSKEKRRAAIAQALAGEVSVVPPSRLMALLGQALKWQQHQGLLPPGMTIDLFRGKAAVKDVEEEKFPTQLSRHIKFGQKSHVECARFSPDGQYLVTGSVDGFIEVWNFTTGKIRKDLKYQAQDNFMMMDDAVLCMCFSRDTEMLATGAQDGKIKVWKIQSGQCLRRFERAHSKGVTCLSFSKDSSQILSASFDQTIRIHGLKSGKTLKEFRGHSSFVNEATFTQDGHYIISASSDGTVKIWNMKTTECSNTFKSLGSTAGTDITVNSVILLPKNPEHFVVCNRSNTVVIMNMQGQIVRSFSSGKREGGDFVCCALSPRGEWIYCVGEDFVLYCFSTVTGKLERTLTVHEKDVIGIAHHPHQNLIATYSEDGLLKLWKP
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
1Acetylation-------MSIEIESS
-------CCCEECHH		9.1022814378
2Phosphorylation------MSIEIESSD
------CCCEECHHH		29.0029507054
2Acetylation------MSIEIESSD
------CCCEECHHH		29.0019413330
17PhosphorylationVIRLIMQYLKENSLH
HHHHHHHHHHHCCHH		11.4521406692
19UbiquitinationRLIMQYLKENSLHRA
HHHHHHHHHCCHHHH		50.3321890473
19UbiquitinationRLIMQYLKENSLHRA
HHHHHHHHHCCHHHH		50.3321890473
22PhosphorylationMQYLKENSLHRALAT
HHHHHHCCHHHHHHH		27.0124719451
33UbiquitinationALATLQEETTVSLNT
HHHHHHHCCEEEECC		36.50-
39UbiquitinationEETTVSLNTVDSIES
HCCEEEECCHHHHHH		30.46-
49AcetylationDSIESFVADINSGHW
HHHHHHHHCCCCCCH		15.23-
53UbiquitinationSFVADINSGHWDTVL
HHHHCCCCCCHHHHH		32.16-
107UbiquitinationTDPMIMLKQTQPERY
CCCCEEEECCCHHHE		33.6421890473
107AcetylationTDPMIMLKQTQPERY
CCCCEEEECCCHHHE		33.6426051181
114PhosphorylationKQTQPERYIHLENLL
ECCCHHHEEEHHHHH		7.3428152594
123MethylationHLENLLARSYFDPRE
EHHHHHHHCCCCHHH		31.68115917325
126UbiquitinationNLLARSYFDPREAYP
HHHHHCCCCHHHHCC		12.59-
128UbiquitinationLARSYFDPREAYPDG
HHHCCCCHHHHCCCC		26.55-
131UbiquitinationSYFDPREAYPDGSSK
CCCCHHHHCCCCCCH		23.57-
132PhosphorylationYFDPREAYPDGSSKE
CCCHHHHCCCCCCHH		9.3425367160
136PhosphorylationREAYPDGSSKEKRRA
HHHCCCCCCHHHHHH		45.6925367160
137PhosphorylationEAYPDGSSKEKRRAA
HHCCCCCCHHHHHHH		50.8125367160
138UbiquitinationAYPDGSSKEKRRAAI
HCCCCCCHHHHHHHH		69.79-
159PhosphorylationEVSVVPPSRLMALLG
CCCCCCHHHHHHHHH		31.79-
182UbiquitinationQGLLPPGMTIDLFRG
CCCCCCCCEEEEECC		3.51-
194AcetylationFRGKAAVKDVEEEKF
ECCCCCCCCHHHHCC		51.8626051181
194UbiquitinationFRGKAAVKDVEEEKF
ECCCCCCCCHHHHCC		51.8621890473
200UbiquitinationVKDVEEEKFPTQLSR
CCCHHHHCCCHHHHH		60.9821890473
200UbiquitinationVKDVEEEKFPTQLSR
CCCHHHHCCCHHHHH		60.9821890473
200AcetylationVKDVEEEKFPTQLSR
CCCHHHHCCCHHHHH		60.9826051181
210UbiquitinationTQLSRHIKFGQKSHV
HHHHHHHCCCCCCCE		37.00-
210AcetylationTQLSRHIKFGQKSHV
HHHHHHHCCCCCCCE		37.0023749302
2102-HydroxyisobutyrylationTQLSRHIKFGQKSHV
HHHHHHHCCCCCCCE		37.00-
214UbiquitinationRHIKFGQKSHVECAR
HHHCCCCCCCEEEEE		42.80-
214AcetylationRHIKFGQKSHVECAR
HHHCCCCCCCEEEEE		42.8025953088
215PhosphorylationHIKFGQKSHVECARF
HHCCCCCCCEEEEEE		25.5220068231
218UbiquitinationFGQKSHVECARFSPD
CCCCCCEEEEEECCC		19.62-
223PhosphorylationHVECARFSPDGQYLV
CEEEEEECCCCCEEE		19.2720068231
228PhosphorylationRFSPDGQYLVTGSVD
EECCCCCEEEEEECC		14.5220068231
231PhosphorylationPDGQYLVTGSVDGFI
CCCCEEEEEECCCEE		22.5720068231
233PhosphorylationGQYLVTGSVDGFIEV
CCEEEEEECCCEEEE		13.9920068231
244PhosphorylationFIEVWNFTTGKIRKD
EEEEEEECCCCCCCC		31.2720068231
245PhosphorylationIEVWNFTTGKIRKDL
EEEEEECCCCCCCCC		32.1320068231
278SulfoxidationCFSRDTEMLATGAQD
HHCCCHHHHHCCCCC		3.1521406390
287AcetylationATGAQDGKIKVWKIQ
HCCCCCCCEEEEEEC		47.8726051181
287UbiquitinationATGAQDGKIKVWKIQ
HCCCCCCCEEEEEEC		47.8721890473
289UbiquitinationGAQDGKIKVWKIQSG
CCCCCCEEEEEECCC		45.59-
292UbiquitinationDGKIKVWKIQSGQCL
CCCEEEEEECCCHHH		33.58-
292AcetylationDGKIKVWKIQSGQCL
CCCEEEEEECCCHHH		33.5825953088
307PhosphorylationRRFERAHSKGVTCLS
HHHHHHHHCCCEEEE		30.0729214152
308UbiquitinationRFERAHSKGVTCLSF
HHHHHHHCCCEEEEE		47.75-
311PhosphorylationRAHSKGVTCLSFSKD
HHHHCCCEEEEECCC		19.1920068231
314PhosphorylationSKGVTCLSFSKDSSQ
HCCCEEEEECCCHHH		29.6224719451
316PhosphorylationGVTCLSFSKDSSQIL
CCEEEEECCCHHHHH		31.9820068231
324PhosphorylationKDSSQILSASFDQTI
CCHHHHHHEECCCEE		24.40-
337AcetylationTIRIHGLKSGKTLKE
EEEECCCCCCCCHHH		62.8525953088
337UbiquitinationTIRIHGLKSGKTLKE
EEEECCCCCCCCHHH		62.85-
343UbiquitinationLKSGKTLKEFRGHSS
CCCCCCHHHHCCCCC		61.10-
379UbiquitinationTVKIWNMKTTECSNT
CEEEEECCCCCCCCC		49.4321890473
379UbiquitinationTVKIWNMKTTECSNT
CEEEEECCCCCCCCC		49.4321890473
379AcetylationTVKIWNMKTTECSNT
CEEEEECCCCCCCCC		49.4325953088
379SumoylationTVKIWNMKTTECSNT
CEEEEECCCCCCCCC		49.4328112733
389PhosphorylationECSNTFKSLGSTAGT
CCCCCHHHCCCCCCC		33.5029255136
392PhosphorylationNTFKSLGSTAGTDIT
CCHHHCCCCCCCCEE		22.0029255136
393PhosphorylationTFKSLGSTAGTDITV
CHHHCCCCCCCCEEE		27.5829255136
396PhosphorylationSLGSTAGTDITVNSV
HCCCCCCCCEEECEE		23.0529255136
399PhosphorylationSTAGTDITVNSVILL
CCCCCCEEECEEEEC		19.2229255136
402PhosphorylationGTDITVNSVILLPKN
CCCEEECEEEECCCC		13.2429255136
434PhosphorylationMQGQIVRSFSSGKRE
CCCCEEEECCCCCCC		20.70-
436PhosphorylationGQIVRSFSSGKREGG
CCEEEECCCCCCCCC		39.1524719451
451PhosphorylationDFVCCALSPRGEWIY
CEEEEEECCCCCEEE		8.2724719451
485AcetylationRTLTVHEKDVIGIAH
EEEEEEHHCEEEECC		42.2826051181
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 SMU1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMU1_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 SMU1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VTNC_HUMANVTNphysical
22939629
ZCH18_HUMANZC3H18physical
22939629
TFPI1_HUMANTFPIphysical
22939629
TPBG_HUMANTPBGphysical
22939629
YBOX1_HUMANYBX1physical
22365833
LSM4_HUMANLSM4physical
22365833
LSM8_HUMANLSM8physical
22365833
MFAP1_HUMANMFAP1physical
22365833
RED_HUMANIKphysical
22365833
CD2B2_HUMANCD2BP2physical
22365833
MR1L1_HUMANMRFAP1L1physical
25416956
RED_HUMANIKphysical
26186194
F172A_HUMANFAM172Aphysical
26344197
RED_HUMANIKphysical
26344197
RED_HUMANIKphysical
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 SMU1_HUMAN

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Related Literatures of Post-Translational Modification

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