CWC27_HUMAN - dbPTM
CWC27_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CWC27_HUMAN
UniProt AC Q6UX04
Protein Name Spliceosome-associated protein CWC27 homolog {ECO:0000305}
Gene Name CWC27 {ECO:0000312|HGNC:HGNC:10664}
Organism Homo sapiens (Human).
Sequence Length 472
Subcellular Localization Nucleus .
Protein Description As part of the spliceosome, plays a role in pre-mRNA splicing. [PubMed: 29360106 Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity]
Protein Sequence MSNIYIQEPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVLFNPFDDIIPREIKRLKKEKPEEEVKKLKPKGTKNFSLLSFGEEAEEEEEEVNRVSQSMKGKSKSSHDLLKDDPHLSSVPVVESEKGDAPDLVDDGEDESAEHDEYIDGDEKNLMRERIAKKLKKDTSANVKSAGEGEVEKKSVSRSEELRKEARQLKRELLAAKQKKVENAAKQAEKRSEEEEAPPDGAVAEYRREKQKYEALRKQQSKKGTSREDQTLALLNQFKSKLTQAIAETPENDIPETEVEDDEGWMSHVLQFEDKSRKVKDASMQDSDTFEIYDPRNPVNKRRREESKKLMREKKERR
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------MSNIYIQEP
------CCCEEEECC		31.7524043423
2Acetylation------MSNIYIQEP
------CCCEEEECC		31.7519413330
5Phosphorylation---MSNIYIQEPPTN
---CCCEEEECCCCC		10.7824043423
11PhosphorylationIYIQEPPTNGKVLLK
EEEECCCCCCCEEEE		68.2824043423
31UbiquitinationIDIELWSKEAPKACR
CEEEEECCCHHHHHH		46.44-
109N-linked_GlycosylationANAGSHDNGSQFFFT
EECCCCCCCCCEEEE		46.74UniProtKB CARBOHYD
119DimethylationQFFFTLGRADELNNK
CEEEECCCHHHHCCC		41.81-
119MethylationQFFFTLGRADELNNK
CEEEECCCHHHHCCC		41.81115390679
128PhosphorylationDELNNKHTIFGKVTG
HHHCCCCEEEEEECC		21.4424719451
137PhosphorylationFGKVTGDTVYNMLRL
EEEECCHHHHHHHHH		26.6628442448
139PhosphorylationKVTGDTVYNMLRLSE
EECCHHHHHHHHHHC		9.2828064214
145PhosphorylationVYNMLRLSEVDIDDD
HHHHHHHHCCCCCCC		29.1920873877
160UbiquitinationERPHNPHKIKSCEVL
CCCCCCCCCCEEEEE		53.76-
162UbiquitinationPHNPHKIKSCEVLFN
CCCCCCCCEEEEECC		54.58-
164GlutathionylationNPHKIKSCEVLFNPF
CCCCCCEEEEECCCH		3.4022555962
192UbiquitinationEKPEEEVKKLKPKGT
CCCHHHHHHHCCCCC		56.52-
193UbiquitinationKPEEEVKKLKPKGTK
CCHHHHHHHCCCCCC		67.90-
200AcetylationKLKPKGTKNFSLLSF
HHCCCCCCCEEEECC		65.7426051181
201N-linked_GlycosylationLKPKGTKNFSLLSFG
HCCCCCCCEEEECCC		31.4216335952
203PhosphorylationPKGTKNFSLLSFGEE
CCCCCCEEEECCCHH		37.4822199227
206PhosphorylationTKNFSLLSFGEEAEE
CCCEEEECCCHHHHH		36.1821712546
222PhosphorylationEEEVNRVSQSMKGKS
HHHHHHHHHHHCCCC		17.1926434776
224PhosphorylationEVNRVSQSMKGKSKS
HHHHHHHHHCCCCCC		18.2426434776
229PhosphorylationSQSMKGKSKSSHDLL
HHHHCCCCCCHHHHH		46.5723186163
231PhosphorylationSMKGKSKSSHDLLKD
HHCCCCCCHHHHHCC		39.7430576142
232PhosphorylationMKGKSKSSHDLLKDD
HCCCCCCHHHHHCCC		25.4223312004
237SumoylationKSSHDLLKDDPHLSS
CCHHHHHCCCCCCCC		68.34-
237SumoylationKSSHDLLKDDPHLSS
CCHHHHHCCCCCCCC		68.34-
243PhosphorylationLKDDPHLSSVPVVES
HCCCCCCCCCCEEEC		26.6729978859
244PhosphorylationKDDPHLSSVPVVESE
CCCCCCCCCCEEECC		36.4829978859
250PhosphorylationSSVPVVESEKGDAPD
CCCCEEECCCCCCCC		32.7629978859
266PhosphorylationVDDGEDESAEHDEYI
CCCCCCCCHHCCCCC		51.8130576142
272PhosphorylationESAEHDEYIDGDEKN
CCHHCCCCCCCCHHH		15.4628796482
293PhosphorylationAKKLKKDTSANVKSA
HHHHHCCCCCCCCCC		38.3217924679
294PhosphorylationKKLKKDTSANVKSAG
HHHHCCCCCCCCCCC		28.1617924679
299PhosphorylationDTSANVKSAGEGEVE
CCCCCCCCCCCCCCC		36.9028985074
309PhosphorylationEGEVEKKSVSRSEEL
CCCCCCCCCCCHHHH		36.07-
313PhosphorylationEKKSVSRSEELRKEA
CCCCCCCHHHHHHHH		28.1025159151
331AcetylationKRELLAAKQKKVENA
HHHHHHHHHHHHHHH		57.9825953088
346PhosphorylationAKQAEKRSEEEEAPP
HHHHHHHHHHCCCCC		61.5028985074
372MethylationQKYEALRKQQSKKGT
HHHHHHHHHHHCCCC		54.24116252985
379PhosphorylationKQQSKKGTSREDQTL
HHHHCCCCCHHHHHH		33.2318785766
385PhosphorylationGTSREDQTLALLNQF
CCCHHHHHHHHHHHH		26.73-
393UbiquitinationLALLNQFKSKLTQAI
HHHHHHHHHHHHHHH		36.60-
411PhosphorylationPENDIPETEVEDDEG
CCCCCCCCEEECCCC		39.72-
437PhosphorylationSRKVKDASMQDSDTF
CCCCCCCCCCCCCCE		27.4027134283
441PhosphorylationKDASMQDSDTFEIYD
CCCCCCCCCCEEECC		22.9729083192
443PhosphorylationASMQDSDTFEIYDPR
CCCCCCCCEEECCCC		27.4129083192
447PhosphorylationDSDTFEIYDPRNPVN
CCCCEEECCCCCCCH		16.8229083192
462AcetylationKRRREESKKLMREKK
HHHHHHHHHHHHHHH		53.887222187
468AcetylationSKKLMREKKERR---
HHHHHHHHHHHC---		49.967261971
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 CWC27_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CWC27_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 CWC27_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNW1_HUMANSNW1physical
22939629
SK2L2_HUMANSKIV2L2physical
22939629
XRCC4_HUMANXRCC4physical
22939629
SI1L1_HUMANSIPA1L1physical
22939629
F10C1_HUMANFRA10AC1physical
22365833
HMGA1_HUMANHMGA1physical
18850631
LSM2_HUMANLSM2physical
26344197
LSM6_HUMANLSM6physical
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 CWC27_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-293 AND SER-294, ANDMASS SPECTROMETRY.

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