ICLN_HUMAN - dbPTM
ICLN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ICLN_HUMAN
UniProt AC P54105
Protein Name Methylosome subunit pICln
Gene Name CLNS1A
Organism Homo sapiens (Human).
Sequence Length 237
Subcellular Localization Cytoplasm, cytosol . Nucleus . Cytoplasm, cytoskeleton . A small fraction is also associated with the cytoskeleton (PubMed:18984161).
Protein Description Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins. [PubMed: 21081503]
Protein Sequence MSFLKSFPPPGPAEGLLRQQPDTEAVLNGKGLGTGTLYIAESRLSWLDGSGLGFSLEYPTISLHALSRDRSDCLGEHLYVMVNAKFEEESKEPVADEEEEDSDDDVEPITEFRFVPSDKSALEAMFTAMCECQALHPDPEDEDSDDYDGEEYDVEAHEQGQGDIPTFYTYEEGLSHLTAEGQATLERLEGMLSQSVSSQYNMAGVRTEDSIRDYEDGMEVDTTPTVAGQFEDADVDH
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------MSFLKSFPP
------CCCHHCCCC		39.0122814378
2Phosphorylation------MSFLKSFPP
------CCCHHCCCC		39.0124719451
5Ubiquitination---MSFLKSFPPPGP
---CCCHHCCCCCCC		48.3021906983
6Phosphorylation--MSFLKSFPPPGPA
--CCCHHCCCCCCCC		45.17-
23PhosphorylationLLRQQPDTEAVLNGK
CCCCCCCCCHHHCCC		32.3122210691
30UbiquitinationTEAVLNGKGLGTGTL
CCHHHCCCCCCCCEE		50.3021890473
34PhosphorylationLNGKGLGTGTLYIAE
HCCCCCCCCEEEEEE		31.8428152594
36PhosphorylationGKGLGTGTLYIAESR
CCCCCCCEEEEEECE		19.0728152594
38PhosphorylationGLGTGTLYIAESRLS
CCCCCEEEEEECEEH		9.6428152594
42PhosphorylationGTLYIAESRLSWLDG
CEEEEEECEEHHCCC		29.5122210691
43MethylationTLYIAESRLSWLDGS
EEEEEECEEHHCCCC		25.01115480105
50PhosphorylationRLSWLDGSGLGFSLE
EEHHCCCCCCCEECC		30.4325159151
90PhosphorylationNAKFEEESKEPVADE
ECEECHHHCCCCCCC		45.6723927012
91UbiquitinationAKFEEESKEPVADEE
CEECHHHCCCCCCCC		70.1221906983
102PhosphorylationADEEEEDSDDDVEPI
CCCCCCCCCCCCCCC		46.3419664994
110PhosphorylationDDDVEPITEFRFVPS
CCCCCCCEEEEECCC		39.5223927012
144PhosphorylationPDPEDEDSDDYDGEE
CCCCCCCCCCCCCCE		30.2724275569
147PhosphorylationEDEDSDDYDGEEYDV
CCCCCCCCCCCEEEH		30.7322817900
152PhosphorylationDDYDGEEYDVEAHEQ
CCCCCCEEEHHHHHC		22.4622817900
168PhosphorylationQGDIPTFYTYEEGLS
CCCCCCEEECHHHHC		15.7622817900
170PhosphorylationDIPTFYTYEEGLSHL
CCCCEEECHHHHCCC		10.7022817900
175PhosphorylationYTYEEGLSHLTAEGQ
EECHHHHCCCCHHHH		27.57-
193PhosphorylationERLEGMLSQSVSSQY
HHHHHHHHHHHHHCC		16.1221945579
195PhosphorylationLEGMLSQSVSSQYNM
HHHHHHHHHHHCCCC		22.1621945579
197PhosphorylationGMLSQSVSSQYNMAG
HHHHHHHHHCCCCCC		19.5721945579
198PhosphorylationMLSQSVSSQYNMAGV
HHHHHHHHCCCCCCC		34.2321945579
200PhosphorylationSQSVSSQYNMAGVRT
HHHHHHCCCCCCCCC		14.6221945579
207PhosphorylationYNMAGVRTEDSIRDY
CCCCCCCCHHHCCCC		41.5621712546
210PhosphorylationAGVRTEDSIRDYEDG
CCCCCHHHCCCCCCC		17.1921712546
212MethylationVRTEDSIRDYEDGME
CCCHHHCCCCCCCCC		44.40115480115
214PhosphorylationTEDSIRDYEDGMEVD
CHHHCCCCCCCCCCC		13.1828674151
222PhosphorylationEDGMEVDTTPTVAGQ
CCCCCCCCCCCCCCC		39.5928796482
223PhosphorylationDGMEVDTTPTVAGQF
CCCCCCCCCCCCCCC		16.7025159151
225PhosphorylationMEVDTTPTVAGQFED
CCCCCCCCCCCCCCC		22.3928796482
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 ICLN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ICLN_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 ICLN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITA2B_HUMANITGA2Bphysical
15075326
ANM5_HUMANPRMT5physical
11713266
RSMB_HUMANSNRPBphysical
11713266
SMD3_HUMANSNRPD3physical
11713266
SMD1_HUMANSNRPD1physical
11713266
SMD2_HUMANSNRPD2physical
11713266
RUXE_HUMANSNRPEphysical
11713266
ANM5_HUMANPRMT5physical
9556550
MEP50_HUMANWDR77physical
11756452
ANM5_HUMANPRMT5physical
11756452
SMD3_HUMANSNRPD3physical
19520849
LSM10_HUMANLSM10physical
16087681
LSM11_HUMANLSM11physical
16087681
RSMB_HUMANSNRPBphysical
18984161
WIPI4_HUMANWDR45physical
18984161
SMD1_HUMANSNRPD1physical
18984161
ANM5_HUMANPRMT5physical
18984161
SMD3_HUMANSNRPD3physical
18984161
SMD2_HUMANSNRPD2physical
18984161
RUXE_HUMANSNRPEphysical
18984161
RUXF_HUMANSNRPFphysical
18984161
RUXG_HUMANSNRPGphysical
18984161
PP4R2_HUMANPPP4R2physical
22939629
LEG1_HUMANLGALS1physical
22939629
LEG3_HUMANLGALS3physical
22939629
PTMS_HUMANPTMSphysical
22939629
RHOA_HUMANRHOAphysical
22939629
OSTF1_HUMANOSTF1physical
22939629
PGAM1_HUMANPGAM1physical
22939629
SC24A_HUMANSEC24Aphysical
22939629
IPYR_HUMANPPA1physical
22939629
PDLI1_HUMANPDLIM1physical
22939629
UFC1_HUMANUFC1physical
22939629
PUR9_HUMANATICphysical
22939629
UBXN1_HUMANUBXN1physical
22939629
PUM1_HUMANPUM1physical
22939629
NEDD8_HUMANNEDD8physical
22939629
TPD54_HUMANTPD52L2physical
22939629
PIR_HUMANPIRphysical
22939629
LPP_HUMANLPPphysical
22939629
RAC1_HUMANRAC1physical
22939629
PLIN3_HUMANPLIN3physical
22939629
NDRG1_HUMANNDRG1physical
22939629
MIF_HUMANMIFphysical
22939629
SC24C_HUMANSEC24Cphysical
22939629
PP2AA_HUMANPPP2CAphysical
22939629
S10A6_HUMANS100A6physical
22939629
SAE2_HUMANUBA2physical
22939629
PDIA6_HUMANPDIA6physical
22939629
PFD3_HUMANVBP1physical
22939629
TRIP6_HUMANTRIP6physical
22939629
PLST_HUMANPLS3physical
22939629
MDHM_HUMANMDH2physical
22939629
SNX12_HUMANSNX12physical
22939629
PSA5_HUMANPSMA5physical
22939629
RL40_HUMANUBA52physical
22939629
UBQL1_HUMANUBQLN1physical
22939629
RD23A_HUMANRAD23Aphysical
22939629
RS21_HUMANRPS21physical
22939629
RSMB_HUMANSNRPBphysical
22365833
SMD1_HUMANSNRPD1physical
22365833
SMD2_HUMANSNRPD2physical
22365833
SMD3_HUMANSNRPD3physical
22365833
RUXF_HUMANSNRPFphysical
22365833
LSM2_HUMANLSM2physical
22365833
LSM3_HUMANLSM3physical
22365833
LSM6_HUMANLSM6physical
22365833
ANM5_HUMANPRMT5physical
22365833
SMD3_HUMANSNRPD3physical
21988832
PYRG1_HUMANCTPS1physical
22863883
GRP78_HUMANHSPA5physical
22863883
PDIA1_HUMANP4HBphysical
22863883
PFD2_HUMANPFDN2physical
22863883
UBP5_HUMANUSP5physical
22863883
41_HUMANEPB41physical
25416956
SMD1_HUMANSNRPD1physical
25416956
SMD2_HUMANSNRPD2physical
25416956
RUXG_HUMANSNRPGphysical
25416956
LSM6_HUMANLSM6physical
25416956
LSM3_HUMANLSM3physical
25416956
LSM2_HUMANLSM2physical
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 ICLN_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-102, AND MASSSPECTROMETRY.
"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-102, 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-102, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND MASSSPECTROMETRY.
"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 SER-102 AND THR-223, ANDMASS SPECTROMETRY.
"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-102, 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 SER-102, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, 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-102, AND MASSSPECTROMETRY.

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