CLPT1_HUMAN - dbPTM
CLPT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLPT1_HUMAN
UniProt AC O96005
Protein Name Cleft lip and palate transmembrane protein 1
Gene Name CLPTM1
Organism Homo sapiens (Human).
Sequence Length 669
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description May play a role in T-cell development..
Protein Sequence MAAAQEADGARSAVVAAGGGSSGQVTSNGSIGRDPPAETQPQNPPAQPAPNAWQVIKGVLFRIFIIWAISSWFRRGPAPQDQAGPGGAPRVASRNLFPKDTLMNLHVYISEHEHFTDFNATSALFWEQHDLVYGDWTSGENSDGCYEHFAELDIPQSVQQNGSIYIHVYFTKSGFHPDPRQKALYRRLATVHMSRMINKYKRRRFQKTKNLLTGETEADPEMIKRAEDYGPVEVISHWHPNITINIVDDHTPWVKGSVPPPLDQYVKFDAVSGDYYPIIYFNDYWNLQKDYYPINESLASLPLRVSFCPLSLWRWQLYAAQSTKSPWNFLGDELYEQSDEEQDSVKVALLETNPYLLALTIIVSIVHSVFEFLAFKNDIQFWNSRQSLEGLSVRSVFFGVFQSFVVLLYILDNETNFVVQVSVFIGVLIDLWKITKVMDVRLDREHRVAGIFPRLSFKDKSTYIESSTKVYDDMAFRYLSWILFPLLGCYAVYSLLYLEHKGWYSWVLSMLYGFLLTFGFITMTPQLFINYKLKSVAHLPWRMLTYKALNTFIDDLFAFVIKMPVMYRIGCLRDDVVFFIYLYQRWIYRVDPTRVNEFGMSGEDPTAAAPVAEVPTAAGALTPTPAPTTTTATREEASTSLPTKPTQGASSASEPQEAPPKPAEDKKKD
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------MAAAQEADG
------CCHHHHCCC		16.1122814378
21PhosphorylationVVAAGGGSSGQVTSN
EEECCCCCCCCCCCC		34.2729978859
22PhosphorylationVAAGGGSSGQVTSNG
EECCCCCCCCCCCCC		36.2029978859
26PhosphorylationGGSSGQVTSNGSIGR
CCCCCCCCCCCCCCC		14.4829978859
27PhosphorylationGSSGQVTSNGSIGRD
CCCCCCCCCCCCCCC		40.0929978859
28N-linked_GlycosylationSSGQVTSNGSIGRDP
CCCCCCCCCCCCCCC		38.57UniProtKB CARBOHYD
30PhosphorylationGQVTSNGSIGRDPPA
CCCCCCCCCCCCCCC		26.5629978859
107UbiquitinationDTLMNLHVYISEHEH
HCEEEEEEEEECCCC		5.24-
119N-linked_GlycosylationHEHFTDFNATSALFW
CCCCCCCCHHHHHHH		45.15UniProtKB CARBOHYD
122UbiquitinationFTDFNATSALFWEQH
CCCCCHHHHHHHCCC		22.14-
161N-linked_GlycosylationIPQSVQQNGSIYIHV
CCHHHHHCCEEEEEE		29.14UniProtKB CARBOHYD
200PhosphorylationMSRMINKYKRRRFQK
HHHHHHHHHHHHHHH		12.7720860994
209UbiquitinationRRRFQKTKNLLTGET
HHHHHHHCCCCCCCC		53.2721890473
209 (in isoform 1)Ubiquitination-53.2721890473
209UbiquitinationRRRFQKTKNLLTGET
HHHHHHHCCCCCCCC		53.2721890473
209UbiquitinationRRRFQKTKNLLTGET
HHHHHHHCCCCCCCC		53.2721890473
209UbiquitinationRRRFQKTKNLLTGET
HHHHHHHCCCCCCCC		53.2721890473
209UbiquitinationRRRFQKTKNLLTGET
HHHHHHHCCCCCCCC		53.2721890473
213PhosphorylationQKTKNLLTGETEADP
HHHCCCCCCCCCCCH		35.8219060867
216PhosphorylationKNLLTGETEADPEMI
CCCCCCCCCCCHHHH		37.5119060867
222SulfoxidationETEADPEMIKRAEDY
CCCCCHHHHHHHHHH		5.5021406390
222UbiquitinationETEADPEMIKRAEDY
CCCCCHHHHHHHHHH		5.50-
224UbiquitinationEADPEMIKRAEDYGP
CCCHHHHHHHHHHCC		44.2221890473
224UbiquitinationEADPEMIKRAEDYGP
CCCHHHHHHHHHHCC		44.2221890473
2242-HydroxyisobutyrylationEADPEMIKRAEDYGP
CCCHHHHHHHHHHCC		44.22-
224UbiquitinationEADPEMIKRAEDYGP
CCCHHHHHHHHHHCC		44.2221890473
224UbiquitinationEADPEMIKRAEDYGP
CCCHHHHHHHHHHCC		44.2221890473
224UbiquitinationEADPEMIKRAEDYGP
CCCHHHHHHHHHHCC		44.2221890473
224 (in isoform 1)Ubiquitination-44.2221890473
241N-linked_GlycosylationVISHWHPNITINIVD
EEEECCCCEEEEEEC		31.02UniProtKB CARBOHYD
267UbiquitinationPPLDQYVKFDAVSGD
CCHHHCEEEEECCCC		32.37-
275PhosphorylationFDAVSGDYYPIIYFN
EEECCCCEEEEEEEE		18.05-
280PhosphorylationGDYYPIIYFNDYWNL
CCEEEEEEEECCCCC		9.32-
284PhosphorylationPIIYFNDYWNLQKDY
EEEEEECCCCCCCCC		9.41-
295N-linked_GlycosylationQKDYYPINESLASLP
CCCCCCCCHHHHCCC		28.4416263699
300PhosphorylationPINESLASLPLRVSF
CCCHHHHCCCCCEEE		35.4924719451
306PhosphorylationASLPLRVSFCPLSLW
HCCCCCEEECCHHHH		18.07-
311PhosphorylationRVSFCPLSLWRWQLY
CEEECCHHHHHHHHH		15.8424719451
324 (in isoform 1)Ubiquitination-60.8221890473
324UbiquitinationLYAAQSTKSPWNFLG
HHHHHCCCCCCHHHC		60.8221906983
334UbiquitinationWNFLGDELYEQSDEE
CHHHCHHHHHCCHHH		7.30-
338PhosphorylationGDELYEQSDEEQDSV
CHHHHHCCHHHCCCH		34.74-
356UbiquitinationLLETNPYLLALTIIV
HHHCCHHHHHHHHHH		2.08-
358UbiquitinationETNPYLLALTIIVSI
HCCHHHHHHHHHHHH		10.48-
392PhosphorylationRQSLEGLSVRSVFFG
CHHHCCCCHHHHHHH		26.7524719451
413N-linked_GlycosylationVLLYILDNETNFVVQ
HHHHHHCCCCCEEEE		55.32UniProtKB CARBOHYD
432UbiquitinationIGVLIDLWKITKVMD
HHHHHHHHHHCEECC		6.05-
436 (in isoform 1)Ubiquitination-38.7521890473
436UbiquitinationIDLWKITKVMDVRLD
HHHHHHCEECCCCCC		38.7521906983
456PhosphorylationAGIFPRLSFKDKSTY
CCEECCCCCCCCCCE		31.3724719451
458UbiquitinationIFPRLSFKDKSTYIE
EECCCCCCCCCCEEE		61.9521906983
458 (in isoform 1)Ubiquitination-61.9521890473
460 (in isoform 1)Ubiquitination-45.3321890473
460UbiquitinationPRLSFKDKSTYIESS
CCCCCCCCCCEEECC		45.3321890473
460UbiquitinationPRLSFKDKSTYIESS
CCCCCCCCCCEEECC		45.3321890473
460UbiquitinationPRLSFKDKSTYIESS
CCCCCCCCCCEEECC		45.3321890473
460UbiquitinationPRLSFKDKSTYIESS
CCCCCCCCCCEEECC		45.3321890473
460UbiquitinationPRLSFKDKSTYIESS
CCCCCCCCCCEEECC		45.3321890473
463PhosphorylationSFKDKSTYIESSTKV
CCCCCCCEEECCCCC		15.1327642862
5342-HydroxyisobutyrylationLFINYKLKSVAHLPW
HHHCCCCCCCCCCCH		38.44-
534UbiquitinationLFINYKLKSVAHLPW
HHHCCCCCCCCCCCH		38.4421890473
534UbiquitinationLFINYKLKSVAHLPW
HHHCCCCCCCCCCCH		38.4421890473
534UbiquitinationLFINYKLKSVAHLPW
HHHCCCCCCCCCCCH		38.4421890473
534UbiquitinationLFINYKLKSVAHLPW
HHHCCCCCCCCCCCH		38.4421890473
534 (in isoform 1)Ubiquitination-38.4421890473
534UbiquitinationLFINYKLKSVAHLPW
HHHCCCCCCCCCCCH		38.4421890473
542UbiquitinationSVAHLPWRMLTYKAL
CCCCCCHHHHHHHHH		14.32-
601PhosphorylationRVNEFGMSGEDPTAA
CCCCCCCCCCCCCCC		39.1329255136
606PhosphorylationGMSGEDPTAAAPVAE
CCCCCCCCCCCCCCC		41.0529255136
616PhosphorylationAPVAEVPTAAGALTP
CCCCCCCCCCCCCCC		34.0229255136
622PhosphorylationPTAAGALTPTPAPTT
CCCCCCCCCCCCCCC		25.2829255136
624PhosphorylationAAGALTPTPAPTTTT
CCCCCCCCCCCCCCC		27.1829255136
628PhosphorylationLTPTPAPTTTTATRE
CCCCCCCCCCCCCHH		38.5929255136
629PhosphorylationTPTPAPTTTTATREE
CCCCCCCCCCCCHHH		22.5329255136
630PhosphorylationPTPAPTTTTATREEA
CCCCCCCCCCCHHHH		19.5329255136
631PhosphorylationTPAPTTTTATREEAS
CCCCCCCCCCHHHHH		24.7627690223
633PhosphorylationAPTTTTATREEASTS
CCCCCCCCHHHHHCC		36.2027690223
638PhosphorylationTATREEASTSLPTKP
CCCHHHHHCCCCCCC		23.0821406692
639PhosphorylationATREEASTSLPTKPT
CCHHHHHCCCCCCCC		41.1321406692
640PhosphorylationTREEASTSLPTKPTQ
CHHHHHCCCCCCCCC		29.8321406692
643PhosphorylationEASTSLPTKPTQGAS
HHHCCCCCCCCCCCC		55.7521406692
644UbiquitinationASTSLPTKPTQGASS
HHCCCCCCCCCCCCC		44.092190698
644 (in isoform 1)Ubiquitination-44.0921890473
646PhosphorylationTSLPTKPTQGASSAS
CCCCCCCCCCCCCCC		40.9921406692
650PhosphorylationTKPTQGASSASEPQE
CCCCCCCCCCCCCCC		33.0121406692
651PhosphorylationKPTQGASSASEPQEA
CCCCCCCCCCCCCCC		34.9721406692
653PhosphorylationTQGASSASEPQEAPP
CCCCCCCCCCCCCCC		52.3221406692
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 CLPT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLPT1_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 CLPT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ICT1_HUMANICT1physical
22939629
TECT2_HUMANTCTN2physical
27173435
LMAN1_HUMANLMAN1physical
27173435
STT3B_HUMANSTT3Bphysical
27173435
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 CLPT1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-295, AND MASSSPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-295, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-213 AND THR-216, ANDMASS SPECTROMETRY.

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