CTSL2_HUMAN - dbPTM
CTSL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTSL2_HUMAN
UniProt AC Q05D32
Protein Name CTD small phosphatase-like protein 2
Gene Name CTDSPL2
Organism Homo sapiens (Human).
Sequence Length 466
Subcellular Localization
Protein Description Probable phosphatase..
Protein Sequence MRLRTRKASQQSNQIQTQRTARAKRKYSEVDDSLPSGGEKPSKNETGLLSSIKKFIKGSTPKEERENPSKRSRIERDIDNNLITSTPRAGEKPNKQISRVRRKSQVNGEAGSYEMTNQHVKQNGKLEDNPSSGSPPRTTLLGTIFSPVFNFFSPANKNGTSGSDSPGQAVEAEEIVKQLDMEQVDEITTSTTTSTNGAAYSNQAVQVRPSLNNGLEEAEETVNRDIPPLTAPVTPDSGYSSAHAEATYEEDWEVFDPYYFIKHVPPLTEEQLNRKPALPLKTRSTPEFSLVLDLDETLVHCSLNELEDAALTFPVLFQDVIYQVYVRLRPFFREFLERMSQMYEIILFTASKKVYADKLLNILDPKKQLVRHRLFREHCVCVQGNYIKDLNILGRDLSKTIIIDNSPQAFAYQLSNGIPIESWFMDKNDNELLKLIPFLEKLVELNEDVRPHIRDRFRLHDLLPPD
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
5Phosphorylation---MRLRTRKASQQS
---CCCCHHHHHHHH		40.9127282143
9PhosphorylationRLRTRKASQQSNQIQ
CCCHHHHHHHHHHHH		31.6123401153
12PhosphorylationTRKASQQSNQIQTQR
HHHHHHHHHHHHHHH		24.0628450419
17PhosphorylationQQSNQIQTQRTARAK
HHHHHHHHHHHHHHH		22.9620873877
26AcetylationRTARAKRKYSEVDDS
HHHHHHHHHHCCCCC		53.0419608861
26MethylationRTARAKRKYSEVDDS
HHHHHHHHHHCCCCC		53.0419608861
27PhosphorylationTARAKRKYSEVDDSL
HHHHHHHHHCCCCCC		17.6923927012
28PhosphorylationARAKRKYSEVDDSLP
HHHHHHHHCCCCCCC		33.8929255136
33PhosphorylationKYSEVDDSLPSGGEK
HHHCCCCCCCCCCCC		37.4025159151
36PhosphorylationEVDDSLPSGGEKPSK
CCCCCCCCCCCCCCC		65.8023927012
40AcetylationSLPSGGEKPSKNETG
CCCCCCCCCCCCCCC		58.8425953088
40UbiquitinationSLPSGGEKPSKNETG
CCCCCCCCCCCCCCC		58.84-
42PhosphorylationPSGGEKPSKNETGLL
CCCCCCCCCCCCCHH		60.2120068231
43SumoylationSGGEKPSKNETGLLS
CCCCCCCCCCCCHHH		68.29-
43SumoylationSGGEKPSKNETGLLS
CCCCCCCCCCCCHHH		68.29-
43AcetylationSGGEKPSKNETGLLS
CCCCCCCCCCCCHHH		68.297681833
46PhosphorylationEKPSKNETGLLSSIK
CCCCCCCCCHHHHHH		42.3920068231
50PhosphorylationKNETGLLSSIKKFIK
CCCCCHHHHHHHHHC		34.7523401153
51PhosphorylationNETGLLSSIKKFIKG
CCCCHHHHHHHHHCC		38.0923401153
53AcetylationTGLLSSIKKFIKGST
CCHHHHHHHHHCCCC		43.5125953088
53UbiquitinationTGLLSSIKKFIKGST
CCHHHHHHHHHCCCC		43.51-
57AcetylationSSIKKFIKGSTPKEE
HHHHHHHCCCCCHHH		50.3619608861
59PhosphorylationIKKFIKGSTPKEERE
HHHHHCCCCCHHHHC		36.2130576142
60PhosphorylationKKFIKGSTPKEEREN
HHHHCCCCCHHHHCC		47.2330576142
69PhosphorylationKEERENPSKRSRIER
HHHHCCHHHHCHHHH		52.8929396449
84PhosphorylationDIDNNLITSTPRAGE
HCCCCCCCCCCCCCC		29.7030266825
85PhosphorylationIDNNLITSTPRAGEK
CCCCCCCCCCCCCCC		29.4430266825
86PhosphorylationDNNLITSTPRAGEKP
CCCCCCCCCCCCCCC		14.2429255136
95UbiquitinationRAGEKPNKQISRVRR
CCCCCCCHHHHHHHH		58.50-
104PhosphorylationISRVRRKSQVNGEAG
HHHHHHHHHHCCCCC		37.2329255136
112PhosphorylationQVNGEAGSYEMTNQH
HHCCCCCCHHHCHHH		25.6029255136
113PhosphorylationVNGEAGSYEMTNQHV
HCCCCCCHHHCHHHH		14.5929255136
116PhosphorylationEAGSYEMTNQHVKQN
CCCCHHHCHHHHHHC		21.5623403867
125AcetylationQHVKQNGKLEDNPSS
HHHHHCCCCCCCCCC		57.1425953088
125UbiquitinationQHVKQNGKLEDNPSS
HHHHHCCCCCCCCCC		57.14-
131PhosphorylationGKLEDNPSSGSPPRT
CCCCCCCCCCCCCCC		54.2930266825
132PhosphorylationKLEDNPSSGSPPRTT
CCCCCCCCCCCCCCE		44.5430266825
134PhosphorylationEDNPSSGSPPRTTLL
CCCCCCCCCCCCEEE		33.4130266825
143PhosphorylationPRTTLLGTIFSPVFN
CCCEEEHHHCCCHHH		20.8629691806
146PhosphorylationTLLGTIFSPVFNFFS
EEEHHHCCCHHHCCC		19.1229632367
153PhosphorylationSPVFNFFSPANKNGT
CCHHHCCCCCCCCCC		20.9722617229
160PhosphorylationSPANKNGTSGSDSPG
CCCCCCCCCCCCCCC		39.0330266825
161PhosphorylationPANKNGTSGSDSPGQ
CCCCCCCCCCCCCCC		37.3823401153
163PhosphorylationNKNGTSGSDSPGQAV
CCCCCCCCCCCCCCC		34.3830266825
165PhosphorylationNGTSGSDSPGQAVEA
CCCCCCCCCCCCCCH		32.4025159151
234PhosphorylationPPLTAPVTPDSGYSS
CCCCCCCCCCCCCCC		21.9626074081
237PhosphorylationTAPVTPDSGYSSAHA
CCCCCCCCCCCCCCE		40.6126074081
239PhosphorylationPVTPDSGYSSAHAEA
CCCCCCCCCCCCEEE		11.9126074081
240PhosphorylationVTPDSGYSSAHAEAT
CCCCCCCCCCCEEEE		25.2826074081
241PhosphorylationTPDSGYSSAHAEATY
CCCCCCCCCCEEEEC		18.6526074081
275SumoylationTEEQLNRKPALPLKT
CHHHHCCCCCCCCCC		33.30-
275UbiquitinationTEEQLNRKPALPLKT
CHHHHCCCCCCCCCC		33.30-
286 (in isoform 2)Ubiquitination-41.7121890473
340PhosphorylationREFLERMSQMYEIIL
HHHHHHHHHHHHHHH		20.3029449344
343PhosphorylationLERMSQMYEIILFTA
HHHHHHHHHHHHHHC		9.0629449344
349PhosphorylationMYEIILFTASKKVYA
HHHHHHHHCCCHHHH		26.9529449344
351PhosphorylationEIILFTASKKVYADK
HHHHHHCCCHHHHHH		29.9229449344
355PhosphorylationFTASKKVYADKLLNI
HHCCCHHHHHHHHHH		20.2620049867
358UbiquitinationSKKVYADKLLNILDP
CCHHHHHHHHHHCCH		46.8621890473
358 (in isoform 1)Ubiquitination-46.8621890473
366UbiquitinationLLNILDPKKQLVRHR
HHHHCCHHHHHHHHH		53.47-
388UbiquitinationCVQGNYIKDLNILGR
EEECCEEECCEECCC		45.89-
434UbiquitinationKNDNELLKLIPFLEK
CCCHHHHHHHHHHHH		57.93-
441UbiquitinationKLIPFLEKLVELNED
HHHHHHHHHHHCCCC		61.04-
450MethylationVELNEDVRPHIRDRF
HHCCCCCCHHHHHHH		29.42-
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 CTSL2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTSL2_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 CTSL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATP5E_HUMANATP5Ephysical
26496610
IPP_HUMANIPPphysical
26496610
JAK1_HUMANJAK1physical
26496610
MYBB_HUMANMYBL2physical
26496610
RL10_HUMANRPL10physical
26496610
ELOC_HUMANTCEB1physical
26496610
MRCKA_HUMANCDC42BPAphysical
26496610
S27A2_HUMANSLC27A2physical
26496610
MED15_HUMANMED15physical
26496610
FXL19_HUMANFBXL19physical
26496610
SCYL1_HUMANSCYL1physical
26496610
KLF16_HUMANKLF16physical
26496610
CPNE8_HUMANCPNE8physical
26496610
IMA1_HUMANKPNA2physical
27880917
IMA4_HUMANKPNA3physical
27880917
IMA3_HUMANKPNA4physical
27880917
IMB1_HUMANKPNB1physical
27880917
NU153_HUMANNUP153physical
27880917
NUP93_HUMANNUP93physical
27880917
RBP2_HUMANRANBP2physical
27880917
RAGP1_HUMANRANGAP1physical
27880917
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 CTSL2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-26 AND LYS-57, AND MASSSPECTROMETRY.
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 THR-86; SER-134 AND SER-165,AND MASS SPECTROMETRY.
"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-165, 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-85; THR-86; SER-104 ANDSER-165, AND MASS 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-134, 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-51 AND SER-104, AND MASSSPECTROMETRY.

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