TAC2N_HUMAN - dbPTM
TAC2N_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAC2N_HUMAN
UniProt AC Q8N9U0
Protein Name Tandem C2 domains nuclear protein
Gene Name TC2N
Organism Homo sapiens (Human).
Sequence Length 490
Subcellular Localization Nucleus.
Protein Description
Protein Sequence MATEFIKSCCGGCFYGETEKHNFSVERDFKAAVPNSQNATISVPPLTSVSVKPQLGCTEDYLLSKLPSDGKEVPFVVPKFKLSYIQPRTQETPSHLEELEGSARASFGDRKVELSSSSQHGPSYDVYNPFYMYQHISPDLSRRFPPRSEVKRLYGSVCDLRTNKLPGSPGLSKSMFDLTNSSQRFIQRHDSLSSVPSSSSSRKNSQGSNRSLDTITLSGDERDFGRLNVKLFYNSSVEQIWITVLQCRDLSWPSSYGDTPTVSIKGILTLPKPVHFKSSAKEGSNAIEFMETFVFAIKLQNLQTVRLVFKIQTQTPRKKTIGECSMSLRTLSTQEMDYSLDITPPSKISVCHAELELGTCFQAVNSRIQLQILEARYLPSSSTPLTLSFFVKVGMFSSGELIYKKKTRLLKASNGRVKWGETMIFPLIQSEKEIVFLIKLYSRSSVRRKHFVGQIWISEDSNNIEAVNQWKETVINPEKVVIRWHKLNPS
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
7Ubiquitination-MATEFIKSCCGGCF
-CCHHHHHHHCCCCC
42.6429901268
15PhosphorylationSCCGGCFYGETEKHN
HHCCCCCCCCHHHCC
20.37-
24PhosphorylationETEKHNFSVERDFKA
CHHHCCCEEEEEHHC
28.5223312004
58PhosphorylationVKPQLGCTEDYLLSK
CCCCCCCCHHHHHHC
30.05-
61PhosphorylationQLGCTEDYLLSKLPS
CCCCCHHHHHHCCCC
11.8725627689
64PhosphorylationCTEDYLLSKLPSDGK
CCHHHHHHCCCCCCC
29.56-
83PhosphorylationVVPKFKLSYIQPRTQ
EEEEEEEEEECCCCC
22.3026657352
84PhosphorylationVPKFKLSYIQPRTQE
EEEEEEEEECCCCCC
17.6328060719
92PhosphorylationIQPRTQETPSHLEEL
ECCCCCCCCCHHHHH
21.9228060719
102PhosphorylationHLEELEGSARASFGD
HHHHHCCCCCCCCCC
12.7628060719
106PhosphorylationLEGSARASFGDRKVE
HCCCCCCCCCCEEEE
24.9824719451
115PhosphorylationGDRKVELSSSSQHGP
CCEEEEECCCCCCCC
18.0527642862
116PhosphorylationDRKVELSSSSQHGPS
CEEEEECCCCCCCCC
46.7828270605
117PhosphorylationRKVELSSSSQHGPSY
EEEEECCCCCCCCCC
30.5528270605
118PhosphorylationKVELSSSSQHGPSYD
EEEECCCCCCCCCCC
28.3028270605
123PhosphorylationSSSQHGPSYDVYNPF
CCCCCCCCCCCCCCC
38.2627642862
124PhosphorylationSSQHGPSYDVYNPFY
CCCCCCCCCCCCCCH
16.7428270605
127PhosphorylationHGPSYDVYNPFYMYQ
CCCCCCCCCCCHHHH
17.7728270605
131PhosphorylationYDVYNPFYMYQHISP
CCCCCCCHHHHCCCC
9.0026657352
133PhosphorylationVYNPFYMYQHISPDL
CCCCCHHHHCCCCCH
5.8828270605
137PhosphorylationFYMYQHISPDLSRRF
CHHHHCCCCCHHHCC
15.3825849741
141PhosphorylationQHISPDLSRRFPPRS
HCCCCCHHHCCCCHH
28.8828270605
154PhosphorylationRSEVKRLYGSVCDLR
HHHHHHHHCCHHHCC
16.0429978859
156PhosphorylationEVKRLYGSVCDLRTN
HHHHHHCCHHHCCCC
13.1523401153
162PhosphorylationGSVCDLRTNKLPGSP
CCHHHCCCCCCCCCC
43.9628060719
168PhosphorylationRTNKLPGSPGLSKSM
CCCCCCCCCCCCHHH
17.5425159151
172PhosphorylationLPGSPGLSKSMFDLT
CCCCCCCCHHHHHCC
28.7129978859
174PhosphorylationGSPGLSKSMFDLTNS
CCCCCCHHHHHCCHH
22.7028355574
179PhosphorylationSKSMFDLTNSSQRFI
CHHHHHCCHHHHHHH
34.59-
181PhosphorylationSMFDLTNSSQRFIQR
HHHHCCHHHHHHHHH
23.7128060719
182PhosphorylationMFDLTNSSQRFIQRH
HHHCCHHHHHHHHHH
27.6928060719
191PhosphorylationRFIQRHDSLSSVPSS
HHHHHHHCCCCCCCC
24.8325849741
193PhosphorylationIQRHDSLSSVPSSSS
HHHHHCCCCCCCCCC
32.9928060719
194PhosphorylationQRHDSLSSVPSSSSS
HHHHCCCCCCCCCCC
43.2528060719
197PhosphorylationDSLSSVPSSSSSRKN
HCCCCCCCCCCCCCC
40.4728060719
198PhosphorylationSLSSVPSSSSSRKNS
CCCCCCCCCCCCCCC
28.3328060719
199PhosphorylationLSSVPSSSSSRKNSQ
CCCCCCCCCCCCCCC
36.3528060719
200PhosphorylationSSVPSSSSSRKNSQG
CCCCCCCCCCCCCCC
35.7928060719
201PhosphorylationSVPSSSSSRKNSQGS
CCCCCCCCCCCCCCC
49.5828060719
205PhosphorylationSSSSRKNSQGSNRSL
CCCCCCCCCCCCCCC
38.6727362937
208PhosphorylationSRKNSQGSNRSLDTI
CCCCCCCCCCCCCEE
22.7927362937
211PhosphorylationNSQGSNRSLDTITLS
CCCCCCCCCCEEEEC
34.5430278072
214PhosphorylationGSNRSLDTITLSGDE
CCCCCCCEEEECCCC
22.5828348404
216PhosphorylationNRSLDTITLSGDERD
CCCCCEEEECCCCCC
19.5727499020
218PhosphorylationSLDTITLSGDERDFG
CCCEEEECCCCCCCC
35.2327362937
313PhosphorylationRLVFKIQTQTPRKKT
EEEEEEECCCCCCCC
37.5729514088
315PhosphorylationVFKIQTQTPRKKTIG
EEEEECCCCCCCCHH
28.5729514088
320O-linked_GlycosylationTQTPRKKTIGECSMS
CCCCCCCCHHCCCEE
36.9330379171
325PhosphorylationKKTIGECSMSLRTLS
CCCHHCCCEEEEECC
13.7028060719
327PhosphorylationTIGECSMSLRTLSTQ
CHHCCCEEEEECCCC
9.8228060719
330PhosphorylationECSMSLRTLSTQEMD
CCCEEEEECCCCCCE
30.2928348404
332PhosphorylationSMSLRTLSTQEMDYS
CEEEEECCCCCCEEE
27.6828348404
333PhosphorylationMSLRTLSTQEMDYSL
EEEEECCCCCCEEEC
31.4928348404
382PhosphorylationARYLPSSSTPLTLSF
EEECCCCCCCEEEEE
38.0828348404
383PhosphorylationRYLPSSSTPLTLSFF
EECCCCCCCEEEEEE
25.0228348404
388PhosphorylationSSTPLTLSFFVKVGM
CCCCEEEEEEEEECC
16.05-
403PhosphorylationFSSGELIYKKKTRLL
CCCCCEEEEECCEEE
29.4025627689
407PhosphorylationELIYKKKTRLLKASN
CEEEEECCEEEECCC
35.1124732914
422PhosphorylationGRVKWGETMIFPLIQ
CCCEECCEEEEEEEC
16.1929052541
430PhosphorylationMIFPLIQSEKEIVFL
EEEEEECCCCCEEEE
43.5829052541
442PhosphorylationVFLIKLYSRSSVRRK
EEEEEHHHCCCCCHH
35.8024719451
473PhosphorylationAVNQWKETVINPEKV
HHHHHHHCCCCHHHE
23.9824719451

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 TAC2N_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAC2N_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 TAC2N_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TAC2N_HUMAN !!

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 TAC2N_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-168; SER-211;THR-214; THR-216 AND SER-218, AND MASS SPECTROMETRY.

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