TMCC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TMCC1_HUMAN
• UniProt AC: O94876
• Protein Name: Transmembrane and coiled-coil domains protein 1
• Gene Name: TMCC1
• Organism: Homo sapiens (Human).
• Sequence Length: 653
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Sequence: MEPSGSEQLFEDPDPGGKSQDAEARKQTESEQKLSKMTHNALENINVIGQGLKHLFQHQRRRSSVSPHDVQQIQADPEPEMDLESQNACAEIDGVPTHPTALNRVLQQIRVPPKMKRGTSLHSRRGKPEAPKGSPQINRKSGQEMTAVMQSGRPRSSSTTDAPTSSAMMEIACAAAAAAAACLPGEEGTAERIERLEVSSLAQTSSAVASSTDGSIHTDSVDGTPDPQRTKAAIAHLQQKILKLTEQIKIAQTARDDNVAEYLKLANSADKQQAARIKQVFEKKNQKSAQTILQLQKKLEHYHRKLREVEQNGIPRQPKDVFRDMHQGLKDVGAKVTGFSEGVVDSVKGGFSSFSQATHSAAGAVVSKPREIASLIRNKFGSADNIPNLKDSLEEGQVDDAGKALGVISNFQSSPKYGSEEDCSSATSGSVGANSTTGGIAVGASSSKTNTLDMQSSGFDALLHEIQEIRETQARLEESFETLKEHYQRDYSLIMQTLQEERYRCERLEEQLNDLTELHQNEILNLKQELASMEEKIAYQSYERARDIQEALEACQTRISKMELQQQQQQVVQLEGLENATARNLLGKLINILLAVMAVLLVFVSTVANCVVPLMKTRNRTFSTLFLVVFIAFLWKHWDALFSYVERFFSSPR

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
1	Acetylation	-------MEPSGSEQ -------CCCCCCCC	18.03	22814378
6 (in isoform 2)	Phosphorylation	-	26.89	30266825
63	Phosphorylation	FQHQRRRSSVSPHDV HHHHHHHCCCCHHHH	33.03	22817900
64	Phosphorylation	QHQRRRSSVSPHDVQ HHHHHHCCCCHHHHH	25.46	22817900
66	Phosphorylation	QRRRSSVSPHDVQQI HHHHCCCCHHHHHHH	20.61	26471730
117	Methylation	RVPPKMKRGTSLHSR CCCCCCCCCCCCCCC	50.56	115918605
120	Phosphorylation	PKMKRGTSLHSRRGK CCCCCCCCCCCCCCC	27.23	26437602
134	Phosphorylation	KPEAPKGSPQINRKS CCCCCCCCCCCCCCC	21.54	21955146
140	Acetylation	GSPQINRKSGQEMTA CCCCCCCCCCCCCHH	55.22	7670837
141	Phosphorylation	SPQINRKSGQEMTAV CCCCCCCCCCCCHHH	42.33	28555341
156	Phosphorylation	MQSGRPRSSSTTDAP HHCCCCCCCCCCCCC	31.18	22817900
157	Phosphorylation	QSGRPRSSSTTDAPT HCCCCCCCCCCCCCC	32.74	22817900
158	Phosphorylation	SGRPRSSSTTDAPTS CCCCCCCCCCCCCCC	36.25	20736484
159	Phosphorylation	GRPRSSSTTDAPTSS CCCCCCCCCCCCCCH	30.55	20736484
160	Phosphorylation	RPRSSSTTDAPTSSA CCCCCCCCCCCCCHH	31.92	20736484
212	Phosphorylation	SSAVASSTDGSIHTD CCHHHCCCCCCCCCC	41.71	24532841
215	Phosphorylation	VASSTDGSIHTDSVD HHCCCCCCCCCCCCC	17.63	24532841
253	Phosphorylation	EQIKIAQTARDDNVA HHHHHHHHCCCCCHH	18.03	-
337	Phosphorylation	KDVGAKVTGFSEGVV HHHCCCCCCCCCCHH	31.63	-
348	Acetylation	EGVVDSVKGGFSSFS CCHHHHHCCCCCCHH	58.21	7704131
353	Phosphorylation	SVKGGFSSFSQATHS HHCCCCCCHHHHHHC	27.02	28857561
374	Phosphorylation	SKPREIASLIRNKFG CCHHHHHHHHHHHHC	29.95	24719451
382	Ubiquitination	LIRNKFGSADNIPNL HHHHHHCCCCCCCCH	35.27	21906983
382	Phosphorylation	LIRNKFGSADNIPNL HHHHHHCCCCCCCCH	35.27	19664994
392	Phosphorylation	NIPNLKDSLEEGQVD CCCCHHHHHHHCCCC	35.77	30266825
409	Phosphorylation	GKALGVISNFQSSPK HHHHHHHHCCCCCCC	29.23	28102081
413	Phosphorylation	GVISNFQSSPKYGSE HHHHCCCCCCCCCCH	44.46	30266825
414	Phosphorylation	VISNFQSSPKYGSEE HHHCCCCCCCCCCHH	18.03	19664994
417	Phosphorylation	NFQSSPKYGSEEDCS CCCCCCCCCCHHHHC	29.30	21406692
419	Phosphorylation	QSSPKYGSEEDCSSA CCCCCCCCHHHHCCC	34.42	21406692
424	Phosphorylation	YGSEEDCSSATSGSV CCCHHHHCCCCCCCC	35.02	21406692
425	Phosphorylation	GSEEDCSSATSGSVG CCHHHHCCCCCCCCC	41.73	21406692
427	Phosphorylation	EEDCSSATSGSVGAN HHHHCCCCCCCCCCC	35.25	21406692
428	Phosphorylation	EDCSSATSGSVGANS HHHCCCCCCCCCCCC	28.87	21406692
430	Phosphorylation	CSSATSGSVGANSTT HCCCCCCCCCCCCCC	19.69	21406692
435	Phosphorylation	SGSVGANSTTGGIAV CCCCCCCCCCCCEEE	27.15	21406692
436	Phosphorylation	GSVGANSTTGGIAVG CCCCCCCCCCCEEEC	29.30	21406692
437	Phosphorylation	SVGANSTTGGIAVGA CCCCCCCCCCEEECC	32.98	21406692
445	Phosphorylation	GGIAVGASSSKTNTL CCEEECCCCCCCCCC	29.26	21406692
446	Phosphorylation	GIAVGASSSKTNTLD CEEECCCCCCCCCCC	35.01	21406692
447	Phosphorylation	IAVGASSSKTNTLDM EEECCCCCCCCCCCC	40.79	21406692
449	Phosphorylation	VGASSSKTNTLDMQS ECCCCCCCCCCCCHH	35.07	27732954
451	Phosphorylation	ASSSKTNTLDMQSSG CCCCCCCCCCCHHHH	29.39	27732954
479	Phosphorylation	TQARLEESFETLKEH HHHHHHHHHHHHHHH	21.00	21815630
482	Phosphorylation	RLEESFETLKEHYQR HHHHHHHHHHHHHHH	40.91	29523821
539	Phosphorylation	SMEEKIAYQSYERAR HHHHHHHHHHHHHHH	11.06	26657352
542	Phosphorylation	EKIAYQSYERARDIQ HHHHHHHHHHHHHHH	8.23	26657352
561	Ubiquitination	ACQTRISKMELQQQQ HHHHHHHHHHHHHHH	33.74	2190698

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TMCC1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TMCC1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TMCC1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of TMCC1_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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-414, AND MASSSPECTROMETRY.
PubMed: 18691976

"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-382, AND MASSSPECTROMETRY.
PubMed: 17081983