dbPTM

COHA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COHA1_HUMAN
UniProt AC	Q9UMD9
Protein Name	Collagen alpha-1(XVII) chain
Gene Name	COL17A1
Organism	Homo sapiens (Human).
Sequence Length	1497
Subcellular Localization	Cell junction, hemidesmosome. Membrane Single-pass type II membrane protein. Localized along the plasma membrane of the hemidesmosome. 120 kDa linear IgA disease antigen: Secreted, extracellular space, extracellular matrix, basement membrane.
Protein Description	May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane.; The 120 kDa linear IgA disease antigen is an anchoring filament component involved in dermal-epidermal cohesion. Is the target of linear IgA bullous dermatosis autoantibodies..
Protein Sequence	MDVTKKNKRDGTEVTERIVTETVTTRLTSLPPKGGTSNGYAKTASLGGGSRLEKQSLTHGSSGYINSTGSTRGHASTSSYRRAHSPASTLPNSPGSTFERKTHVTRHAYEGSSSGNSSPEYPRKEFASSSTRGRSQTRESEIRVRLQSASPSTRWTELDDVKRLLKGSRSASVSPTRNSSNTLPIPKKGTVETKIVTASSQSVSGTYDATILDANLPSHVWSSTLPAGSSMGTYHNNMTTQSSSLLNTNAYSAGSVFGVPNNMASCSPTLHPGLSTSSSVFGMQNNLAPSLTTLSHGTTTTSTAYGVKKNMPQSPAAVNTGVSTSAACTTSVQSDDLLHKDCKFLILEKDNTPAKKEMELLIMTKDSGKVFTASPASIAATSFSEDTLKKEKQAAYNADSGLKAEANGDLKTVSTKGKTTTADIHSYGSSGGGGSGGGGGVGGAGGGPWGPAPAWCPCGSCCSWWKWLLGLLLTWLLLLGLLFGLIALAEEVRKLKARVDELERIRRSILPYGDSMDRIEKDRLQGMAPAAGADLDKIGLHSDSQEELWMFVRKKLMMEQENGNLRGSPGPKGDMGSPGPKGDRGFPGTPGIPGPLGHPGPQGPKGQKGSVGDPGMEGPMGQRGREGPMGPRGEAGPPGSGEKGERGAAGEPGPHGPPGVPGSVGPKGSSGSPGPQGPPGPVGLQGLRGEVGLPGVKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAGPDGHQGPRGEQGLTGMPGIRGPPGPSGDPGKPGLTGPQGPQGLPGTPGRPGIKGEPGAPGKIVTSEGSSMLTVPGPPGPPGAMGPPGPPGAPGPAGPAGLPGHQEVLNLQGPPGPPGPRGPPGPSIPGPPGPRGPPGEGLPGPPGPPGSFLSNSETFLSGPPGPPGPPGPKGDQGPPGPRGHQGEQGLPGFSTSGSSSFGLNLQGPPGPPGPQGPKGDKGDPGVPGALGIPSGPSEGGSSSTMYVSGPPGPPGPPGPPGSISSSGQEIQQYISEYMQSDSIRSYLSGVQGPPGPPGPPGPVTTITGETFDYSELASHVVSYLRTSGYGVSLFSSSISSEDILAVLQRDDVRQYLRQYLMGPRGPPGPPGASGDGSLLSLDYAELSSRILSYMSSSGISIGLPGPPGPPGLPGTSYEELLSLLRGSEFRGIVGPPGPPGPPGIPGNVWSSISVEDLSSYLHTAGLSFIPGPPGPPGPPGPRGPPGVSGALATYAAENSDSFRSELISYLTSPDVRSFIVGPPGPPGPQGPPGDSRLLSTDASHSRGSSSSSHSSSVRRGSSYSSSMSTGGGGAGSLGAGGAFGEAAGDRGPYGTDIGPGGGYGAAAEGGMYAGNGGLLGADFAGDLDYNELAVRVSESMQRQGLLQGMAYTVQGPPGQPGPQGPPGISKVFSAYSNVTADLMDFFQTYGAIQGPPGQKGEMGTPGPKGDRGPAGPPGHPGPPGPRGHKGEKGDKGDQVYAGRRRRRSIAVKP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	KRDGTEVTERIVTET CCCCCCCHHHEEEEE	17.20	29970186
40	Phosphorylation	KGGTSNGYAKTASLG CCCCCCCEEEEEECC	14.80	19534553
43	Phosphorylation	TSNGYAKTASLGGGS CCCCEEEEEECCCCC	17.20	23927012
45	Phosphorylation	NGYAKTASLGGGSRL CCEEEEEECCCCCCC	32.55	23927012
50	Phosphorylation	TASLGGGSRLEKQSL EEECCCCCCCEEECC	36.65	27251275
56	Phosphorylation	GSRLEKQSLTHGSSG CCCCEEECCCCCCCC	46.43	23927012
58	Phosphorylation	RLEKQSLTHGSSGYI CCEEECCCCCCCCEE	29.45	26657352
61	Phosphorylation	KQSLTHGSSGYINST EECCCCCCCCEECCC	17.00	28731282
62	Phosphorylation	QSLTHGSSGYINSTG ECCCCCCCCEECCCC	39.96	23927012
64	Phosphorylation	LTHGSSGYINSTGST CCCCCCCEECCCCCC	10.01	23927012
67	Phosphorylation	GSSGYINSTGSTRGH CCCCEECCCCCCCCC	25.29	23927012
68	Phosphorylation	SSGYINSTGSTRGHA CCCEECCCCCCCCCC	30.57	25106551
70	Phosphorylation	GYINSTGSTRGHAST CEECCCCCCCCCCCC	18.28	29743597
71	Phosphorylation	YINSTGSTRGHASTS EECCCCCCCCCCCCC	41.85	23927012
77	Phosphorylation	STRGHASTSSYRRAH CCCCCCCCCCCCCCC	23.60	26853621
78	Phosphorylation	TRGHASTSSYRRAHS CCCCCCCCCCCCCCC	23.91	26853621
79	Phosphorylation	RGHASTSSYRRAHSP CCCCCCCCCCCCCCC	23.81	29743597
80	Phosphorylation	GHASTSSYRRAHSPA CCCCCCCCCCCCCCC	12.13	-
85	Phosphorylation	SSYRRAHSPASTLPN CCCCCCCCCCCCCCC	22.60	28731282
88	Phosphorylation	RRAHSPASTLPNSPG CCCCCCCCCCCCCCC	33.58	23927012
89	Phosphorylation	RAHSPASTLPNSPGS CCCCCCCCCCCCCCC	48.63	23927012
93	Phosphorylation	PASTLPNSPGSTFER CCCCCCCCCCCCCCC	28.79	28731282
96	Phosphorylation	TLPNSPGSTFERKTH CCCCCCCCCCCCEEC	33.05	23927012
97	Phosphorylation	LPNSPGSTFERKTHV CCCCCCCCCCCEECE	35.12	23927012
105	Phosphorylation	FERKTHVTRHAYEGS CCCEECEEECCCCCC	14.77	-
109	Phosphorylation	THVTRHAYEGSSSGN ECEEECCCCCCCCCC	18.07	23927012
112	Phosphorylation	TRHAYEGSSSGNSSP EECCCCCCCCCCCCC	14.91	23927012
113	Phosphorylation	RHAYEGSSSGNSSPE ECCCCCCCCCCCCCC	53.79	23927012
114	Phosphorylation	HAYEGSSSGNSSPEY CCCCCCCCCCCCCCC	43.63	23927012
117	Phosphorylation	EGSSSGNSSPEYPRK CCCCCCCCCCCCCHH	51.28	26657352
118	Phosphorylation	GSSSGNSSPEYPRKE CCCCCCCCCCCCHHH	26.25	29743597
121	Phosphorylation	SGNSSPEYPRKEFAS CCCCCCCCCHHHHHC	16.24	23927012
128	Phosphorylation	YPRKEFASSSTRGRS CCHHHHHCCCCCCCC	30.09	27794612
129	Phosphorylation	PRKEFASSSTRGRSQ CHHHHHCCCCCCCCC	32.09	27794612
130	Phosphorylation	RKEFASSSTRGRSQT HHHHHCCCCCCCCCC	21.45	29743597
131	Phosphorylation	KEFASSSTRGRSQTR HHHHCCCCCCCCCCC	38.81	27794612
135	Phosphorylation	SSSTRGRSQTRESEI CCCCCCCCCCCHHHH	38.43	27794612
137	Phosphorylation	STRGRSQTRESEIRV CCCCCCCCCHHHHHH	37.34	27794612
140	Phosphorylation	GRSQTRESEIRVRLQ CCCCCCHHHHHHHHH	34.72	29743597
148	Phosphorylation	EIRVRLQSASPSTRW HHHHHHHCCCCCCCC	34.99	28731282
150	Phosphorylation	RVRLQSASPSTRWTE HHHHHCCCCCCCCEE	25.32	28731282
152	Phosphorylation	RLQSASPSTRWTELD HHHCCCCCCCCEEHH	28.27	23927012
153	Phosphorylation	LQSASPSTRWTELDD HHCCCCCCCCEEHHH	33.34	23927012
156	Phosphorylation	ASPSTRWTELDDVKR CCCCCCCEEHHHHHH	24.31	20639409
168	Phosphorylation	VKRLLKGSRSASVSP HHHHHCCCCCCCCCC	22.83	23090842
170	Phosphorylation	RLLKGSRSASVSPTR HHHCCCCCCCCCCCC	26.96	29743597
172	Phosphorylation	LKGSRSASVSPTRNS HCCCCCCCCCCCCCC	25.11	28731282
174	Phosphorylation	GSRSASVSPTRNSSN CCCCCCCCCCCCCCC	20.33	28731282
176	Phosphorylation	RSASVSPTRNSSNTL CCCCCCCCCCCCCCC	34.67	28985074
179	Phosphorylation	SVSPTRNSSNTLPIP CCCCCCCCCCCCCCC	22.98	29743597
180	Phosphorylation	VSPTRNSSNTLPIPK CCCCCCCCCCCCCCC	37.07	29743597
182	Phosphorylation	PTRNSSNTLPIPKKG CCCCCCCCCCCCCCC	35.54	29743597
303	Phosphorylation	HGTTTTSTAYGVKKN CCCCCCCCCCCCCCC	23.08	22817900
305	Phosphorylation	TTTTSTAYGVKKNMP CCCCCCCCCCCCCCC	23.65	22817900
320	Phosphorylation	QSPAAVNTGVSTSAA CCCCCCCCCCCCCCC	32.15	23532336
352	Phosphorylation	LILEKDNTPAKKEME EEEECCCCCCHHHEE	34.45	23927012
365	Acetylation	MELLIMTKDSGKVFT EEEEEEECCCCCEEE	32.30	19859113
367	Phosphorylation	LLIMTKDSGKVFTAS EEEEECCCCCEEECC	41.91	-
369	Acetylation	IMTKDSGKVFTASPA EEECCCCCEEECCHH	37.82	30586161
372	Phosphorylation	KDSGKVFTASPASIA CCCCCEEECCHHHHH	29.25	29743597
374	Phosphorylation	SGKVFTASPASIAAT CCCEEECCHHHHHCC	20.24	29743597
377	Phosphorylation	VFTASPASIAATSFS EEECCHHHHHCCCCC	19.02	29743597
381	Phosphorylation	SPASIAATSFSEDTL CHHHHHCCCCCHHHH	22.68	20639409
382	Phosphorylation	PASIAATSFSEDTLK HHHHHCCCCCHHHHH	23.27	29743597
384	Phosphorylation	SIAATSFSEDTLKKE HHHCCCCCHHHHHHH	34.04	23927012
387	Phosphorylation	ATSFSEDTLKKEKQA CCCCCHHHHHHHHHH	36.10	29743597
389	Ubiquitination	SFSEDTLKKEKQAAY CCCHHHHHHHHHHHH	62.06	22817900
389 (in isoform 1)	Ubiquitination	-	62.06	21906983
389 (in isoform 2)	Ubiquitination	-	62.06	21906983
390	Ubiquitination	FSEDTLKKEKQAAYN CCHHHHHHHHHHHHH	73.57	22817900
392	Ubiquitination	EDTLKKEKQAAYNAD HHHHHHHHHHHHHCC	54.86	22817900
396	Phosphorylation	KKEKQAAYNADSGLK HHHHHHHHHCCCCCE	17.56	27259358
400	Phosphorylation	QAAYNADSGLKAEAN HHHHHCCCCCEEHHC	43.55	17924679
403	Ubiquitination	YNADSGLKAEANGDL HHCCCCCEEHHCCCC	47.94	22817900
403 (in isoform 1)	Ubiquitination	-	47.94	21906983
403 (in isoform 2)	Ubiquitination	-	47.94	21906983
512	Phosphorylation	IRRSILPYGDSMDRI HHHHHCCCCCCHHHH	30.07	-
515	Phosphorylation	SILPYGDSMDRIEKD HHCCCCCCHHHHHHH	20.44	-
542	Phosphorylation	LDKIGLHSDSQEELW HHHCCCCCCCHHHHH	43.96	22817900
544	Phosphorylation	KIGLHSDSQEELWMF HCCCCCCCHHHHHHH	42.37	8669466
610	Phosphorylation	GPKGQKGSVGDPGME CCCCCCCCCCCCCCC	29.93	28674151
640	Phosphorylation	GEAGPPGSGEKGERG CCCCCCCCCCCCCCC	49.94	-
1124	Phosphorylation	SGDGSLLSLDYAELS CCCCCEECCCHHHHH	25.20	-
1131	Phosphorylation	SLDYAELSSRILSYM CCCHHHHHHHHHHHH	14.74	-
1284	O-linked_Glycosylation	GDSRLLSTDASHSRG CCCCCCCCCCCCCCC	35.24	55831783
1284	Phosphorylation	GDSRLLSTDASHSRG CCCCCCCCCCCCCCC	35.24	-
1287	Phosphorylation	RLLSTDASHSRGSSS CCCCCCCCCCCCCCC	25.46	28985074
1289	Phosphorylation	LSTDASHSRGSSSSS CCCCCCCCCCCCCCC	35.52	28985074
1295	Phosphorylation	HSRGSSSSSHSSSVR CCCCCCCCCCCCCCC	33.74	29759185
1296	Phosphorylation	SRGSSSSSHSSSVRR CCCCCCCCCCCCCCC	29.36	29759185
1298	Phosphorylation	GSSSSSHSSSVRRGS CCCCCCCCCCCCCCC	26.68	29759185
1299	Phosphorylation	SSSSSHSSSVRRGSS CCCCCCCCCCCCCCC	27.68	29759185
1300	Phosphorylation	SSSSHSSSVRRGSSY CCCCCCCCCCCCCCC	23.74	29759185
1305	Phosphorylation	SSSVRRGSSYSSSMS CCCCCCCCCCCCCCC	25.04	23312004
1306	Phosphorylation	SSVRRGSSYSSSMST CCCCCCCCCCCCCCC	31.68	23312004
1307	Phosphorylation	SVRRGSSYSSSMSTG CCCCCCCCCCCCCCC	17.80	23312004
1308	Phosphorylation	VRRGSSYSSSMSTGG CCCCCCCCCCCCCCC	20.20	23312004
1309	Phosphorylation	RRGSSYSSSMSTGGG CCCCCCCCCCCCCCC	23.10	23312004
1310	Phosphorylation	RGSSYSSSMSTGGGG CCCCCCCCCCCCCCC	15.71	23312004
1312	Phosphorylation	SSYSSSMSTGGGGAG CCCCCCCCCCCCCCC	26.33	23312004
1313	Phosphorylation	SYSSSMSTGGGGAGS CCCCCCCCCCCCCCC	31.07	23312004
1395	Phosphorylation	GLLQGMAYTVQGPPG CCCCCCEEECCCCCC	9.88	-
1421	N-linked_Glycosylation	KVFSAYSNVTADLMD HHHHHHCCCCHHHHH	23.60	9748270
1421	N-linked_Glycosylation	KVFSAYSNVTADLMD HHHHHHCCCCHHHHH	23.60	9748270

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
542	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
544	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
544	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
544	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
544	S	Phosphorylation		17545155
This cleavage is inhibited by phosphorylation at Ser-544.

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 COHA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DYST_HUMAN	DST	physical	12482924
ACTN4_HUMAN	ACTN4	physical	11739652
ACTN1_HUMAN	ACTN1	physical	11739652
ITB4_HUMAN	ITGB4	physical	9500991
CTND1_HUMAN	CTNND1	physical	10321838
K1C18_HUMAN	KRT18	physical	10022517
DYST_HUMAN	DST	physical	10637308
PEPL_HUMAN	PPL	physical	9521878

Drug and Disease Associations

Kegg Disease
H00586	Epidermolysis bullosa, junctional, including: Epidermolysis bullosa, junctional, Herlitz type (JEB-H
OMIM Disease
226650	Generalized atrophic benign epidermolysis bullosa (GABEB)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of COHA1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Two forms of collagen XVII in keratinocytes. A full-lengthtransmembrane protein and a soluble ectodomain."; Schaecke H., Schumann H., Hammami-Hauasli N., Raghunath M.,Bruckner-Tuderman L.; J. Biol. Chem. 273:25937-25943(1998). Cited for: SUBUNIT, PROTEOLYTIC PROCESSING, GLYCOSYLATION AT ASN-1421, ANDDOMAINS.	9748270 [Abstract]
Phosphorylation
Reference	PubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Extracellular phosphorylation of collagen XVII by ecto-casein kinase2 inhibits ectodomain shedding."; Zimina E.P., Fritsch A., Schermer B., Bakulina A.Y., Bashkurov M.,Benzing T., Bruckner-Tuderman L.; J. Biol. Chem. 282:22737-22746(2007). Cited for: PHOSPHORYLATION AT SER-544.	17545155 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40; TYR-64 AND TYR-396,AND MASS SPECTROMETRY.	19534553 [Abstract]

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