COCA1_HUMAN - dbPTM
COCA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COCA1_HUMAN
UniProt AC Q99715
Protein Name Collagen alpha-1(XII) chain
Gene Name COL12A1
Organism Homo sapiens (Human).
Sequence Length 3063
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Type XII collagen interacts with type I collagen-containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix..
Protein Sequence MRSRLPPALAALGAALLLSSIEAEVDPPSDLNFKIIDENTVHMSWAKPVDPIVGYRITVDPTTDGPTKEFTLSASTTETLLSELVPETEYVVTITSYDEVEESVPVIGQLTIQTGSSTKPVEKKPGKTEIQKCSVSAWTDLVFLVDGSWSVGRNNFKYILDFIAALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYQRDELLAAIKKIPYKGGNTMTGDAIDYLVKNTFTESAGARVGFPKVAIIITDGKSQDEVEIPARELRNVGVEVFSLGIKAADAKELKQIASTPSLNHVFNVANFDAIVDIQNEIISQVCSGVDEQLGELVSGEEVVEPPSNLIAMEVSSKYVKLNWNPSPSPVTGYKVILTPMTAGSRQHALSVGPQTTTLSVRDLSADTEYQISVSAMKGMTSSEPISIMEKTQPMKVQVECSRGVDIKADIVFLVDGSYSIGIANFVKVRAFLEVLVKSFEISPNRVQISLVQYSRDPHTEFTLKKFTKVEDIIEAINTFPYRGGSTNTGKAMTYVREKIFVPSKGSRSNVPKVMILITDGKSSDAFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETHVFTVEDFDAFQRISFELTQSICLRIEQELAAIKKKAYVPPKDLSFSEVTSYGFKTNWSPAGENVFSYHITYKEAAGDDEVTVVEPASSTSVVLSSLKPETLYLVNVTAEYEDGFSIPLAGEETTEEVKGAPRNLKVTDETTDSFKITWTQAPGRVLRYRIIYRPVAGGESREVTTPPNQRRRTLENLIPDTKYEVSVIPEYFSGPGTPLTGNAATEEVRGNPRDLRVSDPTTSTMKLSWSGAPGKVKQYLVTYTPVAGGETQEVTVRGDTTNTVLQGLKEGTQYALSVTALYASGAGDALFGEGTTLEERGSPQDLVTKDITDTSIGAYWTSAPGMVRGYRVSWKSLYDDVDTGEKNLPEDAIHTMIENLQPETKYRISVFATYSSGEGEPLTGDATTELSQDSKTLKVDEETENTMRVTWKPAPGKVVNYRVVYRPHGRGKQMVAKVPPTVTSTVLKRLQPQTTYDITVLPIYKMGEGKLRQGSGTTASRFKSPRNLKTSDPTMSSFRVTWEPAPGEVKGYKVTFHPTGDDRRLGELVVGPYDNTVVLEELRAGTTYKVNVFGMFDGGESSPLVGQEMTTLSDTTVMPILSSGMECLTRAEADIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTLTGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYNVADFESLSRIVDDLTINLCNSVKGPGDLEAPSNLVISERTHRSFRVSWTPPSDSVDRYKVEYYPVSGGKRQEFYVSRMETSTVLKDLKPETEYVVNVYSVVEDEYSEPLKGTEKTLPVPVVSLNIYDVGPTTMHVQWQPVGGATGYILSYKPVKDTEPTRPKEVRLGPTVNDMQLTDLVPNTEYAVTVQAVLHDLTSEPVTVREVTLPLPRPQDLKLRDVTHSTMNVFWEPVPGKVRKYIVRYKTPEEDVKEVEVDRSETSTSLKDLFSQTLYTVSVSAVHDEGESPPVTAQETTRPVPAPTNLKITEVTSEGFRGTWDHGASDVSLYRITWAPFGSSDKMETILNGDENTLVFENLNPNTIYEVSITAIYPDESESDDLIGSERTLPILTTQAPKSGPRNLQVYNATSNSLTVKWDPASGRVQKYRITYQPSTGEGNEQTTTIGGRQNSVVLQKLKPDTPYTITVSSLYPDGEGGRMTGRGKTKPLNTVRNLRVYDPSTSTLNVRWDHAEGNPRQYKLFYAPAAGGPEELVPIPGNTNYAILRNLQPDTSYTVTVVPVYTEGDGGRTSDTGRTLMRGLARNVQVYNPTPNSLDVRWDPAPGPVLQYRVVYSPVDGTRPSESIVVPGNTRMVHLERLIPDTLYSVNLVALYSDGEGNPSPAQGRTLPRSGPRNLRVFGETTNSLSVAWDHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAVYEDGDGGHLTGNGRTVGLLPPQNIHISDEWYTRFRVSWDPSPSPVLGYKIVYKPVGSNEPMEAFVGEMTSYTLHNLNPSTTYDVNVYAQYDSGLSVPLTDQGTTLYLNVTDLKTYQIGWDTFCVKWSPHRAATSYRLKLSPADGTRGQEITVRGSETSHCFTGLSPDTDYGVTVFVQTPNLEGPGVSVKEHTTVKPTEAPTEPPTPPPPPTIPPARDVCKGAKADIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDEISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNTRTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSERHVFIVDDFESFEKIEDNLITFVCETATSSCPLIYLDGYTSPGFKMLEAYNLTEKNFASVQGVSLESGSFPSYSAYRIQKNAFVNQPTADLHPNGLPPSYTIILLFRLLPETPSDPFAIWQITDRDYKPQVGVIADPSSKTLSFFNKDTRGEVQTVTFDTEEVKTLFYGSFHKVHIVVTSKSVKIYIDCYEIIEKDIKEAGNITTDGYEILGKLLKGERKSAAFQIQSFDIVCSPVWTSRDRCCDIPSRRDEGKCPAFPNSCTCTQDSVGPPGPPGPAGGPGAKGPRGERGISGAIGPPGPRGDIGPPGPQGPPGPQGPNGLSIPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRGFTGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRGDIASQNMMRAVARQVCEQLISGQMNRFNQMLNQIPNDYQSSRNQPGPPGPPGPPGSAGARGEPGPGGRPGFPGTPGMQGPPGERGLPGEKGERGTGSSGPRGLPGPPGPQGESRTGPPGSTGSRGPPGPPGRPGNSGIRGPPGPPGYCDSSQCASIPYNGQGYPGSG
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
3 (in isoform 2)Phosphorylation-50.4522210691
19 (in isoform 2)Phosphorylation-29.2822210691
45 (in isoform 2)Phosphorylation-10.7522210691
62PhosphorylationYRITVDPTTDGPTKE
EEEEECCCCCCCCCE
32.8120068231
63PhosphorylationRITVDPTTDGPTKEF
EEEECCCCCCCCCEE
44.3320068231
67PhosphorylationDPTTDGPTKEFTLSA
CCCCCCCCCEEEECC
49.0520068231
147UbiquitinationDLVFLVDGSWSVGRN
CEEEEECCCCCCCCC
24.4329967540
208UbiquitinationDELLAAIKKIPYKGG
HHHHHHHHCCCCCCC
39.6729967540
217PhosphorylationIPYKGGNTMTGDAID
CCCCCCCCCCHHHHH
21.27-
273PhosphorylationNVGVEVFSLGIKAAD
HCCCEEEECCEECCC
30.7520068231
357PhosphorylationVKLNWNPSPSPVTGY
EECCCCCCCCCCCCC
34.4922210691
359PhosphorylationLNWNPSPSPVTGYKV
CCCCCCCCCCCCCEE
36.0222210691
372PhosphorylationKVILTPMTAGSRQHA
EEEEEECCCCCHHHE
29.1222210691
375PhosphorylationLTPMTAGSRQHALSV
EEECCCCCHHHEECC
26.7222210691
413PhosphorylationAMKGMTSSEPISIME
HHCCCCCCCCCCCHH
37.9228176443
417PhosphorylationMTSSEPISIMEKTQP
CCCCCCCCCHHCCCC
26.9728176443
432PhosphorylationMKVQVECSRGVDIKA
CEEEEEECCCCCCCC
20.6822985185
458AcetylationIGIANFVKVRAFLEV
EEHHHHHHHHHHHHH
23.1319813529
485PhosphorylationQISLVQYSRDPHTEF
EEEEEEECCCCCCCE
17.0822210691
490PhosphorylationQYSRDPHTEFTLKKF
EECCCCCCCEEECCC
37.8822210691
493PhosphorylationRDPHTEFTLKKFTKV
CCCCCCEEECCCCCH
31.2822210691
509PhosphorylationDIIEAINTFPYRGGS
HHHHHHHCCCCCCCC
21.6320068231
512PhosphorylationEAINTFPYRGGSTNT
HHHHCCCCCCCCCCC
20.0720068231
524PhosphorylationTNTGKAMTYVREKIF
CCCCCCCCEEEEEEE
24.5922210691
525PhosphorylationNTGKAMTYVREKIFV
CCCCCCCEEEEEEEC
5.6122210691
535AcetylationEKIFVPSKGSRSNVP
EEEECCCCCCCCCCC
55.637671041
535UbiquitinationEKIFVPSKGSRSNVP
EEEECCCCCCCCCCC
55.6329967540
549PhosphorylationPKVMILITDGKSSDA
CEEEEEEECCCCCHH
34.9420068231
689PhosphorylationSSTSVVLSSLKPETL
CCCEEEECCCCCCEE
23.2424719451
700N-linked_GlycosylationPETLYLVNVTAEYED
CCEEEEEEEEEEECC
23.87UniProtKB CARBOHYD
730UbiquitinationKGAPRNLKVTDETTD
CCCCCCCCCCCCCCC
46.7929967540
735PhosphorylationNLKVTDETTDSFKIT
CCCCCCCCCCCEEEE
38.4224719451
738PhosphorylationVTDETTDSFKITWTQ
CCCCCCCCEEEEEEC
26.7524719451
765PhosphorylationRPVAGGESREVTTPP
EECCCCCCCCCCCCC
36.70-
778PhosphorylationPPNQRRRTLENLIPD
CCCHHCHHHHHHCCC
36.2923312004
786PhosphorylationLENLIPDTKYEVSVI
HHHHCCCCCEEEEEC
30.1224719451
798O-linked_GlycosylationSVIPEYFSGPGTPLT
EECCHHHCCCCCCCC
43.08-
802PhosphorylationEYFSGPGTPLTGNAA
HHHCCCCCCCCCCCC
20.47-
856PhosphorylationTPVAGGETQEVTVRG
ECCCCCCEEEEEEEC
33.0524532841
860PhosphorylationGGETQEVTVRGDTTN
CCCEEEEEEECCCHH
12.0624532841
865PhosphorylationEVTVRGDTTNTVLQG
EEEEECCCHHHHHHH
25.4424532841
866PhosphorylationVTVRGDTTNTVLQGL
EEEECCCHHHHHHHH
33.3624532841
889O-linked_GlycosylationSVTALYASGAGDALF
EEEEHHHCCCCHHHC
18.67-
969PhosphorylationIENLQPETKYRISVF
HHHCCCCCCEEEEEE
39.8126699800
981O-linked_GlycosylationSVFATYSSGEGEPLT
EEEEEECCCCCCCCC
30.37-
1003UbiquitinationSQDSKTLKVDEETEN
CCCCCEEEECCCCCC
53.5229967540
1080PhosphorylationEGKLRQGSGTTASRF
CCCCCCCCCCCCHHC
25.3223403867
1082PhosphorylationKLRQGSGTTASRFKS
CCCCCCCCCCHHCCC
22.3823403867
1083PhosphorylationLRQGSGTTASRFKSP
CCCCCCCCCHHCCCC
26.5922210691
1085PhosphorylationQGSGTTASRFKSPRN
CCCCCCCHHCCCCCC
35.8422210691
1089PhosphorylationTTASRFKSPRNLKTS
CCCHHCCCCCCCCCC
26.7822468782
1099O-linked_GlycosylationNLKTSDPTMSSFRVT
CCCCCCCCCCCEEEE
34.3855834385
1106O-linked_GlycosylationTMSSFRVTWEPAPGE
CCCCEEEEEECCCCC
21.6151469513
1115UbiquitinationEPAPGEVKGYKVTFH
ECCCCCCCEEEEEEE
52.8229967540
1118UbiquitinationPGEVKGYKVTFHPTG
CCCCCEEEEEEECCC
43.3929967540
1120O-linked_GlycosylationEVKGYKVTFHPTGDD
CCCEEEEEEECCCCC
16.4555826501
1124O-linked_GlycosylationYKVTFHPTGDDRRLG
EEEEEECCCCCCCCC
44.6855826507
1180O-linked_GlycosylationEMTTLSDTTVMPILS
CEECCCCCCCHHHHC
20.22OGP
1181O-linked_GlycosylationMTTLSDTTVMPILSS
EECCCCCCCHHHHCC
21.57OGP
1213UbiquitinationGSWSIGRANFRTVRS
CCCCCCCCCHHHHHH
17.8229967540
1217PhosphorylationIGRANFRTVRSFISR
CCCCCHHHHHHHHHH
19.0122617229
1220PhosphorylationANFRTVRSFISRIVE
CCHHHHHHHHHHHHH
23.6924501219
1223PhosphorylationRTVRSFISRIVEVFD
HHHHHHHHHHHHHCC
17.5924719451
1261PhosphorylationNAHRDKKSLLQAVAN
CCCCCHHHHHHHHHC
39.8020068231
1271PhosphorylationQAVANLPYKGGNTLT
HHHHCCCCCCCCHHH
25.9822461510
1292PhosphorylationIRQQNFRTQAGMRPR
HHHCCHHHCCCCCCC
20.73-
1311UbiquitinationGVLITDGKSQDDVEA
EEEEECCCCHHCCCC
47.9929967540
1312PhosphorylationVLITDGKSQDDVEAP
EEEECCCCHHCCCCC
44.35-
1397PhosphorylationNLVISERTHRSFRVS
CEEEECCCCCCEEEE
20.00-
1415PhosphorylationPSDSVDRYKVEYYPV
CCCCCCEEEEEEEEC
18.2126657352
1419PhosphorylationVDRYKVEYYPVSGGK
CCEEEEEEEECCCCC
18.9626657352
1423PhosphorylationKVEYYPVSGGKRQEF
EEEEEECCCCCCEEE
37.0126657352
1433PhosphorylationKRQEFYVSRMETSTV
CCEEEEEEEEECCCH
17.96-
1438PhosphorylationYVSRMETSTVLKDLK
EEEEEECCCHHCCCC
11.83-
1441UbiquitinationRMETSTVLKDLKPET
EEECCCHHCCCCCCC
3.4629967540
1450PhosphorylationDLKPETEYVVNVYSV
CCCCCCEEEEEEEEE
19.67-
1452 (in isoform 2)Phosphorylation-3.82-
1511UbiquitinationILSYKPVKDTEPTRP
EEEEECCCCCCCCCC
68.4129967540
1526UbiquitinationKEVRLGPTVNDMQLT
CEEECCCCCCCCCHH
30.0929967540
1743PhosphorylationDLIGSERTLPILTTQ
CCCCCCCEECEEECC
32.6022673903
1748O-linked_GlycosylationERTLPILTTQAPKSG
CCEECEEECCCCCCC
19.9955832145
1748PhosphorylationERTLPILTTQAPKSG
CCEECEEECCCCCCC
19.9922673903
1749O-linked_GlycosylationRTLPILTTQAPKSGP
CEECEEECCCCCCCC
21.2055832151
1749PhosphorylationRTLPILTTQAPKSGP
CEECEEECCCCCCCC
21.2022673903
1763N-linked_GlycosylationPRNLQVYNATSNSLT
CCCEEEEECCCCEEE
37.57UniProtKB CARBOHYD
1788 (in isoform 2)Phosphorylation-19.47-
1853PhosphorylationTVRNLRVYDPSTSTL
CCEEEEEECCCCCEE
18.7224043423
1856PhosphorylationNLRVYDPSTSTLNVR
EEEEECCCCCEEEEE
31.9024043423
1857PhosphorylationLRVYDPSTSTLNVRW
EEEECCCCCEEEEEE
30.9924043423
1858PhosphorylationRVYDPSTSTLNVRWD
EEECCCCCEEEEEEE
34.9224043423
1859PhosphorylationVYDPSTSTLNVRWDH
EECCCCCEEEEEEEC
23.5724043423
1897PhosphorylationPIPGNTNYAILRNLQ
ECCCCCCEEEHHCCC
7.93-
1928PhosphorylationDGGRTSDTGRTLMRG
CCCCCCHHHHHHHHH
28.4722210691
2001PhosphorylationLIPDTLYSVNLVALY
HCCCCEEEEEEEEEE
13.9822210691
2008PhosphorylationSVNLVALYSDGEGNP
EEEEEEEECCCCCCC
8.5822210691
2016PhosphorylationSDGEGNPSPAQGRTL
CCCCCCCCCCCCCCC
36.5522210691
2062PhosphorylationYRIIYSPTVGDPIDE
EEEEECCCCCCCCHH
31.05-
2125PhosphorylationPPQNIHISDEWYTRF
CCCCEEECCCEEEEE
18.47-
2141PhosphorylationVSWDPSPSPVLGYKI
EECCCCCCCCCEEEE
31.7920068231
2146PhosphorylationSPSPVLGYKIVYKPV
CCCCCCEEEEEEECC
8.06-
2206N-linked_GlycosylationQGTTLYLNVTDLKTY
CCCEEEEECCCCCEE
22.53UniProtKB CARBOHYD
2231PhosphorylationWSPHRAATSYRLKLS
CCCCCCCCEEEEEEE
25.88-
22362-HydroxyisobutyrylationAATSYRLKLSPADGT
CCCEEEEEEECCCCC
37.61-
2238PhosphorylationTSYRLKLSPADGTRG
CEEEEEEECCCCCCC
19.2221406692
2243PhosphorylationKLSPADGTRGQEITV
EEECCCCCCCCEEEE
31.9721406692
2295O-linked_GlycosylationEHTTVKPTEAPTEPP
CCCCCCCCCCCCCCC
38.7855834627
2299O-linked_GlycosylationVKPTEAPTEPPTPPP
CCCCCCCCCCCCCCC
69.0855834633
2303O-linked_GlycosylationEAPTEPPTPPPPPTI
CCCCCCCCCCCCCCC
60.1755834639
2309O-linked_GlycosylationPTPPPPPTIPPARDV
CCCCCCCCCCCHHHH
52.4755834645
2377UbiquitinationDEVKSEFKLNTYNDK
HHHHHCEEECCCCHH
36.4529967540
2433PhosphorylationPKVLVVVTDGRSQDE
CEEEEEEECCCCHHH
22.56-
2437PhosphorylationVVVTDGRSQDEVKKA
EEEECCCCHHHHHHH
47.73-
2527PhosphorylationGFKMLEAYNLTEKNF
CCHHHHHCCCCCCCC
11.0029978859
2528N-linked_GlycosylationFKMLEAYNLTEKNFA
CHHHHHCCCCCCCCC
47.7519159218
2530PhosphorylationMLEAYNLTEKNFASV
HHHHCCCCCCCCCEE
41.0729978859
2536PhosphorylationLTEKNFASVQGVSLE
CCCCCCCEEECCEEC
15.73-
2541PhosphorylationFASVQGVSLESGSFP
CCEEECCEECCCCCC
32.99-
2591PhosphorylationRLLPETPSDPFAIWQ
ECCCCCCCCCCCEEE
66.39-
2605UbiquitinationQITDRDYKPQVGVIA
EEECCCCCCCCEEEE
33.0129967540
2615PhosphorylationVGVIADPSSKTLSFF
CEEEECCCCCCEEEC
45.0420068231
2616PhosphorylationGVIADPSSKTLSFFN
EEEECCCCCCEEECC
34.7420068231
2675UbiquitinationEIIEKDIKEAGNITT
HHHHHHHHHHCCCCC
52.2029967540
2679N-linked_GlycosylationKDIKEAGNITTDGYE
HHHHHHCCCCCCHHH
35.1719159218
2690UbiquitinationDGYEILGKLLKGERK
CHHHHHHHHHCCCCC
47.3929967540
2861PhosphorylationGPPGPPGSPGSPGVT
CCCCCCCCCCCCCCC
31.6825159151
2864PhosphorylationGPPGSPGSPGVTGPS
CCCCCCCCCCCCCCC
23.1225159151
2944HydroxylationSRNQPGPPGPPGPPG
HCCCCCCCCCCCCCC
74.06-
2947HydroxylationQPGPPGPPGPPGSAG
CCCCCCCCCCCCCCC
74.06-
2950HydroxylationPPGPPGPPGSAGARG
CCCCCCCCCCCCCCC
56.11-
2952PhosphorylationGPPGPPGSAGARGEP
CCCCCCCCCCCCCCC
29.3320068231
2959HydroxylationSAGARGEPGPGGRPG
CCCCCCCCCCCCCCC
58.04-
2965HydroxylationEPGPGGRPGFPGTPG
CCCCCCCCCCCCCCC
52.64-
2968HydroxylationPGGRPGFPGTPGMQG
CCCCCCCCCCCCCCC
52.22-
2971HydroxylationRPGFPGTPGMQGPPG
CCCCCCCCCCCCCCC
42.02-
2983HydroxylationPPGERGLPGEKGERG
CCCCCCCCCCCCCCC
52.28-
2994PhosphorylationGERGTGSSGPRGLPG
CCCCCCCCCCCCCCC
54.91-
3000HydroxylationSSGPRGLPGPPGPQG
CCCCCCCCCCCCCCC
56.95-
3003HydroxylationPRGLPGPPGPQGESR
CCCCCCCCCCCCCCC
73.36-
3014HydroxylationGESRTGPPGSTGSRG
CCCCCCCCCCCCCCC
51.19-
3023HydroxylationSTGSRGPPGPPGRPG
CCCCCCCCCCCCCCC
71.41-
3026HydroxylationSRGPPGPPGRPGNSG
CCCCCCCCCCCCCCC
58.29-
3029HydroxylationPPGPPGRPGNSGIRG
CCCCCCCCCCCCCCC
52.84-
3043PhosphorylationGPPGPPGYCDSSQCA
CCCCCCCCCCHHHCC
10.00-
3062PhosphorylationNGQGYPGSG------
CCCCCCCCC------
36.50-

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 COCA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COCA1_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 COCA1_HUMAN !!

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

Oops, there are no PPI records of COCA1_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 COCA1_HUMAN

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Related Literatures of Post-Translational Modification
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-2528 AND ASN-2679, ANDMASS SPECTROMETRY.

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