C19L2_HUMAN - dbPTM
C19L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C19L2_HUMAN
UniProt AC Q2TBE0
Protein Name CWF19-like protein 2
Gene Name CWF19L2
Organism Homo sapiens (Human).
Sequence Length 894
Subcellular Localization
Protein Description
Protein Sequence MATSMAAASGRFESAKSIEERKEQTRNARAEVLRQAKANFEKEERRKELKRLRGEDTWMLPDVNERIEQFSQEHSVKKKKKKDKHSKKAKKEKKKKSKKQKYEKNNESSDSSSSSEDEWVEAVPSQTPDKEKAWKVKDEKSGKDDTQIIKRDEWMTVDFMSVKTVSSSSLKAEKETMRKIEQEKNQALEQSKLMERELNPYWKDGGTGLPPEDCSVSSITKVSVVEDGGLSWLRKSYLRMKEQAEKQSRNFEDIVAERYGSMEIFQSKLEDAEKAASTKEDYRRERWRKPTYSDKAQNCQESRESDLVKYGNSSRDRYATTDTAKNSNNEKFIGDEKDKRPGSLETCRRESNPRQNQEFSFGNLRAKFLRPSDDEELSFHSKGRKFEPLSSSSALVAQGSLCSGFRKPTKNSEERLTSWSRSDGRGDKKHSNQKPSETSTDEHQHVPEDPREKSQDEVLRDDPPKKEHLRDTKSTFAGSPERESIHILSVDEKNKLGAKIIKAEMMGNMELAEQLKVQLEKANKFKETITQIPKKSGVENEDQQEVILVRTDQSGRVWPVNTPGKSLESQGGRRKRQMVSTHEERERVRYFHDDDNLSLNDLVKNEKMGTAENQNKLFMRMASKFMGKTDGDYYTLDDMFVSKAAERERLGEEEENQRKKAIAEHRSLAAQMEKCLYCFDSSQFPKHLIVAIGVKVYLCLPNVRSLTEGHCLIVPLQHHRAATLLDEDIWEEIQMFRKSLVKMFEDKGLDCIFLETNMSMKKQYHMVYECIPLPKEVGDMAPIYFKKAIMESDEEWSMNKKLIDLSSKDIRKSVPRGLPYFSVDFGLHGGFAHVIEDQHKFPHYFGKEIIGGMLDIEPRLWRKGIRESFEDQRKKALQFAQWWKPYDFTKSKNY
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
9PhosphorylationATSMAAASGRFESAK
CCHHHHHHCCCHHHH
26.27-
16AcetylationSGRFESAKSIEERKE
HCCCHHHHHHHHHHH
62.3325953088
17PhosphorylationGRFESAKSIEERKEQ
CCCHHHHHHHHHHHH
34.6426091039
34MethylationNARAEVLRQAKANFE
HHHHHHHHHHHHHCC
39.32-
37UbiquitinationAEVLRQAKANFEKEE
HHHHHHHHHHCCHHH
35.2129967540
71PhosphorylationNERIEQFSQEHSVKK
HHHHHHHHHHHHHHH
34.0620068231
75PhosphorylationEQFSQEHSVKKKKKK
HHHHHHHHHHHHHHH
34.5725159151
102PhosphorylationKKSKKQKYEKNNESS
HHHHHHHHHHCCCCC
29.6427134283
108PhosphorylationKYEKNNESSDSSSSS
HHHHCCCCCCCCCCC
41.3830576142
109PhosphorylationYEKNNESSDSSSSSE
HHHCCCCCCCCCCCH
35.0230576142
115PhosphorylationSSDSSSSSEDEWVEA
CCCCCCCCHHHHHHC
51.52-
127PhosphorylationVEAVPSQTPDKEKAW
HHCCCCCCCCHHHCC
37.4827134283
161PhosphorylationWMTVDFMSVKTVSSS
CEEEEEEEEEECCHH
22.0624719451
163UbiquitinationTVDFMSVKTVSSSSL
EEEEEEEEECCHHHH
35.58-
168PhosphorylationSVKTVSSSSLKAEKE
EEEECCHHHHHHHHH
31.9825690035
169PhosphorylationVKTVSSSSLKAEKET
EEECCHHHHHHHHHH
35.5225690035
171SumoylationTVSSSSLKAEKETMR
ECCHHHHHHHHHHHH
57.3528112733
176PhosphorylationSLKAEKETMRKIEQE
HHHHHHHHHHHHHHH
33.0923401153
184UbiquitinationMRKIEQEKNQALEQS
HHHHHHHHHHHHHHH
54.79-
192UbiquitinationNQALEQSKLMERELN
HHHHHHHHHHHHHCC
52.1029967540
203UbiquitinationRELNPYWKDGGTGLP
HHCCCCCCCCCCCCC
40.4229967540
223PhosphorylationVSSITKVSVVEDGGL
CCCCEEEEEEECCCC
23.2326074081
231PhosphorylationVVEDGGLSWLRKSYL
EEECCCCHHHHHHHH
27.6026074081
261PhosphorylationIVAERYGSMEIFQSK
HHHHHHCCHHHHHHH
12.3328555341
268UbiquitinationSMEIFQSKLEDAEKA
CHHHHHHHHHHHHHH
45.1529967540
291PhosphorylationRERWRKPTYSDKAQN
HHHHCCCCCCHHHHH
38.4026657352
309UbiquitinationSRESDLVKYGNSSRD
HHHHHHHHCCCCCCC
55.5329967540
310PhosphorylationRESDLVKYGNSSRDR
HHHHHHHCCCCCCCC
17.66-
343PhosphorylationEKDKRPGSLETCRRE
CCCCCCCCHHHHHHC
26.2220873877
346PhosphorylationKRPGSLETCRRESNP
CCCCCHHHHHHCCCC
19.3323882029
351PhosphorylationLETCRRESNPRQNQE
HHHHHHCCCCCCCCC
50.7729214152
360PhosphorylationPRQNQEFSFGNLRAK
CCCCCCCCCCCEEEE
31.3423917254
367AcetylationSFGNLRAKFLRPSDD
CCCCEEEEECCCCCC
38.2025953088
372PhosphorylationRAKFLRPSDDEELSF
EEEECCCCCCCCCCC
51.7825159151
378PhosphorylationPSDDEELSFHSKGRK
CCCCCCCCCCCCCCC
24.9620873877
381PhosphorylationDEELSFHSKGRKFEP
CCCCCCCCCCCCCCC
34.4927080861
382UbiquitinationEELSFHSKGRKFEPL
CCCCCCCCCCCCCCC
54.91-
390PhosphorylationGRKFEPLSSSSALVA
CCCCCCCCCCHHHHH
38.6020562096
391PhosphorylationRKFEPLSSSSALVAQ
CCCCCCCCCHHHHHC
35.6720562096
392PhosphorylationKFEPLSSSSALVAQG
CCCCCCCCHHHHHCC
19.0920562096
393PhosphorylationFEPLSSSSALVAQGS
CCCCCCCHHHHHCCC
27.80-
400PhosphorylationSALVAQGSLCSGFRK
HHHHHCCCCCCCCCC
17.7020562096
403PhosphorylationVAQGSLCSGFRKPTK
HHCCCCCCCCCCCCC
46.3818491316
409PhosphorylationCSGFRKPTKNSEERL
CCCCCCCCCCCHHHH
45.98-
412PhosphorylationFRKPTKNSEERLTSW
CCCCCCCCHHHHHHC
42.25-
436PhosphorylationKHSNQKPSETSTDEH
CCCCCCCCCCCCCCC
61.6230576142
439PhosphorylationNQKPSETSTDEHQHV
CCCCCCCCCCCCCCC
29.7928555341
440PhosphorylationQKPSETSTDEHQHVP
CCCCCCCCCCCCCCC
53.4830576142
454PhosphorylationPEDPREKSQDEVLRD
CCCCCCCCHHHHHHC
37.8025159151
472PhosphorylationKKEHLRDTKSTFAGS
CHHHHCCCCCCCCCC
22.0626074081
474PhosphorylationEHLRDTKSTFAGSPE
HHHCCCCCCCCCCCC
30.7423927012
475PhosphorylationHLRDTKSTFAGSPER
HHCCCCCCCCCCCCC
21.0423927012
479PhosphorylationTKSTFAGSPERESIH
CCCCCCCCCCCCCEE
21.8429255136
484PhosphorylationAGSPERESIHILSVD
CCCCCCCCEEEEECC
26.2023927012
489PhosphorylationRESIHILSVDEKNKL
CCCEEEEECCCCCCH
27.2423927012
499UbiquitinationEKNKLGAKIIKAEMM
CCCCHHHHHHHHHHH
43.0729967540
521AcetylationQLKVQLEKANKFKET
HHHHHHHHHHHHHHH
66.8925953088
535UbiquitinationTITQIPKKSGVENED
HHHHCCHHHCCCCCC
47.2729967540
562PhosphorylationGRVWPVNTPGKSLES
CCEEECCCCCCCHHH
33.3821815630
565UbiquitinationWPVNTPGKSLESQGG
EECCCCCCCHHHCCC
53.7429967540
580PhosphorylationRRKRQMVSTHEERER
HHCCCCCCCHHHHHH
20.7823186163
581PhosphorylationRKRQMVSTHEERERV
HCCCCCCCHHHHHHH
23.1523186163
598PhosphorylationFHDDDNLSLNDLVKN
CCCCCCCCHHHHHHH
31.2320873877
604UbiquitinationLSLNDLVKNEKMGTA
CCHHHHHHHCCCCCH
67.6829967540
604SumoylationLSLNDLVKNEKMGTA
CCHHHHHHHCCCCCH
67.6828112733
604SumoylationLSLNDLVKNEKMGTA
CCHHHHHHHCCCCCH
67.68-
610PhosphorylationVKNEKMGTAENQNKL
HHHCCCCCHHHHHHH
27.5730622161
623PhosphorylationKLFMRMASKFMGKTD
HHHHHHHHHHCCCCC
19.6528985074
624AcetylationLFMRMASKFMGKTDG
HHHHHHHHHCCCCCC
29.8125953088
629PhosphorylationASKFMGKTDGDYYTL
HHHHCCCCCCCEECH
39.21-
633PhosphorylationMGKTDGDYYTLDDMF
CCCCCCCEECHHHHH
12.1328796482
634PhosphorylationGKTDGDYYTLDDMFV
CCCCCCEECHHHHHH
12.9327642862
643UbiquitinationLDDMFVSKAAERERL
HHHHHHHHHHHHHHH
46.4429967540
742UbiquitinationMFRKSLVKMFEDKGL
HHHHHHHHHHHHCCC
43.0729967540
759PhosphorylationIFLETNMSMKKQYHM
EEEECCCCHHHHCCE
29.5324719451
764PhosphorylationNMSMKKQYHMVYECI
CCCHHHHCCEEEEEE
10.7727134283
768PhosphorylationKKQYHMVYECIPLPK
HHHCCEEEEEEECCC
9.4827134283
786UbiquitinationDMAPIYFKKAIMESD
CCCCEEHHHHHHHCC
25.0729967540
792PhosphorylationFKKAIMESDEEWSMN
HHHHHHHCCHHHHCC
32.70-
797PhosphorylationMESDEEWSMNKKLID
HHCCHHHHCCHHHHC
18.76-

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 C19L2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C19L2_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 C19L2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
FAM9B_HUMANFAM9Bphysical
25416956
CCD57_HUMANCCDC57physical
25416956
BRCA1_HUMANBRCA1physical
25184681

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 C19L2_HUMAN

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Related Literatures of Post-Translational Modification
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 SER-479, 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-479, AND MASSSPECTROMETRY.

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