SCG2_HUMAN - dbPTM
SCG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCG2_HUMAN
UniProt AC P13521
Protein Name Secretogranin-2
Gene Name SCG2
Organism Homo sapiens (Human).
Sequence Length 617
Subcellular Localization Secreted. Neuroendocrine and endocrine secretory granules.
Protein Description Secretogranin-2 is a neuroendocrine secretory granule protein, which is the precursor for biologically active peptides..
Protein Sequence MAEAKTHWLGAALSLIPLIFLISGAEAASFQRNQLLQKEPDLRLENVQKFPSPEMIRALEYIENLRQQAHKEESSPDYNPYQGVSVPLQQKENGDESHLPERDSLSEEDWMRIILEALRQAENEPQSAPKENKPYALNSEKNFPMDMSDDYETQQWPERKLKHMQFPPMYEENSRDNPFKRTNEIVEEQYTPQSLATLESVFQELGKLTGPNNQKRERMDEEQKLYTDDEDDIYKANNIAYEDVVGGEDWNPVEEKIESQTQEEVRDSKENIEKNEQINDEMKRSGQLGIQEEDLRKESKDQLSDDVSKVIAYLKRLVNAAGSGRLQNGQNGERATRLFEKPLDSQSIYQLIEISRNLQIPPEDLIEMLKTGEKPNGSVEPERELDLPVDLDDISEADLDHPDLFQNRMLSKSGYPKTPGRAGTEALPDGLSVEDILNLLGMESAANQKTSYFPNPYNQEKVLPRLPYGAGRSRSNQLPKAAWIPHVENRQMAYENLNDKDQELGEYLARMLVKYPEIINSNQVKRVPGQGSSEDDLQEEEQIEQAIKEHLNQGSSQETDKLAPVSKRFPVGPPKNDDTPNRQYWDEDLLMKVLEYLNQEKAEKGREHIAKRAMENM
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
38UbiquitinationQRNQLLQKEPDLRLE
HHHHHHHHCCCCCHH		71.7923503661
49UbiquitinationLRLENVQKFPSPEMI
CCHHCHHHCCCHHHH		55.7623503661
49AcetylationLRLENVQKFPSPEMI
CCHHCHHHCCCHHHH		55.7621339330
97PhosphorylationQKENGDESHLPERDS
ECCCCCCCCCCCCCC		34.7624505115
104PhosphorylationSHLPERDSLSEEDWM
CCCCCCCCCCHHHHH		39.7626657352
106PhosphorylationLPERDSLSEEDWMRI
CCCCCCCCHHHHHHH		42.7829691806
127PhosphorylationQAENEPQSAPKENKP
HHCCCCCCCCCCCCC		58.2024505115
135PhosphorylationAPKENKPYALNSEKN
CCCCCCCCCCCCCCC		25.9022210691
148PhosphorylationKNFPMDMSDDYETQQ
CCCCCCCCCCCCCCC		24.0622210691
151SulfationPMDMSDDYETQQWPE
CCCCCCCCCCCCCCH		26.352745426
151SulfationPMDMSDDYETQQWPE
CCCCCCCCCCCCCCH		26.35-
153PhosphorylationDMSDDYETQQWPERK
CCCCCCCCCCCCHHH		21.6022210691
174PhosphorylationPPMYEENSRDNPFKR
CCCCCCCCCCCCCCH		44.27-
182PhosphorylationRDNPFKRTNEIVEEQ
CCCCCCHHHHHHHHH		37.4829978859
190PhosphorylationNEIVEEQYTPQSLAT
HHHHHHHCCHHHHHH		24.5429978859
191PhosphorylationEIVEEQYTPQSLATL
HHHHHHCCHHHHHHH		17.9729978859
194PhosphorylationEEQYTPQSLATLESV
HHHCCHHHHHHHHHH		22.6029978859
197PhosphorylationYTPQSLATLESVFQE
CCHHHHHHHHHHHHH		36.0329978859
200PhosphorylationQSLATLESVFQELGK
HHHHHHHHHHHHHHH		31.2029978859
259PhosphorylationPVEEKIESQTQEEVR
HHHHHHHHHHHHHHH		41.8424505115
261PhosphorylationEEKIESQTQEEVRDS
HHHHHHHHHHHHHHH		47.4224505115
268PhosphorylationTQEEVRDSKENIEKN
HHHHHHHHHHHHHHH		31.1629255136
285PhosphorylationINDEMKRSGQLGIQE
HCHHHHHHCCCCCCH		25.9326657352
349PhosphorylationPLDSQSIYQLIEISR
CCCCCHHHHHHHHHH		11.5228450419
355PhosphorylationIYQLIEISRNLQIPP
HHHHHHHHHHCCCCH		11.4328450419
378PhosphorylationTGEKPNGSVEPEREL
CCCCCCCCCCCCCCC		29.9223312004
395PhosphorylationPVDLDDISEADLDHP
CCCHHHCCCCCCCCH		33.4527732954
413PhosphorylationQNRMLSKSGYPKTPG
HHHHHHHCCCCCCCC		39.9422210691
415PhosphorylationRMLSKSGYPKTPGRA
HHHHHCCCCCCCCCC		14.5122210691
432PhosphorylationEALPDGLSVEDILNL
CCCCCCCCHHHHHHH		29.0526657352
451PhosphorylationSAANQKTSYFPNPYN
HHHCCCCCCCCCCCC		31.6326657352
452PhosphorylationAANQKTSYFPNPYNQ
HHCCCCCCCCCCCCH		28.4326657352
457PhosphorylationTSYFPNPYNQEKVLP
CCCCCCCCCHHHCCC		35.8026657352
461UbiquitinationPNPYNQEKVLPRLPY
CCCCCHHHCCCCCCC		39.0323503661
468PhosphorylationKVLPRLPYGAGRSRS
HCCCCCCCCCCCCCC		24.9728331001
494PhosphorylationVENRQMAYENLNDKD
CCHHHHHHHHCCHHH		10.4622817900
507PhosphorylationKDQELGEYLARMLVK
HHHHHHHHHHHHHHH		12.1222817900
521PhosphorylationKYPEIINSNQVKRVP
HCHHHCCCCCCCCCC		20.4522461510
525UbiquitinationIINSNQVKRVPGQGS
HCCCCCCCCCCCCCC		37.6023503661
532PhosphorylationKRVPGQGSSEDDLQE
CCCCCCCCCHHHHHH		23.7522617229
533PhosphorylationRVPGQGSSEDDLQEE
CCCCCCCCHHHHHHH		52.4421082442
555PhosphorylationKEHLNQGSSQETDKL
HHHHHCCCCCCCHHC		21.0526657352
556PhosphorylationEHLNQGSSQETDKLA
HHHHCCCCCCCHHCC		38.5726657352
559PhosphorylationNQGSSQETDKLAPVS
HCCCCCCCHHCCCCH		30.6926657352
596PhosphorylationLLMKVLEYLNQEKAE
HHHHHHHHHHHHHHH		13.5422817900
601UbiquitinationLEYLNQEKAEKGREH
HHHHHHHHHHHHHHH		52.6723503661
604UbiquitinationLNQEKAEKGREHIAK
HHHHHHHHHHHHHHH		69.0323503661
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 SCG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCG2_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 SCG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBB4B_HUMANTUBB4Bphysical
21988832
ATRIP_HUMANATRIPphysical
25416956
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 SCG2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532 AND SER-533, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory