RISC_HUMAN - dbPTM
RISC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RISC_HUMAN
UniProt AC Q9HB40
Protein Name Retinoid-inducible serine carboxypeptidase
Gene Name SCPEP1
Organism Homo sapiens (Human).
Sequence Length 452
Subcellular Localization Secreted .
Protein Description May be involved in vascular wall and kidney homeostasis..
Protein Sequence MELALRRSPVPRWLLLLPLLLGLNAGAVIDWPTEEGKEVWDYVTVRKDAYMFWWLYYATNSCKNFSELPLVMWLQGGPGGSSTGFGNFEEIGPLDSDLKPRKTTWLQAASLLFVDNPVGTGFSYVNGSGAYAKDLAMVASDMMVLLKTFFSCHKEFQTVPFYIFSESYGGKMAAGIGLELYKAIQRGTIKCNFAGVALGDSWISPVDSVLSWGPYLYSMSLLEDKGLAEVSKVAEQVLNAVNKGLYREATELWGKAEMIIEQNTDGVNFYNILTKSTPTSTMESSLEFTQSHLVCLCQRHVRHLQRDALSQLMNGPIRKKLKIIPEDQSWGGQATNVFVNMEEDFMKPVISIVDELLEAGINVTVYNGQLDLIVDTMGQEAWVRKLKWPELPKFSQLKWKALYSDPKSLETSAFVKSYKNLAFYWILKAGHMVPSDQGDMALKMMRLVTQQE
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
42PhosphorylationEGKEVWDYVTVRKDA
CCCCEEEEEEEECHH
5.15-
64N-linked_GlycosylationYATNSCKNFSELPLV
HHHCCCCCHHHCCEE
50.43UniProtKB CARBOHYD
126N-linked_GlycosylationGTGFSYVNGSGAYAK
CCCCCEECCCCCHHH
30.5812754519
126N-linked_GlycosylationGTGFSYVNGSGAYAK
CCCCCEECCCCCHHH
30.5812754519
243UbiquitinationQVLNAVNKGLYREAT
HHHHHHHHCHHHHHH
43.6321890473
243 (in isoform 1)Ubiquitination-43.6321890473
243 (in isoform 2)Ubiquitination-43.6321890473
280O-linked_GlycosylationLTKSTPTSTMESSLE
EECCCCCCCCHHHHH
27.2829351928
281O-linked_GlycosylationTKSTPTSTMESSLEF
ECCCCCCCCHHHHHH
27.6929351928
362N-linked_GlycosylationELLEAGINVTVYNGQ
HHHHCCCCEEEECCE
23.61UniProtKB CARBOHYD
400UbiquitinationKFSQLKWKALYSDPK
CCCHHCHHHHHCCCC
27.25-
404PhosphorylationLKWKALYSDPKSLET
HCHHHHHCCCCCCCH
48.57-
407UbiquitinationKALYSDPKSLETSAF
HHHHCCCCCCCHHHH
73.07-
4072-HydroxyisobutyrylationKALYSDPKSLETSAF
HHHHCCCCCCCHHHH
73.07-
408PhosphorylationALYSDPKSLETSAFV
HHHCCCCCCCHHHHH
36.50-
411PhosphorylationSDPKSLETSAFVKSY
CCCCCCCHHHHHHHH
30.56-
416UbiquitinationLETSAFVKSYKNLAF
CCHHHHHHHHHHHHH
41.43-

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 RISC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RISC_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 RISC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBA1A_HUMANTUBA1Aphysical
22863883
TBB5_HUMANTUBBphysical
22863883
XPO1_HUMANXPO1physical
22863883
1433E_HUMANYWHAEphysical
22863883
CD2AP_HUMANCD2APphysical
26344197
PRDX6_HUMANPRDX6physical
26344197
ZN507_HUMANZNF507physical
28514442

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 RISC_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-126.

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