PCSK5_MOUSE - dbPTM
PCSK5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCSK5_MOUSE
UniProt AC Q04592
Protein Name Proprotein convertase subtilisin/kexin type 5
Gene Name Pcsk5
Organism Mus musculus (Mouse).
Sequence Length 1877
Subcellular Localization Isoform PC5A: Secreted. Secreted through the regulated secretory pathway.
Isoform PC5B: Endomembrane system
Single-pass type I membrane protein. Type I membrane protein localized to a paranuclear post-Golgi network compartment in communication
Protein Description Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive and regulated secretory pathways. Plays an essential role in pregnancy establishment by proteolytic activation of a number of important factors such as BMP2, CALD1 and alpha-integrins. May be responsible for the maturation of gastrointestinal peptides. May be involved in the cellular proliferation of adrenal cortex via the activation of growth factors..
Protein Sequence MDWDWGNRCSRPGRRDLLCVLALLAGCLLPVCRTRVYTNHWAVKIAGGFAEADRIASKYGFINVGQIGALKDYYHFYHSRTIKRSVLSSRGTHSFISMEPKVEWIQQQVVKKRTKRDYDLSHAQSTYFNDPKWPSMWYMHCSDNTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRYDASNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGKTVDGPAPLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGESYDKKIITTDLRQRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRAGHLNANDWKTNAAGFKVSHLYGFGLMDAEAMVMEAEKWTTVPQQHVCVESTDRQIKTIRPNSAVRSIYKASGCSDNPNHHVNYLEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTPSQLRNFKTPGKLKEWSLVLYGTSVQPYSPTNEFPKVERFRYSRVEDPTDDYGAEDYAGPCDPECSEVGCDGPGPDHCSDCLHYYYKLKNNTRICVSSCPPGHYHADKKRCRKCAPNCESCFGSHGNQCLSCKYGYFLNEETSSCVTQCPDGSYEDIKKNVCGKCSENCKACIGFHNCTECKGGLSLQGSRCSVTCEDGQFFNGHDCQPCHRFCATCSGAGADGCINCTEGYVMEEGRCVQSCSVSYYLDHSSEGGYKSCKRCDNSCLTCNGPGFKNCSSCPSGYLLDLGTCQMGAICKDGEYIDDQGHCQTCEASCAKCWGPTQEDCISCPVTRVLDDGRCVMNCPSWKFEFKKQCHPCHYTCQGCQGSGPSNCTSCRADKHGQERFLYHGECLENCPVGHYPAKGHACLPCPDNCELCYNPHVCSRCMSGYVIIPPNHTCQKLECRQGEFQDSEYEECMPCEEGCLGCTEDDPGACTSCATGYYMFERHCYKACPEKTFGVKWECRACGTNCGSCDQHECYWCEEGFFLSGGSCVQDCGPGFHGDQELGECKPCHRACENCTGSGYNQCSSCQEGLQLWHGTCLWSTWPQVEGKDWNEAVPTEKPSLVRSLLQDRRKWKVQIKRDATSQNQPCHSSCKTCNGSLCASCPTGMYLWLQACVPSCPQGTWPSVTSGSCEKCSEDCVSCSGADLCQQCLSQPDNTLLLHEGRCYHSCPEGFYAKDGVCEHCSSPCKTCEGNATSCNSCEGDFVLDHGVCWKTCPEKHVAVEGVCKHCPERCQDCIHEKTCKECMPDFFLYNDMCHRSCPKSFYPDMRQCVPCHKNCLECNGPKEDDCKVCADTSKALHNGLCLDECPEGTYKEEENDECRDCPESCLICSSAWTCLACREGFTVVHDVCTAPKECAAVEYWDEGSHRCQPCHKKCSRCSGPSEDQCYTCPRETFLLNTTCVKECPEGYHTDKDSQQCVLCHSSCRTCEGPHSMQCLSCRPGWFQLGKECLLQCRDGYYGESTSGRCEKCDKSCKSCRGPRPTDCQSCDTFFFLLRSKGQCHRACPEHYYADQHAQTCERCHPTCDKCSGKEAWSCLSCVWSYHLLKGICIPECIVGEYREGKGENFNCKKCHESCMECKGPGSKNCTGCSAGLLLDMDDNRCLHCCNASHSRRSQDCCDCQSSTDECILPAREAEFYEHTKTALLVTSGAMLLLLLGAAAVVWRKSRSRPVAKGRYEKLAEPTVSYSSYRSSYLDEDQVIEYRDRDYDEDDEDDIVYMGQDGTVYRKFKYGLLDETEDDELEYDDESYSYQ
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
88PhosphorylationTIKRSVLSSRGTHSF
CCHHHHHHCCCCCCC
18.8121743459
89PhosphorylationIKRSVLSSRGTHSFI
CHHHHHHCCCCCCCC
30.4821743459
227N-linked_GlycosylationGEVAATANNSHCTVG
HHHHHHCCCCCCEEE
46.30-
319PhosphorylationASGNGGRSKDHCSCD
ECCCCCCCCCCEECC
45.7924759943
324PhosphorylationGRSKDHCSCDGYTNS
CCCCCCEECCCCCCE
16.3024759943
329PhosphorylationHCSCDGYTNSIYTIS
CEECCCCCCEEEEEE
28.1924759943
331PhosphorylationSCDGYTNSIYTISIS
ECCCCCCEEEEEEEE
14.7924759943
333PhosphorylationDGYTNSIYTISISST
CCCCCEEEEEEEEEC
9.6124759943
383N-linked_GlycosylationLRQRCTDNHTGTSAS
HHHHHCCCCCCCCCC
19.23-
515PhosphorylationEHVVVRITITHPRRG
EEEEEEEEECCCCCC
14.8422006019
517PhosphorylationVVVRITITHPRRGDL
EEEEEEECCCCCCCE
19.7122006019
667N-linked_GlycosylationHYYYKLKNNTRICVS
HHHHCCCCCCEEEEE
66.59-
754N-linked_GlycosylationKACIGFHNCTECKGG
CCEEEECCCCCCCCC
31.95-
804N-linked_GlycosylationAGADGCINCTEGYVM
CCCCCCEECCCCEEE
30.63-
854N-linked_GlycosylationCNGPGFKNCSSCPSG
CCCCCCCCCCCCCCC
28.74-
951N-linked_GlycosylationCQGSGPSNCTSCRAD
CCCCCCCCCCCCCCC
35.90-
980PhosphorylationENCPVGHYPAKGHAC
HCCCCCCCCCCCCCC
10.0429899451
1016N-linked_GlycosylationGYVIIPPNHTCQKLE
CEEEECCCCCCCEEE
37.43-
1220N-linked_GlycosylationHSSCKTCNGSLCASC
CCCCCCCCCCEECCC
48.60-
1317N-linked_GlycosylationPCKTCEGNATSCNSC
CCCCCCCCCCCCCCC
20.11-
1523N-linked_GlycosylationPRETFLLNTTCVKEC
CCCEEEEECEEECCC
35.17-
1583PhosphorylationLLQCRDGYYGESTSG
HHCCCCCCCCCCCCC
16.7621659605
1711N-linked_GlycosylationCKGPGSKNCTGCSAG
CCCCCCCCCCCCCCE
30.22-
1733N-linked_GlycosylationNRCLHCCNASHSRRS
CCCCCCCCCCCCCCC
50.28-
1804UbiquitinationVAKGRYEKLAEPTVS
CCCCCHHHHCCCCCC
44.0222790023
1833PhosphorylationIEYRDRDYDEDDEDD
EEECCCCCCCCCCCC
23.33-
1843PhosphorylationDDEDDIVYMGQDGTV
CCCCCEEEECCCCCE
8.89-
1849PhosphorylationVYMGQDGTVYRKFKY
EEECCCCCEEEEECC
23.74-
1851PhosphorylationMGQDGTVYRKFKYGL
ECCCCCEEEEECCCC
14.13-

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 PCSK5_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCSK5_MOUSE !!

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 PCSK5_MOUSE !!

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

Oops, there are no PPI records of PCSK5_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCSK5_MOUSE

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Related Literatures of Post-Translational Modification

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