BRNP2_HUMAN - dbPTM
BRNP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRNP2_HUMAN
UniProt AC Q9C0B6
Protein Name BMP/retinoic acid-inducible neural-specific protein 2
Gene Name BRINP2
Organism Homo sapiens (Human).
Sequence Length 783
Subcellular Localization Secreted .
Protein Description Inhibits neuronal cell proliferation by negative regulation of the cell cycle transition..
Protein Sequence MRWQCGTRFRGLRPAVAPWTALLALGLPGWVLAVSATAAAVVPEQHASVAGQHPLDWLLTDRGPFHRAQEYADFMERYRQGFTTRYRIYREFARWKVNNLALERKDFFSLPLPLAPEFIRNIRLLGRRPNLQQVTENLIKKYGTHFLLSATLGGEESLTIFVDKQKLGRKTETTGGASIIGGSGNSTAVSLETLHQLAASYFIDRESTLRRLHHIQIATGAIKVTETRTGPLGCSNYDNLDSVSSVLVQSPENKVQLLGLQVLLPEYLRERFVAAALSYITCSSEGELVCKENDCWCKCSPTFPECNCPDADIQAMEDSLLQIQDSWATHNRQFEESEEFQALLKRLPDDRFLNSTAISQFWAMDTSLQHRYQQLGAGLKVLFKKTHRILRRLFNLCKRCHRQPRFRLPKERSLSYWWNRIQSLLYCGESTFPGTFLEQSHSCTCPYDQSSCQGPIPCALGEGPACAHCAPDNSTRCGSCNPGYVLAQGLCRPEVAESLENFLGLETDLQDLELKYLLQKQDSRIEVHSIFISNDMRLGSWFDPSWRKRMLLTLKSNKYKPGLVHVMLALSLQICLTKNSTLEPVMAIYVNPFGGSHSESWFMPVNEGSFPDWERTNVDAAAQCQNWTITLGNRWKTFFETVHVYLRSRIKSLDDSSNETIYYEPLEMTDPSKNLGYMKINTLQVFGYSLPFDPDAIRDLILQLDYPYTQGSQDSALLQLIELRDRVNQLSPPGKVRLDLFSCLLRHRLKLANNEVGRIQSSLRAFNSKLPNPVEYETGKLCS
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
78PhosphorylationYADFMERYRQGFTTR
HHHHHHHHHCCCCHH
24043423
83PhosphorylationERYRQGFTTRYRIYR
HHHHCCCCHHHHHHH
24043423
84PhosphorylationRYRQGFTTRYRIYRE
HHHCCCCHHHHHHHH
24043423
151PhosphorylationTHFLLSATLGGEESL
CEEEEEEECCCCCEE
-
157PhosphorylationATLGGEESLTIFVDK
EECCCCCEEEEEECH
-
185N-linked_GlycosylationSIIGGSGNSTAVSLE
EEECCCCCCCEECHH
UniProtKB CARBOHYD
240UbiquitinationGCSNYDNLDSVSSVL
CCCCCCCCCCCCEEE
20972266
354N-linked_GlycosylationLPDDRFLNSTAISQF
CCCCCCCCHHHHHHH
UniProtKB CARBOHYD
473N-linked_GlycosylationCAHCAPDNSTRCGSC
CCCCCCCCCCCCCCC
UniProtKB CARBOHYD
545PhosphorylationLGSWFDPSWRKRMLL
CCCCCCHHHHHHHHH
26091039
555UbiquitinationKRMLLTLKSNKYKPG
HHHHHHHHCCCCCCC
20972266
579N-linked_GlycosylationLQICLTKNSTLEPVM
HHHHHCCCCCCCCEE
UniProtKB CARBOHYD
626N-linked_GlycosylationDAAAQCQNWTITLGN
HHHHHHCCEEEEECH
UniProtKB CARBOHYD
658N-linked_GlycosylationKSLDDSSNETIYYEP
HCCCCCCCCEEEEEE
UniProtKB CARBOHYD

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 BRNP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRNP2_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 BRNP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RDH14_HUMANRDH14physical
28514442
AT5G1_HUMANATP5G1physical
28514442
CALX_HUMANCANXphysical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
EDEM2_HUMANEDEM2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRNP2_HUMAN

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Related Literatures of Post-Translational Modification

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