BRNP1_HUMAN - dbPTM
BRNP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRNP1_HUMAN
UniProt AC O60477
Protein Name BMP/retinoic acid-inducible neural-specific protein 1
Gene Name BRINP1
Organism Homo sapiens (Human).
Sequence Length 761
Subcellular Localization Cytoplasm .
Protein Description Inhibits cell proliferation by negative regulation of the G1/S transition. Mediates cell death which is not of the classical apoptotic type and regulates expression of components of the plasminogen pathway..
Protein Sequence MNWRFVELLYFLFIWGRISVQPSHQEPAGTDQHVSKEFDWLISDRGPFHHSRSYLSFVERHRQGFTTRYKIYREFARWKVRNTAIERRDLVRHPVPLMPEFQRSIRLLGRRPTTQQFIDTIIKKYGTHLLISATLGGEEALTMYMDKSRLDRKSGNATQSVEALHQLASSYFVDRDGTMRRLHEIQISTGAIKVTETRTGPLGCNSYDNLDSVSSVLLQSTESKLHLQGLQIIFPQYLQEKFVQSALSYIMCNGEGEYLCQNSQCRCQCAEEFPQCNCPITDIQIMEYTLANMAKSWAEAYKDLENSDEFKSFMKRLPSNHFLTIGSIHQHWGNDWDLQNRYKLLQSATEAQRQKIQRTARKLFGLSVRCRHNPNHQLPRERTIQQWLARVQSLLYCNENGFWGTFLESQRSCVCHGSTTLCQRPIPCVIGGNNSCAMCSLANISLCGSCNKGYKLYRGRCEPQNVDSERSEQFISFETDLDFQDLELKYLLQKMDSRLYVHTTFISNEIRLDTFFDPRWRKRMSLTLKSNKNRMDFIHMVIGMSMRICQMRNSSLDPMFFVYVNPFSGSHSEGWNMPFGEFGYPRWEKIRLQNSQCYNWTLLLGNRWKTFFETVHIYLRSRTRLPTLLRNETGQGPVDLSDPSKRQFYIKISDVQVFGYSLRFNADLLRSAVQQVNQSYTQGGQFYSSSSVMLLLLDIRDRINRLAPPVAPGKPQLDLFSCMLKHRLKLTNSEIIRVNHALDLYNTEILKQSDQMTAKLC
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
66PhosphorylationERHRQGFTTRYKIYR
HHHCCCCCHHHHHHH
-
104O-linked_GlycosylationLMPEFQRSIRLLGRR
CCHHHHHHHHHHCCC
30379171
132PhosphorylationYGTHLLISATLGGEE
HCCEEEEEEEECCHH
23532336
142PhosphorylationLGGEEALTMYMDKSR
ECCHHHHHHHHCHHH
23532336
156N-linked_GlycosylationRLDRKSGNATQSVEA
HCCCCCCCHHHHHHH
UniProtKB CARBOHYD
281PhosphorylationPQCNCPITDIQIMEY
CCCCCCCCCHHHHHH
24043423
288PhosphorylationTDIQIMEYTLANMAK
CCHHHHHHHHHHHHH
24043423
289PhosphorylationDIQIMEYTLANMAKS
CHHHHHHHHHHHHHH
24043423
358DimethylationAQRQKIQRTARKLFG
HHHHHHHHHHHHHHC
-
367PhosphorylationARKLFGLSVRCRHNP
HHHHHCCCCCCCCCC
24719451
433N-linked_GlycosylationIPCVIGGNNSCAMCS
CCEEECCCCCCCHHC
UniProtKB CARBOHYD
443N-linked_GlycosylationCAMCSLANISLCGSC
CCHHCCCCEEECCCC
UniProtKB CARBOHYD
525PhosphorylationPRWRKRMSLTLKSNK
HHHHHHHEEEECCCC
24719451
553N-linked_GlycosylationMRICQMRNSSLDPMF
HHHHHHCCCCCCCEE
UniProtKB CARBOHYD
599N-linked_GlycosylationLQNSQCYNWTLLLGN
ECCCCEECEEEEECC
UniProtKB CARBOHYD
623PhosphorylationHIYLRSRTRLPTLLR
HHHHHCCCCCCCCCC
23403867
627O-linked_GlycosylationRSRTRLPTLLRNETG
HCCCCCCCCCCCCCC
30379171
627PhosphorylationRSRTRLPTLLRNETG
HCCCCCCCCCCCCCC
23403867
631N-linked_GlycosylationRLPTLLRNETGQGPV
CCCCCCCCCCCCCCC
UniProtKB CARBOHYD
661PhosphorylationDVQVFGYSLRFNADL
CEEEEEEEEEECHHH
24719451
677N-linked_GlycosylationRSAVQQVNQSYTQGG
HHHHHHHHHHHHCCC
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 BRNP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRNP1_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 BRNP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUV91_HUMANSUV39H1physical
19218236
RPB1_HUMANPOLR2Aphysical
22446626
ROA1_HUMANHNRNPA1physical
22446626
SIR1_HUMANSIRT1physical
22446626
SIR1_HUMANSIRT1physical
18235501
RAC1_HUMANRAC1physical
21988832
PBIP1_HUMANPBXIP1physical
26186194
P53_HUMANTP53physical
25732823

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRNP1_HUMAN

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Related Literatures of Post-Translational Modification

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