BPIB1_HUMAN - dbPTM
BPIB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BPIB1_HUMAN
UniProt AC Q8TDL5
Protein Name BPI fold-containing family B member 1
Gene Name BPIFB1
Organism Homo sapiens (Human).
Sequence Length 484
Subcellular Localization Secreted.
Protein Description May play a role in innate immunity in mouth, nose and lungs. Binds bacterial lipopolysaccharide (LPS) and modulates the cellular responses to LPS..
Protein Sequence MAGPWTFTLLCGLLAATLIQATLSPTAVLILGPKVIKEKLTQELKDHNATSILQQLPLLSAMREKPAGGIPVLGSLVNTVLKHIIWLKVITANILQLQVKPSANDQELLVKIPLDMVAGFNTPLVKTIVEFHMTTEAQATIRMDTSASGPTRLVLSDCATSHGSLRIQLLHKLSFLVNALAKQVMNLLVPSLPNLVKNQLCPVIEASFNGMYADLLQLVKVPISLSIDRLEFDLLYPAIKGDTIQLYLGAKLLDSQGKVTKWFNNSAASLTMPTLDNIPFSLIVSQDVVKAAVAAVLSPEEFMVLLDSVLPESAHRLKSSIGLINEKAADKLGSTQIVKILTQDTPEFFIDQGHAKVAQLIVLEVFPSSEALRPLFTLGIEASSEAQFYTKGDQLILNLNNISSDRIQLMNSGIGWFQPDVLKNIITEIIHSILLPNQNGKLRSGVPVSLVKALGFEAAESSLTKDALVLTPASLWKPSSPVSQ
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
48N-linked_GlycosylationTQELKDHNATSILQQ
HHHHHHCCHHHHHHH
55.86UniProtKB CARBOHYD
48N-linked_GlycosylationTQELKDHNATSILQQ
HHHHHHCCHHHHHHH
55.8617623646
127PhosphorylationFNTPLVKTIVEFHMT
CCCHHHHHHEEECCC
23.8329759185
134PhosphorylationTIVEFHMTTEAQATI
HHEEECCCCCCCEEE
16.9629759185
135PhosphorylationIVEFHMTTEAQATIR
HEEECCCCCCCEEEE
23.0429759185
140PhosphorylationMTTEAQATIRMDTSA
CCCCCCEEEEECCCC
9.3129759185
145PhosphorylationQATIRMDTSASGPTR
CEEEEECCCCCCCEE
19.4921406692
146PhosphorylationATIRMDTSASGPTRL
EEEEECCCCCCCEEE
19.0421406692
148PhosphorylationIRMDTSASGPTRLVL
EEECCCCCCCEEEEE
45.1021406692
151PhosphorylationDTSASGPTRLVLSDC
CCCCCCCEEEEEEEC
39.9121406692
156PhosphorylationGPTRLVLSDCATSHG
CCEEEEEEECCCCCC
24.1421406692
160PhosphorylationLVLSDCATSHGSLRI
EEEEECCCCCCHHHH
27.8221406692
161PhosphorylationVLSDCATSHGSLRIQ
EEEECCCCCCHHHHH
13.8121406692
164PhosphorylationDCATSHGSLRIQLLH
ECCCCCCHHHHHHHH
14.7321406692
191PhosphorylationVMNLLVPSLPNLVKN
HHHHHCCCCCHHHHC
49.32-
264N-linked_GlycosylationGKVTKWFNNSAASLT
CCCCHHCCCCCCCCC
40.19UniProtKB CARBOHYD
281PhosphorylationTLDNIPFSLIVSQDV
CCCCCCEEEEECHHH
16.3125332170
327UbiquitinationSIGLINEKAADKLGS
HHHCCCHHHHHHCCC
44.37-
401N-linked_GlycosylationQLILNLNNISSDRIQ
EEEEECCCCCCHHHH
38.3917623646
401N-linked_GlycosylationQLILNLNNISSDRIQ
EEEEECCCCCCHHHH
38.39UniProtKB CARBOHYD
444PhosphorylationNQNGKLRSGVPVSLV
CCCCCCCCCCCHHHH
55.3622817900

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 BPIB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BPIB1_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 BPIB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ENL_HUMANMLLT1physical
28514442
AF9_HUMANMLLT3physical
28514442
TIM50_HUMANTIMM50physical
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 BPIB1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP