PX11B_HUMAN - dbPTM
PX11B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PX11B_HUMAN
UniProt AC O96011
Protein Name Peroxisomal membrane protein 11B
Gene Name PEX11B
Organism Homo sapiens (Human).
Sequence Length 259
Subcellular Localization Peroxisome membrane
Single-pass membrane protein .
Protein Description Involved in peroxisomal proliferation. [PubMed: 9792670 May regulate peroxisome division by recruiting the dynamin-related GTPase DNM1L to the peroxisomal membrane]
Protein Sequence MDAWVRFSAQSQARERLCRAAQYACSLLGHALQRHGASPELQKQIRQLESHLSLGRKLLRLGNSADALESAKRAVHLSDVVLRFCITVSHLNRALYFACDNVLWAGKSGLAPRVDQEKWAQRSFRYYLFSLIMNLSRDAYEIRLLMEQESSACSRRLKGSGGGVPGGSETGGLGGPGTPGGGLPQLALKLRLQVLLLARVLRGHPPLLLDVVRNACDLFIPLDKLGLWRCGPGIVGLCGLVSSILSILTLIYPWLRLKP
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
11PhosphorylationWVRFSAQSQARERLC
CHHHHHHHHHHHHHH
26.0628348404
26PhosphorylationRAAQYACSLLGHALQ
HHHHHHHHHHHHHHH
20.6123898821
29UbiquitinationQYACSLLGHALQRHG
HHHHHHHHHHHHHCC
14.8719608861
29AcetylationQYACSLLGHALQRHG
HHHHHHHHHHHHHCC
14.8719608861
38PhosphorylationALQRHGASPELQKQI
HHHHCCCCHHHHHHH
24.4125849741
43UbiquitinationGASPELQKQIRQLES
CCCHHHHHHHHHHHH
61.3921906983
43AcetylationGASPELQKQIRQLES
CCCHHHHHHHHHHHH
61.3919608861
53PhosphorylationRQLESHLSLGRKLLR
HHHHHHHHHHHHHHH
24.2923312004
64PhosphorylationKLLRLGNSADALESA
HHHHCCCCHHHHHHH
26.2330622161
72UbiquitinationADALESAKRAVHLSD
HHHHHHHHHHHHHHH
50.6021906983
72AcetylationADALESAKRAVHLSD
HHHHHHHHHHHHHHH
50.6030591217
96PhosphorylationSHLNRALYFACDNVL
HHHHHHHHHHHCCCH
6.53-
107UbiquitinationDNVLWAGKSGLAPRV
CCCHHCCCCCCCCCC
33.3421906983
126PhosphorylationWAQRSFRYYLFSLIM
HHHHHHHHHHHHHHH
11.5122817900
136PhosphorylationFSLIMNLSRDAYEIR
HHHHHHHCCCHHHHH
24.1019413330
158UbiquitinationSACSRRLKGSGGGVP
HHHHHHHCCCCCCCC
49.5821906983
160PhosphorylationCSRRLKGSGGGVPGG
HHHHHCCCCCCCCCC
32.4525159151
168PhosphorylationGGGVPGGSETGGLGG
CCCCCCCCCCCCCCC
37.5928857561
170PhosphorylationGVPGGSETGGLGGPG
CCCCCCCCCCCCCCC
37.9423312004
224UbiquitinationDLFIPLDKLGLWRCG
CCEECHHHHCCCCCC
52.7321906983

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 PX11B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PX11B_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 PX11B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNM1L_HUMANDNM1Lgenetic
20826455
FIS1_HUMANFIS1genetic
20826455
PX11B_HUMANPEX11Bphysical
20826455
FIS1_HUMANFIS1physical
20826455
PEX19_HUMANPEX19physical
12096124

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614920Peroxisome biogenesis disorder 14B (PBD14B)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PX11B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43, AND MASS SPECTROMETRY.

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