ASB8_HUMAN - dbPTM
ASB8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASB8_HUMAN
UniProt AC Q9H765
Protein Name Ankyrin repeat and SOCS box protein 8
Gene Name ASB8
Organism Homo sapiens (Human).
Sequence Length 288
Subcellular Localization Cytoplasm .
Protein Description May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins..
Protein Sequence MSSSMWYIMQSIQSKYSLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEKDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLIGQTPISRLVALLVRGLGTEKEDSCFELLHRAVGHFELRKNGTMPREVARDPQLCEKLTVLCSAPGTLKTLARYAVRRSLGLQYLPDAVKGLPLPASLKEYLLLLE
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
2Phosphorylation------MSSSMWYIM
------CCHHHHHHH
30.9923663014
3Phosphorylation-----MSSSMWYIMQ
-----CCHHHHHHHH
23.9423663014
4Phosphorylation----MSSSMWYIMQS
----CCHHHHHHHHH
13.1623663014
7Phosphorylation-MSSSMWYIMQSIQS
-CCHHHHHHHHHHHH
4.2923663014
11PhosphorylationSMWYIMQSIQSKYSL
HHHHHHHHHHHCCCH
12.7623663014
14PhosphorylationYIMQSIQSKYSLSER
HHHHHHHHCCCHHHH
31.7123663014
17PhosphorylationQSIQSKYSLSERLIR
HHHHHCCCHHHHHHH
29.20-
31PhosphorylationRTIAAIRSFPHDNVE
HHHHHHHCCCCCCHH
36.70-
85PhosphorylationEVNALDGYNRTALHY
CCCCCCCCCHHHHHH
10.92-
203UbiquitinationVRGLGTEKEDSCFEL
HHCCCCCCCHHHHHH
67.66-
239UbiquitinationRDPQLCEKLTVLCSA
CCHHHHHHHHHHHCC
48.76-
241PhosphorylationPQLCEKLTVLCSAPG
HHHHHHHHHHHCCCC
23.6221712546
249PhosphorylationVLCSAPGTLKTLARY
HHHCCCCHHHHHHHH
24.8321712546
251UbiquitinationCSAPGTLKTLARYAV
HCCCCHHHHHHHHHH
41.13-
272UbiquitinationQYLPDAVKGLPLPAS
CCCCHHHCCCCCCCH
57.35-

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
17SPhosphorylationKinaseIKKEQ14164
PSP
17SPhosphorylationKinaseTBK1Q9UHD2
PSP
31SPhosphorylationKinaseIKKBO14920
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASB8_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 ASB8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELOB_HUMANTCEB2physical
12559969
ELOC_HUMANTCEB1physical
12559969
MCM7_HUMANMCM7physical
21988832
RCN1_HUMANRCN1physical
21988832
ELOC_HUMANTCEB1physical
21988832
SRTD1_HUMANSERTAD1physical
21988832
ZC3H6_HUMANZC3H6physical
24337577
CUL5_HUMANCUL5physical
24337577
HIF1N_HUMANHIF1ANphysical
24337577
NEDD8_HUMANNEDD8physical
24337577
ELOC_HUMANTCEB1physical
24337577
ELOB_HUMANTCEB2physical
24337577
PCNA_HUMANPCNAphysical
24337577
TMEDA_HUMANTMED10physical
24337577
TBB3_HUMANTUBB3physical
24337577
AMRA1_HUMANAMBRA1physical
24337577
KI26B_HUMANKIF26Bphysical
24337577
CMC2_HUMANSLC25A13physical
24337577
ADT3_HUMANSLC25A6physical
24337577
CUL5_HUMANCUL5physical
26186194
HIF1N_HUMANHIF1ANphysical
26186194
NPAT_HUMANNPATphysical
26186194
TRI11_HUMANTRIM11physical
26186194
AMRA1_HUMANAMBRA1physical
26186194
CUL5_HUMANCUL5physical
28514442
SYIM_HUMANIARS2physical
28514442
HIF1N_HUMANHIF1ANphysical
28514442
NPAT_HUMANNPATphysical
28514442
TRI11_HUMANTRIM11physical
28514442
AMRA1_HUMANAMBRA1physical
28514442
RUFY3_HUMANRUFY3physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASB8_HUMAN

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Related Literatures of Post-Translational Modification

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