ASB1_HUMAN - dbPTM
ASB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASB1_HUMAN
UniProt AC Q9Y576
Protein Name Ankyrin repeat and SOCS box protein 1
Gene Name ASB1
Organism Homo sapiens (Human).
Sequence Length 335
Subcellular Localization
Protein Description May play a role in testis development (By similarity). Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins..
Protein Sequence MAEGGSPDGRAGPGSAGRNLKEWLREQFCDHPLEHCEDTRLHDAAYVGDLQTLRSLLQEESYRSRINEKSVWCCGWLPCTPLRIAATAGHGSCVDFLIRKGAEVDLVDVKGQTALYVAVVNGHLESTQILLEAGADPNGSRHHRSTPVYHASRVGRADILKALIRYGADVDVNHHLTPDVQPRFSRRLTSLVVCPLYISAAYHNLQCFRLLLLAGANPDFNCNGPVNTQGFYRGSPGCVMDAVLRHGCEAAFVSLLVEFGANLNLVKWESLGPESRGRRKVDPEALQVFKEARSVPRTLLCLCRVAVRRALGKHRLHLIPSLPLPDPIKKFLLHE
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
2Acetylation------MAEGGSPDG
------CCCCCCCCC
24.92-
6Phosphorylation--MAEGGSPDGRAGP
--CCCCCCCCCCCCC
30.5822199227
15PhosphorylationDGRAGPGSAGRNLKE
CCCCCCCHHHHCHHH
30.5926074081
21UbiquitinationGSAGRNLKEWLREQF
CHHHHCHHHHHHHHH
50.85-
46PhosphorylationTRLHDAAYVGDLQTL
CCCCCCCHHHCHHHH
13.4927642862
55PhosphorylationGDLQTLRSLLQEESY
HCHHHHHHHHCHHHH
36.22-
69UbiquitinationYRSRINEKSVWCCGW
HHHHCCCCCEEECCE
45.91-
161UbiquitinationVGRADILKALIRYGA
CCHHHHHHHHHHHCC
41.29-
280UbiquitinationPESRGRRKVDPEALQ
CCCCCCCCCCHHHHH
50.02-

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 ASB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASB1_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 ASB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL5_HUMANCUL5physical
16325183
RBX2_HUMANRNF7physical
16325183
CUL5_HUMANCUL5physical
18187417
ELOB_HUMANTCEB2physical
18187417
ELOC_HUMANTCEB1physical
18187417
CUL5_HUMANCUL5physical
24337577
ELOB_HUMANTCEB2physical
24337577
SSBP_HUMANSSBP1physical
24337577
HCD2_HUMANHSD17B10physical
24337577
HMGB1_HUMANHMGB1physical
24337577
BASI_HUMANBSGphysical
24337577
CAND1_HUMANCAND1physical
24337577
AT2A2_HUMANATP2A2physical
24337577
PTPS_HUMANPTSphysical
24337577
ELOC_HUMANTCEB1physical
24337577
MRRP1_HUMANTRMT10Cphysical
24337577
CPSM_HUMANCPS1physical
24337577
SSRD_HUMANSSR4physical
24337577
U5S1_HUMANEFTUD2physical
24337577
ARL1_HUMANARL1physical
24337577
SMD1_HUMANSNRPD1physical
24337577
PROF1_HUMANPFN1physical
24337577

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 ASB1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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