ASB9_HUMAN - dbPTM
ASB9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASB9_HUMAN
UniProt AC Q96DX5
Protein Name Ankyrin repeat and SOCS box protein 9
Gene Name ASB9
Organism Homo sapiens (Human).
Sequence Length 294
Subcellular Localization Mitochondrion .
Protein Description 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. Recognizes at least two forms of creatine kinase, CKB and CKMT1A..
Protein Sequence MDGKQGGMDGSKPAGPRDFPGIRLLSNPLMGDAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQPESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVNQGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPESPLAQLFLEREGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL
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
1Acetylation-------MDGKQGGM
-------CCCCCCCC
16.1022814378
11PhosphorylationKQGGMDGSKPAGPRD
CCCCCCCCCCCCCCC
31.07-
51PhosphorylationAIHGHQLSLRNLISQ
HHHCHHHHHHHHHHC
20.7914702039
165PhosphorylationGNIDHKISHLGTPLY
CCCCHHHHCCCCCHH
19.9123312004
169PhosphorylationHKISHLGTPLYLACE
HHHHCCCCCHHHHCC
19.2423312004
172PhosphorylationSHLGTPLYLACENQQ
HCCCCCHHHHCCHHH
8.0823312004
185UbiquitinationQQRACVKKLLESGAD
HHHHHHHHHHHCCCC
37.60-
201PhosphorylationNQGKGQDSPLHAVAR
CCCCCCCCHHHHHHH
22.8225159151
209PhosphorylationPLHAVARTASEELAC
HHHHHHHHHCHHHHH
25.4629759185
211PhosphorylationHAVARTASEELACLL
HHHHHHHCHHHHHHH
30.8729759185
225PhosphorylationLMDFGADTQAKNAEG
HHHCCCCCCCCCCCC
29.8725278378
243PhosphorylationVELVPPESPLAQLFL
CEECCCCCHHHHHHH
30.8725850435
246 (in isoform 3)Phosphorylation-13.8625954137
256 (in isoform 2)Phosphorylation-51.4525954137

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 ASB9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASB9_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 ASB9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELOB_HUMANTCEB2physical
20302626
ELOC_HUMANTCEB1physical
20302626
CUL5_HUMANCUL5physical
20302626
KCRU_HUMANCKMT1Bphysical
20302626
KCRB_HUMANCKBphysical
20302626
KCRB_HUMANCKBphysical
17148442
CH60_HUMANHSPD1physical
17148442
HSP74_HUMANHSPA4physical
17148442
CUL5_HUMANCUL5physical
17148442
ELOC_HUMANTCEB1physical
17148442
ELOA1_HUMANTCEB3physical
17148442
UB2D1_HUMANUBE2D1physical
20302626
KCRB_HUMANCKBphysical
19060904
HIF1N_HUMANHIF1ANphysical
19060904
ELOC_HUMANTCEB1physical
23806657
ELOB_HUMANTCEB2physical
23806657
ELOC_HUMANTCEB1physical
23837592
ELOB_HUMANTCEB2physical
23837592
CUL5_HUMANCUL5physical
23837592
ELOB_HUMANTCEB2physical
24337577
H33_HUMANH3F3Aphysical
24337577
KCRB_HUMANCKBphysical
24337577
KCRU_HUMANCKMT1Bphysical
24337577
H2B1N_HUMANHIST1H2BNphysical
24337577
ELOC_HUMANTCEB1physical
24337577
H2AZ_HUMANH2AFZphysical
24337577
VIME_HUMANVIMphysical
24337577
ENOG_HUMANENO2physical
24337577
H12_HUMANHIST1H1Cphysical
24337577
RAB1A_HUMANRAB1Aphysical
24337577
PGAM1_HUMANPGAM1physical
24337577
ACTB_HUMANACTBphysical
24337577
CUL5_HUMANCUL5physical
24337577
TLN1_HUMANTLN1physical
24337577
ANXA5_HUMANANXA5physical
24337577
ASSY_HUMANASS1physical
24337577
ACON_HUMANACO2physical
24337577
ALDR_HUMANAKR1B1physical
24337577
LDHA_HUMANLDHAphysical
24337577
ANXA2_HUMANANXA2physical
24337577
PGK1_HUMANPGK1physical
24337577
KPRA_HUMANPRPSAP1physical
24337577
UBB_HUMANUBBphysical
26186194
ELOC_HUMANTCEB1physical
26186194
CUL5_HUMANCUL5physical
26186194
KCRM_HUMANCKMphysical
26186194
KCRB_HUMANCKBphysical
26186194
HIF1N_HUMANHIF1ANphysical
26186194
ARI2_HUMANARIH2physical
26186194
CRK_HUMANCRKphysical
25814554
KCRB_HUMANCKBphysical
25654263
ELOC_HUMANTCEB1physical
28514442
ARI2_HUMANARIH2physical
28514442
KCRB_HUMANCKBphysical
28514442
KCRM_HUMANCKMphysical
28514442
CUL5_HUMANCUL5physical
28514442
UBB_HUMANUBBphysical
28514442
HIF1N_HUMANHIF1ANphysical
28514442
ELOB_HUMANTCEB2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASB9_HUMAN

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Related Literatures of Post-Translational Modification

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