USBP1_HUMAN - dbPTM
USBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID USBP1_HUMAN
UniProt AC Q8N6Y0
Protein Name Usher syndrome type-1C protein-binding protein 1
Gene Name USHBP1 {ECO:0000312|EMBL:AAH27910.1}
Organism Homo sapiens (Human).
Sequence Length 703
Subcellular Localization
Protein Description
Protein Sequence MSARATRPRSRRGRHAPPGELDPVAESSEEVEAASGSSKPSFAPPPVSSGLEQLGPMEEVSGQGLGSRTDKKMDGGSGRELASAPEVPHKPAVEAHQAPEAALQYKETVPPGNGAPDVFQTLQHTLSSLEAAAAAWRHQPPSHSGPMEFEGTSEGGAGSLGKQEGAGSCQREAARLAERNAWLRLALSSREDELVRTQASLEAIRAEKETLQKEVQELQDSLLRLEPCPHLSHNQAGGSGSGSSSSEADREPWETQDSFSLAHPLLRRLRSHSSTQILGSLPNQPLSPEMHIMEAQMEQLRGSIEKLKCFNRLLSAVLQGYKGRCEGLSMQLGQREAEATALHLALQYSEHCEEAYRVLLALREADSGAGDEAPMSDLQAAEKEAWRLLAQEEAAMDAGAQQNPQPSPEGSSVDKPTPQEVAFQLRSYVQRLQERRSLMKILSEPGPTLAPMPTVPRAEAMVQAILGTQAGPALPRLEKTQIQQDLVAAREALADLMLRLQLVRREKRGLELREAALRALGPAHVLLLEQLRWERAELQAGGANSSGGHSSGGGSSGDEEEWYQGLPAVPGGTSGIDGGQVGRAWDPEKLAQELAASLTRTLDLQEQLQSLRRELEQVAQKGRARRSQSAELNRDLCKAHSALVLAFRGAHRKQEEQRRKLEQQMALMEAQQAEEVAVLEATARALGKPRPPLPPPQLGDTFL
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
83PhosphorylationGSGRELASAPEVPHK
CCCCCCCCCCCCCCC
57.9124719451
221PhosphorylationEVQELQDSLLRLEPC
HHHHHHHHHHCCCCC
19.1524719451
315PhosphorylationKCFNRLLSAVLQGYK
HHHHHHHHHHHCHHC
22.41-
322AcetylationSAVLQGYKGRCEGLS
HHHHCHHCCCHHHHH
46.8619815655
340PhosphorylationGQREAEATALHLALQ
CHHHHHHHHHHHHHH
22.6630177828
348PhosphorylationALHLALQYSEHCEEA
HHHHHHHHHHHHHHH
19.5130177828
349PhosphorylationLHLALQYSEHCEEAY
HHHHHHHHHHHHHHH
14.1130177828
356PhosphorylationSEHCEEAYRVLLALR
HHHHHHHHHHHHHHH
12.4430177828
627PhosphorylationQKGRARRSQSAELNR
HHHHHHHHHHHHHHH
23.96-

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 USBP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of USBP1_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 USBP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DYDC1_HUMANDYDC1physical
16189514
FBF1_HUMANFBF1physical
16189514
FATE1_HUMANFATE1physical
16189514
USBP1_HUMANUSHBP1physical
16189514
CA216_HUMANC1orf216physical
16189514
KANL1_HUMANKANSL1physical
16189514
EXOC8_HUMANEXOC8physical
16189514
CC120_HUMANCCDC120physical
16189514
USH1C_HUMANUSH1Cphysical
11311560
SRTD3_HUMANSERTAD3physical
19060904
USBP1_HUMANUSHBP1physical
25416956
FBF1_HUMANFBF1physical
25416956
KLC4_HUMANKLC4physical
25416956
CC120_HUMANCCDC120physical
25416956
IFT20_HUMANIFT20physical
25416956
UBX11_HUMANUBXN11physical
25416956
ZN765_HUMANZNF765physical
25416956
INT4_HUMANINTS4physical
25416956
HAUS1_HUMANHAUS1physical
25416956
K1C40_HUMANKRT40physical
25416956
CA216_HUMANC1orf216physical
25416956
CC148_HUMANCCDC148physical
25416956
DYDC1_HUMANDYDC1physical
25416956
KLC3_HUMANKLC3physical
25416956
CCD24_HUMANCCDC24physical
25416956
CF206_HUMANC6orf165physical
25416956
ZN483_HUMANZNF483physical
25416956
CC116_HUMANCCDC116physical
25416956
TXLNB_HUMANTXLNBphysical
25416956
TXLNA_HUMANTXLNAphysical
25416956
S14L4_HUMANSEC14L4physical
25416956
K2C79_HUMANKRT79physical
25416956
KLH38_HUMANKLHL38physical
25416956
CENPP_HUMANCENPPphysical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of USBP1_HUMAN

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Related Literatures of Post-Translational Modification

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