AVIL_HUMAN - dbPTM
AVIL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AVIL_HUMAN
UniProt AC O75366
Protein Name Advillin
Gene Name AVIL
Organism Homo sapiens (Human).
Sequence Length 819
Subcellular Localization Cytoplasm, cytoskeleton. Cell projection. Cell projection, axon.
Protein Description Ca(2+)-regulated actin-binding protein. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis..
Protein Sequence MPLTSAFRAVDNDPGIIVWRIEKMELALVPVSAHGNFYEGDCYVILSTRRVASLLSQDIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQYHESDTFRGYFKQGIIYKQGGVASGMKHVETNTYDVKRLLHVKGKRNIRATEVEMSWDSFNRGDVFLLDLGKVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAKIGVIEGDKEAASPELMKVLQDTLGRRSIIKPTVPDEIIDQKQKSTIMLYHISDSAGQLAVTEVATRPLVQDLLNHDDCYILDQSGTKIYVWKGKGATKAEKQAAMSKALGFIKMKSYPSSTNVETVNDGAESAMFKQLFQKWSVKDQTMGLGKTFSIGKIAKVFQDKFDVTLLHTKPEVAAQERMVDDGNGKVEVWRIENLELVPVEYQWYGFFYGGDCYLVLYTYEVNGKPHHILYIWQGRHASQDELAASAYQAVEVDRQFDGAAVQVRVRMGTEPRHFMAIFKGKLVIFEGGTSRKGNAEPDPPVRLFQIHGNDKSNTKAVEVPAFASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELASLLCDGSENTVAEGQEPAEFWDLLGGKTPYANDKRLQQEILDVQSRLFECSNKTGQFVVTEITDFTQDDLNPTDVMLLDTWDQVFLWIGAEANATEKESALATAQQYLHTHPSGRDPDTPILIIKQGFEPPIFTGWFLAWDPNIWSAGKTYEQLKEELGDAAAIMRITADMKNATLSLNSNDSEPKYYPIAVLLKNQNQELPEDVNPAKKENYLSEQDFVSVFGITRGQFAALPGWKQLQMKKEKGLF
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
2 (in isoform 2)Phosphorylation-44.3324043423
3 (in isoform 2)Phosphorylation-5.9624043423
4 (in isoform 2)Phosphorylation-16.4924043423
4Phosphorylation----MPLTSAFRAVD
----CCCCCCCCCCC		16.4923663014
5Phosphorylation---MPLTSAFRAVDN
---CCCCCCCCCCCC		32.8523663014
9 (in isoform 2)Phosphorylation-13.4324043423
10 (in isoform 2)Phosphorylation-6.5224043423
53PhosphorylationLSTRRVASLLSQDIH
EEHHHHHHHHHCCEE		27.30-
85PhosphorylationYTTQLDDYLGGSPVQ
EEECHHHHCCCCCCC		13.60-
107PhosphorylationESDTFRGYFKQGIIY
CCCCCHHHCCCCEEE		11.8926074081
114PhosphorylationYFKQGIIYKQGGVAS
HCCCCEEEEECCCCC		8.7126074081
121PhosphorylationYKQGGVASGMKHVET
EEECCCCCCCEEEEC		36.6926074081
124AcetylationGGVASGMKHVETNTY
CCCCCCCEEEECCCC		48.2819827443
128PhosphorylationSGMKHVETNTYDVKR
CCCEEEECCCCCHHH		31.6026074081
130PhosphorylationMKHVETNTYDVKRLL
CEEEECCCCCHHHHH		28.6326074081
131PhosphorylationKHVETNTYDVKRLLH
EEEECCCCCHHHHHC		22.3226074081
216PhosphorylationEGDKEAASPELMKVL
ECCHHHCCHHHHHHH		26.42-
231PhosphorylationQDTLGRRSIIKPTVP
HHHHCCCCCCCCCCC		27.5724719451
248PhosphorylationIIDQKQKSTIMLYHI
HCCCCCCCEEEEEEE		22.2226471730
249PhosphorylationIDQKQKSTIMLYHIS
CCCCCCCEEEEEEEE		19.9026471730
253PhosphorylationQKSTIMLYHISDSAG
CCCEEEEEEEECCCC		4.6326471730
256PhosphorylationTIMLYHISDSAGQLA
EEEEEEEECCCCCEE		16.5226471730
258PhosphorylationMLYHISDSAGQLAVT
EEEEEECCCCCEEEE		27.7526471730
296AcetylationGTKIYVWKGKGATKA
CCEEEEEECCCCCHH		40.4712654405
310PhosphorylationAEKQAAMSKALGFIK
HHHHHHHHHHHCCEE		15.28-
319MethylationALGFIKMKSYPSSTN
HHCCEEECCCCCCCC		41.66-
320PhosphorylationLGFIKMKSYPSSTNV
HCCEEECCCCCCCCC		38.48-
329PhosphorylationPSSTNVETVNDGAES
CCCCCCEECCCHHHH		21.96-
336PhosphorylationTVNDGAESAMFKQLF
ECCCHHHHHHHHHHH		25.21-
426UbiquitinationYGGDCYLVLYTYEVN
ECCEEEEEEEEEEEC		1.2321963094
444UbiquitinationHHILYIWQGRHASQD
EEEEEEECCCCCCHH		29.5021963094
616PhosphorylationQEILDVQSRLFECSN
HHHHHHHHHHHHHCC		30.6919413330
720UbiquitinationPNIWSAGKTYEQLKE
CCHHHCCHHHHHHHH		47.8821963094
743UbiquitinationMRITADMKNATLSLN
HHHEEECCCCEEECC		43.9321963094
754PhosphorylationLSLNSNDSEPKYYPI
EECCCCCCCCCCCEE		61.1124719451
758PhosphorylationSNDSEPKYYPIAVLL
CCCCCCCCCEEEEEE		25.78-
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 AVIL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AVIL_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 AVIL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX11_HUMANDDX11physical
28514442
DUS3L_HUMANDUS3Lphysical
28514442
FIGL1_HUMANFIGNL1physical
28514442
SCYL1_HUMANSCYL1physical
28514442
DOCK7_HUMANDOCK7physical
28514442
VILI_HUMANVIL1physical
28514442
TMOD2_HUMANTMOD2physical
28514442
RICTR_HUMANRICTORphysical
28514442
DCTN6_HUMANDCTN6physical
28514442
MCM8_HUMANMCM8physical
28514442
THUM3_HUMANTHUMPD3physical
28514442
FANCJ_HUMANBRIP1physical
28514442
MYO5C_HUMANMYO5Cphysical
28514442
ALMS1_HUMANALMS1physical
28514442
MYO1F_HUMANMYO1Fphysical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
TBB8_HUMANTUBB8physical
28514442
MYO1B_HUMANMYO1Bphysical
28514442
MYO5A_HUMANMYO5Aphysical
28514442
UBP47_HUMANUSP47physical
28514442
CN080_HUMANC14orf80physical
28514442
TBB3_HUMANTUBB3physical
28514442
WDR59_HUMANWDR59physical
28514442
BBS1_HUMANBBS1physical
28514442
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 AVIL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND MASSSPECTROMETRY.

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