AB1IP_HUMAN - dbPTM
AB1IP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AB1IP_HUMAN
UniProt AC Q7Z5R6
Protein Name Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
Gene Name APBB1IP
Organism Homo sapiens (Human).
Sequence Length 666
Subcellular Localization Cell membrane
Peripheral membrane protein. Cell projection, lamellipodium. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Colocalizes with ENA/VASP proteins at lamellipodia tips and focal adhesions, and F-actin at the leading edge. At the m
Protein Description Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion..
Protein Sequence MGESSEDIDQMFSTLLGEMDLLTQSLGVDTLPPPDPNPPRAEFNYSVGFKDLNESLNALEDQDLDALMADLVADISEAEQRTIQAQKESLQNQHHSASLQASIFSGAASLGYGTNVAATGISQYEDDLPPPPADPVLDLPLPPPPPEPLSQEEEEAQAKADKIKLALEKLKEAKVKKLVVKVHMNDNSTKSLMVDERQLARDVLDNLFEKTHCDCNVDWCLYEIYPELQIERFFEDHENVVEVLSDWTRDTENKILFLEKEEKYAVFKNPQNFYLDNRGKKESKETNEKMNAKNKESLLEESFCGTSIIVPELEGALYLKEDGKKSWKRRYFLLRASGIYYVPKGKTKTSRDLACFIQFENVNIYYGTQHKMKYKAPTDYCFVLKHPQIQKESQYIKYLCCDDTRTLNQWVMGIRIAKYGKTLYDNYQRAVAKAGLASRWTNLGTVNAAAPAQPSTGPKTGTTQPNGQIPQATHSVSAVLQEAQRHAETSKDKKPALGNHHDPAVPRAPHAPKSSLPPPPPVRRSSDTSGSPATPLKAKGTGGGGLPAPPDDFLPPPPPPPPLDDPELPPPPPDFMEPPPDFVPPPPPSYAGIAGSELPPPPPPPPAPAPAPVPDSARPPPAVAKRPPVPPKRQENPGHPGGAGGGEQDFMSDLMKALQKKRGNVS
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
45PhosphorylationPPRAEFNYSVGFKDL
CCCCCCEEEECCCHH		15.2828796482
46PhosphorylationPRAEFNYSVGFKDLN
CCCCCEEEECCCHHH		19.5028796482
55PhosphorylationGFKDLNESLNALEDQ
CCCHHHHHHHHHCCC		26.3328464451
164UbiquitinationQAKADKIKLALEKLK
HHHHHHHHHHHHHHH		33.1929967540
169UbiquitinationKIKLALEKLKEAKVK
HHHHHHHHHHHHCCC		66.7529967540
171UbiquitinationKLALEKLKEAKVKKL
HHHHHHHHHHCCCEE		67.69-
181UbiquitinationKVKKLVVKVHMNDNS
CCCEEEEEEECCCCC		20.9529967540
190UbiquitinationHMNDNSTKSLMVDER
ECCCCCCCCCEECHH		41.22-
210UbiquitinationVLDNLFEKTHCDCNV
HHHHHHHHHCCCCCC		35.91-
225PhosphorylationDWCLYEIYPELQIER
CHHHHHHCCHHCHHH		4.44-
254UbiquitinationWTRDTENKILFLEKE
HCCCCCCCEEEEECH		34.26-
260UbiquitinationNKILFLEKEEKYAVF
CCEEEEECHHHEEEE		73.6229967540
263UbiquitinationLFLEKEEKYAVFKNP
EEEECHHHEEEECCC		39.3322817900
268UbiquitinationEEKYAVFKNPQNFYL
HHHEEEECCCCCCCC		62.2122817900
274PhosphorylationFKNPQNFYLDNRGKK
ECCCCCCCCCCCCCC		22.2428796482
331PhosphorylationKKSWKRRYFLLRASG
CCCCCCEEEEEECCE		11.56-
337PhosphorylationRYFLLRASGIYYVPK
EEEEEECCEEEEECC		21.20-
340PhosphorylationLLRASGIYYVPKGKT
EEECCEEEEECCCCC		11.2625147952
341PhosphorylationLRASGIYYVPKGKTK
EECCEEEEECCCCCC		14.35-
344UbiquitinationSGIYYVPKGKTKTSR
CEEEEECCCCCCCCC		64.10-
346UbiquitinationIYYVPKGKTKTSRDL
EEEECCCCCCCCCCE		53.63-
370UbiquitinationNIYYGTQHKMKYKAP
EEEEECCCCCEEECC		31.8322817900
373UbiquitinationYGTQHKMKYKAPTDY
EECCCCCEEECCCCE		48.6921890473
374PhosphorylationGTQHKMKYKAPTDYC
ECCCCCEEECCCCEE		14.6422817900
375MalonylationTQHKMKYKAPTDYCF
CCCCCEEECCCCEEE		42.2326320211
375UbiquitinationTQHKMKYKAPTDYCF
CCCCCEEECCCCEEE		42.2329967540
380PhosphorylationKYKAPTDYCFVLKHP
EEECCCCEEEEECCH		7.1125839225
385UbiquitinationTDYCFVLKHPQIQKE
CCEEEEECCHHHHCH		48.1929967540
391UbiquitinationLKHPQIQKESQYIKY
ECCHHHHCHHHEEEE		62.0529967540
397UbiquitinationQKESQYIKYLCCDDT
HCHHHEEEEEECCCC		27.51-
418UbiquitinationVMGIRIAKYGKTLYD
HHHHHHHHCCCCHHH		52.7622817900
421UbiquitinationIRIAKYGKTLYDNYQ
HHHHHCCCCHHHHHH		32.0622817900
433UbiquitinationNYQRAVAKAGLASRW
HHHHHHHHHCHHHHC		36.0729967540
455PhosphorylationAAAPAQPSTGPKTGT
CCCCCCCCCCCCCCC		33.6422210691
456PhosphorylationAAPAQPSTGPKTGTT
CCCCCCCCCCCCCCC		65.2722210691
514PhosphorylationRAPHAPKSSLPPPPP
CCCCCCHHHCCCCCC		35.7323882029
515PhosphorylationAPHAPKSSLPPPPPV
CCCCCHHHCCCCCCC		51.5323882029
525PhosphorylationPPPPVRRSSDTSGSP
CCCCCCCCCCCCCCC		23.2323401153
526PhosphorylationPPPVRRSSDTSGSPA
CCCCCCCCCCCCCCC		43.0022617229
528PhosphorylationPVRRSSDTSGSPATP
CCCCCCCCCCCCCCC		36.6123401153
529PhosphorylationVRRSSDTSGSPATPL
CCCCCCCCCCCCCCC		42.1123911959
531PhosphorylationRSSDTSGSPATPLKA
CCCCCCCCCCCCCCC		15.8923401153
534PhosphorylationDTSGSPATPLKAKGT
CCCCCCCCCCCCCCC		32.3223882029
541PhosphorylationTPLKAKGTGGGGLPA
CCCCCCCCCCCCCCC		31.7626074081
652PhosphorylationGGEQDFMSDLMKALQ
CCHHHHHHHHHHHHH		27.82-
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 AB1IP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AB1IP_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 AB1IP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PKHH1_HUMANPLEKHH1physical
26186194
ANX13_HUMANANXA13physical
26186194
PKHH1_HUMANPLEKHH1physical
28514442
ANX13_HUMANANXA13physical
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 AB1IP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-526 AND SER-531,AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASSSPECTROMETRY.

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