BAIP2_RAT - dbPTM
BAIP2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAIP2_RAT
UniProt AC Q6GMN2
Protein Name Brain-specific angiogenesis inhibitor 1-associated protein 2
Gene Name Baiap2
Organism Rattus norvegicus (Rat).
Sequence Length 535
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Cell projection, filopodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membran
Protein Description Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions (By similarity)..
Protein Sequence MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTFAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKAFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPNKIPDRAAQLMQQMANSNGSILPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQENVPVMNGVAGADSEDYNPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLALPPPDYGTSSRAFPSQTAGTFKQRPYSVAVPAFSQGLDDYGARSVSRNPFANVHLKPTVTNDRSAPLLS
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
151PhosphorylationLRKKSQGSKNPQKYS
HHHHHCCCCCCCCCC		22.9425403869
160AcetylationNPQKYSDKELQYIDA
CCCCCCHHHHHHHHH		55.1522902405
171AcetylationYIDAISNKQGELENY
HHHHHHCCCCHHHHH		53.5422902405
250PhosphorylationLMQQMANSNGSILPS
HHHHHHHCCCCCCHH		32.7923984901
253PhosphorylationQMANSNGSILPSALS
HHHHCCCCCCHHHHH		25.7923984901
257PhosphorylationSNGSILPSALSASKS
CCCCCCHHHHHHCCC		38.0927097102
260PhosphorylationSILPSALSASKSNLV
CCCHHHHHHCCCCEE		30.1623984901
262PhosphorylationLPSALSASKSNLVIS
CHHHHHHCCCCEEEC		32.9929779826
264PhosphorylationSALSASKSNLVISDP
HHHHHCCCCEEECCC		32.6627097102
269PhosphorylationSKSNLVISDPIPGAK
CCCCEEECCCCCCCC		29.8327097102
276UbiquitinationSDPIPGAKPLPVPPE
CCCCCCCCCCCCCHH		53.66-
324PhosphorylationRKAAQPKSLSPPQSQ
HHCCCCCCCCCCCHH		40.5423984901
326PhosphorylationAAQPKSLSPPQSQSK
CCCCCCCCCCCHHHH		41.4430411139
335PhosphorylationPQSQSKLSDSYSNTL
CCHHHHCCCCCCCCC		28.3928432305
337PhosphorylationSQSKLSDSYSNTLPV
HHHHCCCCCCCCCCC		27.3828432305
338PhosphorylationQSKLSDSYSNTLPVR
HHHCCCCCCCCCCCC		15.7827097102
339PhosphorylationSKLSDSYSNTLPVRK
HHCCCCCCCCCCCCC		27.5627097102
341PhosphorylationLSDSYSNTLPVRKSV
CCCCCCCCCCCCCCC		26.8827097102
347PhosphorylationNTLPVRKSVTPKNSY
CCCCCCCCCCCCCCC		22.2127097102
349PhosphorylationLPVRKSVTPKNSYAT
CCCCCCCCCCCCCCC		35.3227097102
353PhosphorylationKSVTPKNSYATTENK
CCCCCCCCCCCCCCC		23.4428689409
354PhosphorylationSVTPKNSYATTENKT
CCCCCCCCCCCCCCC		19.84-
357PhosphorylationPKNSYATTENKTLPR
CCCCCCCCCCCCCCC		29.4128432305
361PhosphorylationYATTENKTLPRSSSM
CCCCCCCCCCCCHHH		54.2827097102
365PhosphorylationENKTLPRSSSMAAGL
CCCCCCCCHHHHHHC		25.4827097102
366PhosphorylationNKTLPRSSSMAAGLE
CCCCCCCHHHHHHCH		25.9727097102
367PhosphorylationKTLPRSSSMAAGLER
CCCCCCHHHHHHCHH		17.4330411139
385PhosphorylationMRVKAIFSHAAGDNS
HHEEEEEECCCCCCC		13.20-
396PhosphorylationGDNSTLLSFKEGDLI
CCCCEEEEECCCCEE		37.0730240740
416PhosphorylationEARDGWHYGESEKTK
CCCCCCCCCCCCCCC		18.97-
447PhosphorylationGSDRLHMSLQQGKSS
CCCCCEEEHHCCCCC		16.5725403869
453PhosphorylationMSLQQGKSSSTGNLL
EEHHCCCCCCCCCCC		36.0229779826
454PhosphorylationSLQQGKSSSTGNLLD
EHHCCCCCCCCCCCC		35.0923984901
455PhosphorylationLQQGKSSSTGNLLDK
HHCCCCCCCCCCCCH		47.6411514062
456PhosphorylationQQGKSSSTGNLLDKD
HCCCCCCCCCCCCHH		31.8530411139
472PhosphorylationLALPPPDYGTSSRAF
CCCCCCCCCCCCCCC		28.2528689409
476PhosphorylationPPDYGTSSRAFPSQT
CCCCCCCCCCCCCCC		27.7128689409
483PhosphorylationSRAFPSQTAGTFKQR
CCCCCCCCCCCCCCC		31.2428432305
486PhosphorylationFPSQTAGTFKQRPYS
CCCCCCCCCCCCCCE		25.7928432305
492PhosphorylationGTFKQRPYSVAVPAF
CCCCCCCCEEECCCC		20.2628689409
493PhosphorylationTFKQRPYSVAVPAFS
CCCCCCCEEECCCCC		13.2928689409
506PhosphorylationFSQGLDDYGARSVSR
CCCCCCCCCCCCCCC		16.61-
512 (in isoform 2)Phosphorylation-27.8228432305
513 (in isoform 2)Phosphorylation-53.3228432305
515 (in isoform 2)Phosphorylation-28.7228432305
517 (in isoform 2)Phosphorylation-20.5628432305
520 (in isoform 2)Phosphorylation-28.1328432305
521 (in isoform 2)Phosphorylation-6.5625403869
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 BAIP2_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAIP2_RAT !!
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 BAIP2_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLG3_RATDlg3physical
14596909
CNKR3_RATCnksr3physical
14596909
DLG1_RATDlg1physical
14596909
MAGI2_RATMagi2physical
14596909
LIN7B_RATLin7bphysical
14596909
ESPN_RATEspnphysical
12598619
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAIP2_RAT

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory