SLAI2_MOUSE - dbPTM
SLAI2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLAI2_MOUSE
UniProt AC Q8CI08
Protein Name SLAIN motif-containing protein 2
Gene Name Slain2
Organism Mus musculus (Mouse).
Sequence Length 581
Subcellular Localization Cytoplasm, cytoskeleton. Colocalizes with microtubules. Detected at the plus end of growing microtubules (By similarity)..
Protein Description Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase..
Protein Sequence MEDVNSNVNADQEVRKLQELVKKLEKQNEQLRSRSGAVQGAGLLGPGSPARVGVSTPSSGAASPRGFPLGLGAKASGGAGSGPRRTSSEDLRDATSLLAAGEGGLLDEVEPLRPDELERLSGWEEEEESWLYSSPKKKLTPMQKSVSPLVWCRQVLDYPSPDVECAKKSLIHKLDQTMSALKRQNLYNNPFNSVSYSNSYSPNASSPYSSGFNSPSSTPVRPPIVKQLILPGNSGNFKSSSDRNPPLSPQSSIDSELSASELDEDSIGSNYKLNDVTDVQILARMQEESLRQEYAASTSRRSSGSSCNSTRRGTFSDQELDAQSLDDEDDSLQHAVHPALNRFSPSPRNSPRPSPKQSPRNSPRSRSPARGIEYSRASPQPMISRLQQPRLSLQGHPTDLQTSNVKNEEKLRRSLPNLSRTSSTQVDSVKSSRSDSNFQVPNGGIPRMQPQASAIPSPGKFRSPAAPSPLALRQPVKAFSNHGSGSGSQETTQFTQTTSSPGPPVVQNSAPANPSSNINSATLTRPAGTTAMRSGLPRPSAPSAGGIPVPRSKLVQPVRRSLPAPKSYGSMKDDSWKDGCY
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-------MEDVNSNV
-------CCCHHHCC		10.02-
35PhosphorylationNEQLRSRSGAVQGAG
HHHHHHCCCCCCCCC		32.14-
48PhosphorylationAGLLGPGSPARVGVS
CCCCCCCCCCEEEEC		20.6526824392
55PhosphorylationSPARVGVSTPSSGAA
CCCEEEECCCCCCCC		28.7723737553
56PhosphorylationPARVGVSTPSSGAAS
CCEEEECCCCCCCCC		25.4523737553
58PhosphorylationRVGVSTPSSGAASPR
EEEECCCCCCCCCCC		41.3023737553
59PhosphorylationVGVSTPSSGAASPRG
EEECCCCCCCCCCCC		33.3826824392
63PhosphorylationTPSSGAASPRGFPLG
CCCCCCCCCCCCCCC		18.0025521595
86PhosphorylationAGSGPRRTSSEDLRD
CCCCCCCCCHHHHHH		37.5726239621
87PhosphorylationGSGPRRTSSEDLRDA
CCCCCCCCHHHHHHH		29.8926824392
88PhosphorylationSGPRRTSSEDLRDAT
CCCCCCCHHHHHHHH		34.2221082442
95PhosphorylationSEDLRDATSLLAAGE
HHHHHHHHHHHHHCC		24.9719060867
96PhosphorylationEDLRDATSLLAAGEG
HHHHHHHHHHHHCCC		24.0925367039
132PhosphorylationEEEESWLYSSPKKKL
HHHHHHCCCCCCCCC		10.8026643407
133PhosphorylationEEESWLYSSPKKKLT
HHHHHCCCCCCCCCC		37.6826643407
134PhosphorylationEESWLYSSPKKKLTP
HHHHCCCCCCCCCCC		27.4726643407
145PhosphorylationKLTPMQKSVSPLVWC
CCCCCCCCCCHHHHH		15.7823984901
147PhosphorylationTPMQKSVSPLVWCRQ
CCCCCCCCHHHHHHH		21.4321082442
160PhosphorylationRQVLDYPSPDVECAK
HHHHCCCCCCHHHHH		27.7430635358
177PhosphorylationLIHKLDQTMSALKRQ
HHHHHHHHHHHHHHC		16.8628066266
179PhosphorylationHKLDQTMSALKRQNL
HHHHHHHHHHHHCCC		33.5628066266
208PhosphorylationSPNASSPYSSGFNSP
CCCCCCCCCCCCCCC		19.88-
214PhosphorylationPYSSGFNSPSSTPVR
CCCCCCCCCCCCCCC		24.73-
234PhosphorylationQLILPGNSGNFKSSS
EEECCCCCCCCCCCC		40.8226745281
239PhosphorylationGNSGNFKSSSDRNPP
CCCCCCCCCCCCCCC		30.8225619855
240PhosphorylationNSGNFKSSSDRNPPL
CCCCCCCCCCCCCCC		36.5325619855
241PhosphorylationSGNFKSSSDRNPPLS
CCCCCCCCCCCCCCC		47.9125619855
248PhosphorylationSDRNPPLSPQSSIDS
CCCCCCCCCCHHHCC		27.0225619855
251PhosphorylationNPPLSPQSSIDSELS
CCCCCCCHHHCCCCC		32.4225619855
252PhosphorylationPPLSPQSSIDSELSA
CCCCCCHHHCCCCCH		25.7625619855
255PhosphorylationSPQSSIDSELSASEL
CCCHHHCCCCCHHHC		38.4725619855
258PhosphorylationSSIDSELSASELDED
HHHCCCCCHHHCCCC		26.2025619855
260PhosphorylationIDSELSASELDEDSI
HCCCCCHHHCCCCCC		35.0025619855
266PhosphorylationASELDEDSIGSNYKL
HHHCCCCCCCCCCCC		27.1425619855
269PhosphorylationLDEDSIGSNYKLNDV
CCCCCCCCCCCCCCC		35.0025619855
277PhosphorylationNYKLNDVTDVQILAR
CCCCCCCCHHHHHHH		33.0628066266
314PhosphorylationCNSTRRGTFSDQELD
CCCCCCCCCCHHHHC		20.3926824392
316PhosphorylationSTRRGTFSDQELDAQ
CCCCCCCCHHHHCHH		37.9226824392
324PhosphorylationDQELDAQSLDDEDDS
HHHHCHHCCCCCCHH		35.1721082442
331PhosphorylationSLDDEDDSLQHAVHP
CCCCCCHHHHHHHHH		42.1025619855
344PhosphorylationHPALNRFSPSPRNSP
HHHHHHCCCCCCCCC		22.6423684622
346PhosphorylationALNRFSPSPRNSPRP
HHHHCCCCCCCCCCC		34.9823684622
350PhosphorylationFSPSPRNSPRPSPKQ
CCCCCCCCCCCCCCC		24.4627742792
354PhosphorylationPRNSPRPSPKQSPRN
CCCCCCCCCCCCCCC		46.1126824392
358PhosphorylationPRPSPKQSPRNSPRS
CCCCCCCCCCCCCCC		31.7726824392
362PhosphorylationPKQSPRNSPRSRSPA
CCCCCCCCCCCCCCC		23.9921659605
365PhosphorylationSPRNSPRSRSPARGI
CCCCCCCCCCCCCCC		40.2626643407
367PhosphorylationRNSPRSRSPARGIEY
CCCCCCCCCCCCCCC		24.9429899451
374PhosphorylationSPARGIEYSRASPQP
CCCCCCCCCCCCCCC		11.0922324799
375PhosphorylationPARGIEYSRASPQPM
CCCCCCCCCCCCCCC		14.4726824392
378PhosphorylationGIEYSRASPQPMISR
CCCCCCCCCCCCHHH		23.9825521595
384PhosphorylationASPQPMISRLQQPRL
CCCCCCHHHHCCCCH		22.2322324799
392PhosphorylationRLQQPRLSLQGHPTD
HHCCCCHHHCCCCCC		21.6726824392
398PhosphorylationLSLQGHPTDLQTSNV
HHHCCCCCCHHCCCC		43.6026745281
402PhosphorylationGHPTDLQTSNVKNEE
CCCCCHHCCCCCCHH		29.5726643407
403PhosphorylationHPTDLQTSNVKNEEK
CCCCHHCCCCCCHHH		27.0226643407
414PhosphorylationNEEKLRRSLPNLSRT
CHHHHHHHCCCCCCC		41.5722942356
419PhosphorylationRRSLPNLSRTSSTQV
HHHCCCCCCCCCCCC		39.9026643407
421PhosphorylationSLPNLSRTSSTQVDS
HCCCCCCCCCCCCHH		24.53-
422PhosphorylationLPNLSRTSSTQVDSV
CCCCCCCCCCCCHHC		30.22-
423PhosphorylationPNLSRTSSTQVDSVK
CCCCCCCCCCCHHCC		23.4228542873
424PhosphorylationNLSRTSSTQVDSVKS
CCCCCCCCCCHHCCC		32.1729899451
431PhosphorylationTQVDSVKSSRSDSNF
CCCHHCCCCCCCCCC		28.9119060867
432PhosphorylationQVDSVKSSRSDSNFQ
CCHHCCCCCCCCCCC		30.0419060867
434PhosphorylationDSVKSSRSDSNFQVP
HHCCCCCCCCCCCCC		47.5425521595
436PhosphorylationVKSSRSDSNFQVPNG
CCCCCCCCCCCCCCC		40.5719060867
457PhosphorylationPQASAIPSPGKFRSP
CCCCCCCCCCCCCCC		39.9226643407
463PhosphorylationPSPGKFRSPAAPSPL
CCCCCCCCCCCCCCC		23.2524899341
468PhosphorylationFRSPAAPSPLALRQP
CCCCCCCCCCHHCCC		28.0224899341
476 (in isoform 2)Phosphorylation-5.4529514104
483 (in isoform 2)Phosphorylation-37.6425266776
489 (in isoform 2)Phosphorylation-56.4329514104
494 (in isoform 2)Phosphorylation-5.2629514104
538MethylationAMRSGLPRPSAPSAG
HHHCCCCCCCCCCCC		42.7324129315
540PhosphorylationRSGLPRPSAPSAGGI
HCCCCCCCCCCCCCC		54.83-
551MethylationAGGIPVPRSKLVQPV
CCCCCCCHHHCCCCH		46.8124129315
567PhosphorylationRSLPAPKSYGSMKDD
HCCCCCCCCCCCCCC		33.4022871156
570PhosphorylationPAPKSYGSMKDDSWK
CCCCCCCCCCCCCCC		17.9022871156
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 SLAI2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLAI2_MOUSE !!
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 SLAI2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FXR1_HUMANFXR1physical
26496610
CUL2_HUMANCUL2physical
26496610
ARK72_HUMANAKR7A2physical
26496610
HERC1_HUMANHERC1physical
26496610
CKAP5_HUMANCKAP5physical
26496610
KI26A_HUMANKIF26Aphysical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLAI2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-392, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASSSPECTROMETRY.

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