SPAST_HUMAN - dbPTM
SPAST_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPAST_HUMAN
UniProt AC Q9UBP0
Protein Name Spastin {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000303|PubMed:10610178}
Gene Name SPAST {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000312|HGNC:HGNC:11233}
Organism Homo sapiens (Human).
Sequence Length 616
Subcellular Localization Membrane
Peripheral membrane protein . Endoplasmic reticulum . Midbody . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton . Cytoplasm, perinuclear region . Nucleus . Cytoplasm, cytoskeleton, spindle . Cytoplas
Protein Description ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. [PubMed: 11809724]
Protein Sequence MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKMQPVLPFSKSQTDVYNDSTNLACRNGHLQSESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
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
3Phosphorylation-----MNSPGGRGKK
-----CCCCCCCCCC		24.5124905233
10AcetylationSPGGRGKKKGSGGAS
CCCCCCCCCCCCCCC		66.257378757
11AcetylationPGGRGKKKGSGGASN
CCCCCCCCCCCCCCC		62.897378767
17PhosphorylationKKGSGGASNPVPPRP
CCCCCCCCCCCCCCC		44.9628787133
51PhosphorylationSPHKRNLYYFSYPLF
CCCCCCCEEEHHHHH		13.1525002506
52PhosphorylationPHKRNLYYFSYPLFV
CCCCCCEEEHHHHHH		6.8225002506
54PhosphorylationKRNLYYFSYPLFVGF
CCCCEEEHHHHHHHH		15.1025002506
55PhosphorylationRNLYYFSYPLFVGFA
CCCEEEHHHHHHHHH		8.2825002506
92PhosphorylationALMAAKRSSGAAPAP
HHHHHHHCCCCCCCC		32.2025159151
93PhosphorylationLMAAKRSSGAAPAPA
HHHHHHCCCCCCCCC		36.1625159151
93 (in isoform 2)Phosphorylation-36.16-
101 (in isoform 2)Phosphorylation-23.00-
101PhosphorylationGAAPAPASASAPAPV
CCCCCCCCCCCCCCC		23.0015345747
103 (in isoform 2)Phosphorylation-32.08-
103PhosphorylationAPAPASASAPAPVPG
CCCCCCCCCCCCCCC		32.0815345747
103O-linked_GlycosylationAPAPASASAPAPVPG
CCCCCCCCCCCCCCC		32.08OGP
126PhosphorylationFHKQAFEYISIALRI
EEHHHHHHHEEEEEC		8.1020068231
128 (in isoform 2)Phosphorylation-10.83-
128PhosphorylationKQAFEYISIALRIDE
HHHHHHHEEEEECCC		10.8320068231
205PhosphorylationMQPVLPFSKSQTDVY
HCCCCCCCCCCCCCC		29.4723917254
206UbiquitinationQPVLPFSKSQTDVYN
CCCCCCCCCCCCCCC		47.14-
207PhosphorylationPVLPFSKSQTDVYND
CCCCCCCCCCCCCCC		36.7925159151
209PhosphorylationLPFSKSQTDVYNDST
CCCCCCCCCCCCCCC		34.2326657352
212PhosphorylationSKSQTDVYNDSTNLA
CCCCCCCCCCCCCCC		18.9629978859
213 (in isoform 2)Phosphorylation-36.28-
215PhosphorylationQTDVYNDSTNLACRN
CCCCCCCCCCCCCCC		18.6329978859
216PhosphorylationTDVYNDSTNLACRNG
CCCCCCCCCCCCCCC		36.8029978859
236 (in isoform 2)Phosphorylation-70.58-
236MethylationSGAVPKRKDPLTHTS
CCCCCCCCCCCCCCC		70.58115980661
240PhosphorylationPKRKDPLTHTSNSLP
CCCCCCCCCCCCCCC		28.6123927012
242PhosphorylationRKDPLTHTSNSLPRS
CCCCCCCCCCCCCCC		25.1125159151
243PhosphorylationKDPLTHTSNSLPRSK
CCCCCCCCCCCCCCC		19.4722167270
245PhosphorylationPLTHTSNSLPRSKTV
CCCCCCCCCCCCCCE		39.2529255136
248MethylationHTSNSLPRSKTVMKT
CCCCCCCCCCCEECC		56.96115917561
249PhosphorylationTSNSLPRSKTVMKTG
CCCCCCCCCCEECCC		30.6422210691
251PhosphorylationNSLPRSKTVMKTGSA
CCCCCCCCEECCCCC		27.3821406692
254UbiquitinationPRSKTVMKTGSAGLS
CCCCCEECCCCCCCC		45.45-
255PhosphorylationRSKTVMKTGSAGLSG
CCCCEECCCCCCCCC		20.4824719451
257PhosphorylationKTVMKTGSAGLSGHH
CCEECCCCCCCCCCC		25.1327470641
261PhosphorylationKTGSAGLSGHHRAPS
CCCCCCCCCCCCCCC		34.8523882029
268PhosphorylationSGHHRAPSYSGLSMV
CCCCCCCCCCCCEEC		30.8325159151
269PhosphorylationGHHRAPSYSGLSMVS
CCCCCCCCCCCEECC		13.0021945579
270PhosphorylationHHRAPSYSGLSMVSG
CCCCCCCCCCEECCC		37.2821945579
271 (in isoform 2)Phosphorylation-17.34-
273PhosphorylationAPSYSGLSMVSGVKQ
CCCCCCCEECCCCCC		22.2121945579
273 (in isoform 2)Phosphorylation-22.21-
274 (in isoform 2)Phosphorylation-3.15-
276PhosphorylationYSGLSMVSGVKQGSG
CCCCEECCCCCCCCC		29.2721945579
282PhosphorylationVSGVKQGSGPAPTTH
CCCCCCCCCCCCCCC		38.8323403867
287PhosphorylationQGSGPAPTTHKGTPK
CCCCCCCCCCCCCCC		43.5723403867
288PhosphorylationGSGPAPTTHKGTPKT
CCCCCCCCCCCCCCC		22.1123403867
292PhosphorylationAPTTHKGTPKTNRTN
CCCCCCCCCCCCCCC		26.8123403867
295PhosphorylationTHKGTPKTNRTNKPS
CCCCCCCCCCCCCCC		31.0126074081
298PhosphorylationGTPKTNRTNKPSTPT
CCCCCCCCCCCCCCC		50.0623403867
302PhosphorylationTNRTNKPSTPTTATR
CCCCCCCCCCCCCCC		48.9425159151
303PhosphorylationNRTNKPSTPTTATRK
CCCCCCCCCCCCCCC		32.9325159151
305PhosphorylationTNKPSTPTTATRKKK
CCCCCCCCCCCCCHH		29.2021712546
306PhosphorylationNKPSTPTTATRKKKD
CCCCCCCCCCCCHHH		27.5126055452
308PhosphorylationPSTPTTATRKKKDLK
CCCCCCCCCCHHHHH		40.7123403867
322PhosphorylationKNFRNVDSNLANLIM
HCCCCCCHHHHHHHH		29.4727251275
362PhosphorylationQEIVILPSLRPELFT
HHHHHCCCCCHHHHC		33.3024719451
389PhosphorylationGPPGNGKTMLAKAVA
CCCCCCHHHHHHHHH		20.8624719451
402PhosphorylationVAAESNATFFNISAA
HHHHCCCEEEEECHH		32.7722210691
410PhosphorylationFFNISAASLTSKYVG
EEEECHHHHCCCCCC		31.7126699800
413PhosphorylationISAASLTSKYVGEGE
ECHHHHCCCCCCCHH		27.5522210691
421UbiquitinationKYVGEGEKLVRALFA
CCCCCHHHHHHHHHH		64.24-
436PhosphorylationVARELQPSIIFIDEV
HHHHHCCCEEEEECH		18.50-
445PhosphorylationIFIDEVDSLLCERRE
EEEECHHHHHHHHCC		28.54-
519UbiquitinationETRLLLLKNLLCKQG
HHHHHHHHHHHHHCC		45.58-
519AcetylationETRLLLLKNLLCKQG
HHHHHHHHHHHHHCC		45.5826051181
527PhosphorylationNLLCKQGSPLTQKEL
HHHHHCCCCCCHHHH		17.7827470641
532UbiquitinationQGSPLTQKELAQLAR
CCCCCCHHHHHHHHH		49.84-
547PhosphorylationMTDGYSGSDLTALAK
HCCCCCHHHHHHHHH		24.4120068231
550PhosphorylationGYSGSDLTALAKDAA
CCCHHHHHHHHHHHH		25.3120068231
563 (in isoform 2)Phosphorylation-62.96-
565 (in isoform 2)Phosphorylation-41.58-
572 (in isoform 2)Phosphorylation-2.68-
595PhosphorylationSLKKIKRSVSPQTLE
HHHHHHHCCCHHHHH		23.1923898821
597PhosphorylationKKIKRSVSPQTLEAY
HHHHHCCCHHHHHHH		16.7311087788
600PhosphorylationKRSVSPQTLEAYIRW
HHCCCHHHHHHHHHH		29.9228450419
604PhosphorylationSPQTLEAYIRWNKDF
CHHHHHHHHHHHCCC		5.0120068231
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
268SPhosphorylationKinaseHIPK2Q9H2X6
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPAST_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 SPAST_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHM1B_HUMANCHMP1Bphysical
20719964
IST1_HUMANIST1physical
20719964
IST1_HUMANIST1physical
28514442
NUP98_HUMANNUP98physical
28514442
NU107_HUMANNUP107physical
28514442
WIPI4_HUMANWDR45physical
28514442
NUP43_HUMANNUP43physical
28514442
NU133_HUMANNUP133physical
28514442
CHM2A_HUMANCHMP2Aphysical
28514442
H2A2B_HUMANHIST2H2ABphysical
28514442
VTA1_HUMANVTA1physical
28514442
NUP85_HUMANNUP85physical
28514442
Drug and Disease Associations
Kegg Disease
H00266 Hereditary spastic paraplegia (SPG)
OMIM Disease
182601Spastic paraplegia 4, autosomal dominant (SPG4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPAST_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-268, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; THR-303 ANDTHR-306, AND MASS SPECTROMETRY.

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