KTNA1_HUMAN - dbPTM
KTNA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KTNA1_HUMAN
UniProt AC O75449
Protein Name Katanin p60 ATPase-containing subunit A1 {ECO:0000255|HAMAP-Rule:MF_03023}
Gene Name KATNA1 {ECO:0000255|HAMAP-Rule:MF_03023}
Organism Homo sapiens (Human).
Sequence Length 491
Subcellular Localization Cytoplasm . Midbody . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton, spindle . Predominantly cytoplasmic (PubMed:9658175). Localized diffusely in the cytoplasm dur
Protein Description Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth..
Protein Sequence MSLLMISENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTYLQQKWQQVWQEINVEAKHVKDIMKTLESFKLDSTPLKAAQHDLPASEGEVWSMPVPVERRPSPGPRKRQSSQYSDPKSHGNRPSTTVRVHRSSAQNVHNDRGKAVRCREKKEQNKGREEKNKSPAAVTEPETNKFDSTGYDKDLVEALERDIISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGTSENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSKEEMHMPTTMEDFEMALKKVSKSVSAADIERYEKWIFEFGSC
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
2Phosphorylation------MSLLMISEN
------CCCCCCCCC		30.1523917254
7Phosphorylation-MSLLMISENVKLAR
-CCCCCCCCCHHHHH		14.7823917254
22PhosphorylationEYALLGNYDSAMVYY
HHHHHCCCCHHHHHH		14.96-
29PhosphorylationYDSAMVYYQGVLDQM
CCHHHHHHHHHHHHH		6.33-
42PhosphorylationQMNKYLYSVKDTYLQ
HHHHHHHHHHHHHHH		21.7919287380
44UbiquitinationNKYLYSVKDTYLQQK
HHHHHHHHHHHHHHH		38.11-
51 (in isoform 2)Ubiquitination-33.7321890473
51 (in isoform 1)Ubiquitination-33.7321890473
51UbiquitinationKDTYLQQKWQQVWQE
HHHHHHHHHHHHHHH		33.7321906983
71 (in isoform 2)Ubiquitination-50.7421890473
71UbiquitinationKHVKDIMKTLESFKL
HHHHHHHHHHHHCCC		50.7421890473
72PhosphorylationHVKDIMKTLESFKLD
HHHHHHHHHHHCCCC		20.5526074081
75PhosphorylationDIMKTLESFKLDSTP
HHHHHHHHCCCCCCC		30.6928450419
77UbiquitinationMKTLESFKLDSTPLK
HHHHHHCCCCCCCCC		61.74-
80PhosphorylationLESFKLDSTPLKAAQ
HHHCCCCCCCCCHHC		42.2222617229
81PhosphorylationESFKLDSTPLKAAQH
HHCCCCCCCCCHHCC		32.1022617229
84UbiquitinationKLDSTPLKAAQHDLP
CCCCCCCCHHCCCCC		42.77-
93PhosphorylationAQHDLPASEGEVWSM
HCCCCCCCCCCCEEC		44.1625850435
99PhosphorylationASEGEVWSMPVPVER
CCCCCCEECCCCCCC		20.5526074081
109PhosphorylationVPVERRPSPGPRKRQ
CCCCCCCCCCCCCCC		40.4526846344
117PhosphorylationPGPRKRQSSQYSDPK
CCCCCCCCCCCCCCC		24.3628796482
118PhosphorylationGPRKRQSSQYSDPKS
CCCCCCCCCCCCCCC		25.4628796482
120PhosphorylationRKRQSSQYSDPKSHG
CCCCCCCCCCCCCCC		19.5928796482
121PhosphorylationKRQSSQYSDPKSHGN
CCCCCCCCCCCCCCC		39.5428796482
125PhosphorylationSQYSDPKSHGNRPST
CCCCCCCCCCCCCCC		41.8528555341
133PhosphorylationHGNRPSTTVRVHRSS
CCCCCCCEEEEEHHH		15.6219287380
148MethylationAQNVHNDRGKAVRCR
CCCCCCCCCCCHHHH		54.5580701039
167AcetylationQNKGREEKNKSPAAV
HHCCCCCCCCCCCCC		65.997374143
169AcetylationKGREEKNKSPAAVTE
CCCCCCCCCCCCCCC		69.737374153
170PhosphorylationGREEKNKSPAAVTEP
CCCCCCCCCCCCCCC		29.2129255136
175PhosphorylationNKSPAAVTEPETNKF
CCCCCCCCCCCCCCC		40.8923927012
179PhosphorylationAAVTEPETNKFDSTG
CCCCCCCCCCCCCCC		55.1923403867
181 (in isoform 1)Ubiquitination-58.9521890473
181UbiquitinationVTEPETNKFDSTGYD
CCCCCCCCCCCCCCC		58.9521906983
184PhosphorylationPETNKFDSTGYDKDL
CCCCCCCCCCCCHHH		27.1923403867
185PhosphorylationETNKFDSTGYDKDLV
CCCCCCCCCCCHHHH		41.4221406692
187PhosphorylationNKFDSTGYDKDLVEA
CCCCCCCCCHHHHHH		21.6521406692
189UbiquitinationFDSTGYDKDLVEALE
CCCCCCCHHHHHHHH		44.47-
205 (in isoform 2)Ubiquitination-43.4621890473
218UbiquitinationIADLVEAKKLLKEAV
HHHHHHHHHHHHHHC		30.3721890473
218 (in isoform 1)Ubiquitination-30.3721890473
219UbiquitinationADLVEAKKLLKEAVV
HHHHHHHHHHHHHCH		67.13-
236UbiquitinationMWMPEFFKGIRRPWK
HHCHHHHCCCCCCCC		59.76-
260UbiquitinationTGKTLLAKAVATECK
CCHHHHHHHHHHCCC		43.28-
281UbiquitinationSSSTLTSKYRGESEK
CCCHHHCCCCCCHHH		33.4621890473
281 (in isoform 1)Ubiquitination-33.4621890473
286PhosphorylationTSKYRGESEKLVRLL
HCCCCCCHHHHHHHH		42.7428270605
378PhosphorylationRRLEKRIYIPLPSAK
HHHHHCEEEECCCCC		10.6629496907
383PhosphorylationRIYIPLPSAKGREEL
CEEEECCCCCCHHHH		50.7424719451
385UbiquitinationYIPLPSAKGREELLR
EEECCCCCCHHHHHH		63.94-
422PhosphorylationGYSGADITNVCRDAS
CCCCCCHHHHHHHHH		23.34-
441PhosphorylationRRRIEGLTPEEIRNL
HHHHCCCCHHHHHCC		39.2421815630
450UbiquitinationEEIRNLSKEEMHMPT
HHHHCCCHHHHCCCC		61.94-
457PhosphorylationKEEMHMPTTMEDFEM
HHHHCCCCCHHHHHH		31.0626552605
458PhosphorylationEEMHMPTTMEDFEMA
HHHCCCCCHHHHHHH		16.8226552605
471UbiquitinationMALKKVSKSVSAADI
HHHHHHHCCCCHHHH		58.842190698
471 (in isoform 1)Ubiquitination-58.8421890473
474PhosphorylationKKVSKSVSAADIERY
HHHHCCCCHHHHHHH		25.4924532841
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
42SPhosphorylationKinaseDYRK2Q92630
Uniprot
109SPhosphorylationKinaseDYRK2Q92630
Uniprot
133TPhosphorylationKinaseDYRK2Q92630
Uniprot
-KUbiquitinationE3 ubiquitin ligaseDCAF1Q9Y4B6
PMID:19287380
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KTNA1_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 KTNA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL3_HUMANCUL3physical
19261606
UBR5_HUMANUBR5physical
19287380
DYRK2_HUMANDYRK2physical
19287380
DCAF1_HUMANVPRBPphysical
19287380
DDB1_HUMANDDB1physical
19287380
KTNB1_HUMANKATNB1physical
9568719
NDEL1_MOUSENdel1physical
16203747
DYHC1_MOUSEDync1h1physical
16203747
KTNB1_MOUSEKatnb1physical
16203747
KTNB1_HUMANKATNB1physical
16203747
KTNB1_HUMANKATNB1physical
22939629
UBP47_HUMANUSP47physical
23904609
CHIP_HUMANSTUB1physical
23904609
HS90A_HUMANHSP90AA1physical
23904609
CAN1_HUMANCAPN1physical
26496610
TAU_HUMANMAPTphysical
26496610
SRSF2_HUMANSRSF2physical
26496610
SRSF3_HUMANSRSF3physical
26496610
SOAT1_HUMANSOAT1physical
26496610
SPTB2_HUMANSPTBN1physical
26496610
SRPRA_HUMANSRPRphysical
26496610
UBP1_HUMANUSP1physical
26496610
ARK72_HUMANAKR7A2physical
26496610
LATS1_HUMANLATS1physical
26496610
VINEX_HUMANSORBS3physical
26496610
KTNB1_HUMANKATNB1physical
26496610
GOT1B_HUMANGOLT1Bphysical
26496610
RTEL1_HUMANRTEL1physical
26496610
NCK5L_HUMANNCKAP5Lphysical
26496610
SRPRB_HUMANSRPRBphysical
26496610
ENOPH_HUMANENOPH1physical
26496610
KTBL1_HUMANKATNBL1physical
26496610
RHG39_HUMANARHGAP39physical
26496610
ZNT7_HUMANSLC30A7physical
26496610
DAPLE_HUMANCCDC88Cphysical
26496610
KTNB1_HUMANKATNB1physical
28514442
TCPH_HUMANCCT7physical
28514442
LACRT_HUMANLACRTphysical
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 KTNA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3ligase.";
Maddika S., Chen J.;
Nat. Cell Biol. 11:409-419(2009).
Cited for: PHOSPHORYLATION AT SER-42; SER-109 AND THR-133 BY DYRK2, FUNCTION ASKATNA1 KINASE, AND INTERACTION WITH EDVP COMPLEX.
"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-170, 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-170, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND MASSSPECTROMETRY.

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