KTNB1_HUMAN - dbPTM
KTNB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KTNB1_HUMAN
UniProt AC Q9BVA0
Protein Name Katanin p80 WD40 repeat-containing subunit B1 {ECO:0000255|HAMAP-Rule:MF_03022}
Gene Name KATNB1 {ECO:0000255|HAMAP-Rule:MF_03022}
Organism Homo sapiens (Human).
Sequence Length 655
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, spindle . Predominantly cytoplasmic. Localized to the interphase centrosome an
Protein Description Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. 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 MATPVVTKTAWKLQEIVAHASNVSSLVLGKASGRLLATGGDDCRVNLWSINKPNCIMSLTGHTSPVESVRLNTPEELIVAGSQSGSIRVWDLEAAKILRTLMGHKANICSLDFHPYGEFVASGSQDTNIKLWDIRRKGCVFRYRGHSQAVRCLRFSPDGKWLASAADDHTVKLWDLTAGKMMSEFPGHTGPVNVVEFHPNEYLLASGSSDRTIRFWDLEKFQVVSCIEGEPGPVRSVLFNPDGCCLYSGCQDSLRVYGWEPERCFDVVLVNWGKVADLAICNDQLIGVAFSQSNVSSYVVDLTRVTRTGTVARDPVQDHRPLAQPLPNPSAPLRRIYERPSTTCSKPQRVKQNSESERRSPSSEDDRDERESRAEIQNAEDYNEIFQPKNSISRTPPRRSEPFPAPPEDDAATAKEAAKPSPAMDVQFPVPNLEVLPRPPVVASTPAPKAEPAIIPATRNEPIGLKASDFLPAVKIPQQAELVDEDAMSQIRKGHDTMCVVLTSRHKNLDTVRAVWTMGDIKTSVDSAVAINDLSVVVDLLNIVNQKASLWKLDLCTTVLPQIEKLLQSKYESYVQTGCTSLKLILQRFLPLITDMLAAPPSVGVDISREERLHKCRLCYKQLKSISGLVKSKSGLSGRHGSTFRELHLLMASLD
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
8UbiquitinationMATPVVTKTAWKLQE
CCCCCCCHHHHHHHH		25.33-
96UbiquitinationVWDLEAAKILRTLMG
EEEHHHHHHHHHHHC		49.6922817900
144MethylationKGCVFRYRGHSQAVR
CCEEEEECCCCCEEE		31.90115480843
160UbiquitinationLRFSPDGKWLASAAD
EEECCCCCEECCCCC		46.5529967540
170PhosphorylationASAADDHTVKLWDLT
CCCCCCCEEEEEECC		26.74-
172UbiquitinationAADDHTVKLWDLTAG
CCCCCEEEEEECCCC		45.0429967540
310PhosphorylationTRVTRTGTVARDPVQ
EEEECCCCCCCCCCC		15.4724260401
337PhosphorylationSAPLRRIYERPSTTC
CCCHHHHHCCCCCCC		12.2225884760
341PhosphorylationRRIYERPSTTCSKPQ
HHHHCCCCCCCCCCH		42.4426552605
342PhosphorylationRIYERPSTTCSKPQR
HHHCCCCCCCCCCHH		34.2125394399
343PhosphorylationIYERPSTTCSKPQRV
HHCCCCCCCCCCHHC		21.0826552605
345PhosphorylationERPSTTCSKPQRVKQ
CCCCCCCCCCHHCCC		45.3226552605
346UbiquitinationRPSTTCSKPQRVKQN
CCCCCCCCCHHCCCC		47.5224816145
346AcetylationRPSTTCSKPQRVKQN
CCCCCCCCCHHCCCC		47.5225953088
354PhosphorylationPQRVKQNSESERRSP
CHHCCCCCCCCCCCC		39.7524719451
356PhosphorylationRVKQNSESERRSPSS
HCCCCCCCCCCCCCC		35.9024719451
360PhosphorylationNSESERRSPSSEDDR
CCCCCCCCCCCCCCH		35.0420873877
362PhosphorylationESERRSPSSEDDRDE
CCCCCCCCCCCCHHH		47.8320873877
363PhosphorylationSERRSPSSEDDRDER
CCCCCCCCCCCHHHH		48.7233259812
382PhosphorylationEIQNAEDYNEIFQPK
HHHCHHHHHHHHCCC		13.2428796482
389UbiquitinationYNEIFQPKNSISRTP
HHHHHCCCCCCCCCC		53.1729967540
391PhosphorylationEIFQPKNSISRTPPR
HHHCCCCCCCCCCCC		28.2430266825
393PhosphorylationFQPKNSISRTPPRRS
HCCCCCCCCCCCCCC		29.8930266825
395PhosphorylationPKNSISRTPPRRSEP
CCCCCCCCCCCCCCC		30.7430266825
400PhosphorylationSRTPPRRSEPFPAPP
CCCCCCCCCCCCCCC		51.4030576142
413PhosphorylationPPEDDAATAKEAAKP
CCCCCHHHHHHHCCC		39.7321712546
421PhosphorylationAKEAAKPSPAMDVQF
HHHHCCCCCCCCCCC		25.2822199227
444PhosphorylationPRPPVVASTPAPKAE
CCCCEEECCCCCCCC		24.2621712546
445PhosphorylationRPPVVASTPAPKAEP
CCCEEECCCCCCCCC		17.4621712546
458O-linked_GlycosylationEPAIIPATRNEPIGL
CCCEEECCCCCCCCC		28.7730379171
466UbiquitinationRNEPIGLKASDFLPA
CCCCCCCCHHHCCCC		40.4029967540
493UbiquitinationDAMSQIRKGHDTMCV
HHHHHHHCCCCCEEE		63.33-
517PhosphorylationDTVRAVWTMGDIKTS
HHEEEEEEHHHHCCC		12.5030576142
558PhosphorylationWKLDLCTTVLPQIEK
HHHHHHHHHHHHHHH		21.0330576142
565UbiquitinationTVLPQIEKLLQSKYE
HHHHHHHHHHHHCHH		57.01-
570UbiquitinationIEKLLQSKYESYVQT
HHHHHHHCHHHHHHH		39.8229967540
571PhosphorylationEKLLQSKYESYVQTG
HHHHHHCHHHHHHHC		18.4924043423
573PhosphorylationLLQSKYESYVQTGCT
HHHHCHHHHHHHCCH		27.7524043423
574PhosphorylationLQSKYESYVQTGCTS
HHHCHHHHHHHCCHH		5.6624043423
577PhosphorylationKYESYVQTGCTSLKL
CHHHHHHHCCHHHHH		24.9524043423
580PhosphorylationSYVQTGCTSLKLILQ
HHHHHCCHHHHHHHH		38.1424043423
581PhosphorylationYVQTGCTSLKLILQR
HHHHCCHHHHHHHHH		27.8124043423
594PhosphorylationQRFLPLITDMLAAPP
HHHHHHHHHHHHCCC		24.0428348404
621AcetylationHKCRLCYKQLKSISG
HHHHHHHHHHHHHHC		48.4325953088
634PhosphorylationSGLVKSKSGLSGRHG
HCHHHCCCCCCCCCC		52.6527251275
637PhosphorylationVKSKSGLSGRHGSTF
HHCCCCCCCCCCHHH		36.9927251275
642PhosphorylationGLSGRHGSTFRELHL
CCCCCCCHHHHHHHH		20.46-
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 KTNB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KTNB1_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 KTNB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KTNB1_HUMANKATNB1physical
10751153
NDEL1_MOUSENdel1physical
16203747
DYHC1_MOUSEDync1h1physical
16203747
LIS1_MOUSEPafah1b1physical
16203747
KTNA1_HUMANKATNA1physical
16203747
PTN2_HUMANPTPN2physical
22939629
MSH3_HUMANMSH3physical
22939629
BTK_HUMANBTKphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616212Lissencephaly 6, with microcephaly (LIS6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KTNB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395, AND MASSSPECTROMETRY.

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