KATL1_HUMAN - dbPTM
KATL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KATL1_HUMAN
UniProt AC Q9BW62
Protein Name Katanin p60 ATPase-containing subunit A-like 1 {ECO:0000255|HAMAP-Rule:MF_03024}
Gene Name KATNAL1 {ECO:0000255|HAMAP-Rule:MF_03024}
Organism Homo sapiens (Human).
Sequence Length 490
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton, spindle . Colocalizes with microtubules throughout the basal and adluminal compartments of Sertoli cells (By similarity). Localizes within the cyto
Protein Description Regulates microtubule dynamics in Sertoli cells, a process that is essential for spermiogenesis and male fertility. Severs microtubules in an ATP-dependent manner, promoting rapid reorganization of cellular microtubule arrays (By similarity). Has microtubule-severing activity in vitro. [PubMed: 26929214]
Protein Sequence MNLAEICDNAKKGREYALLGNYDSSMVYYQGVMQQIQRHCQSVRDPAIKGKWQQVRQELLEEYEQVKSIVSTLESFKIDKPPDFPVSCQDEPFRDPAVWPPPVPAEHRAPPQIRRPNREVRPLRKEMAGVGARGPVGRAHPISKSEKPSTSRDKDYRARGRDDKGRKNMQDGASDGEMPKFDGAGYDKDLVEALERDIVSRNPSIHWDDIADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVGGALENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPTAKGRAELLKINLREVELDPDIQLEDIAEKIEGYSGADITNVCRDASLMAMRRRINGLSPEEIRALSKEELQMPVTKGDFELALKKIAKSVSAADLEKYEKWMVEFGSA
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-------MNLAEICD
-------CCHHHHHH
9.2922814378
63PhosphorylationRQELLEEYEQVKSIV
HHHHHHHHHHHHHHH
11.4229978859
133MethylationEMAGVGARGPVGRAH
HHCCCCCCCCCCCCC
43.98115480835
138MethylationGARGPVGRAHPISKS
CCCCCCCCCCCCCCC
29.9224381695
174PhosphorylationKNMQDGASDGEMPKF
CCCCCCCCCCCCCCC
52.2425850435
186PhosphorylationPKFDGAGYDKDLVEA
CCCCCCCCCHHHHHH
21.20-
188UbiquitinationFDGAGYDKDLVEALE
CCCCCCCHHHHHHHH
44.47-
204PhosphorylationDIVSRNPSIHWDDIA
HHHHCCCCCCHHHCC
30.5420873877
217UbiquitinationIADLEEAKKLLREAV
CCCHHHHHHHHHHHC
47.43-
255PhosphorylationGPPGTGKTMLAKAVA
CCCCCCHHHHHHHHH
20.8224719451
280UbiquitinationSSSTLTSKYRGESEK
CCCHHCCCCCCCHHH
33.46-
285PhosphorylationTSKYRGESEKLVRLL
CCCCCCCHHHHHHHH
42.7428270605
382PhosphorylationRIYIPLPTAKGRAEL
CCCCCCCCCCCHHHH
49.0024719451
421PhosphorylationGYSGADITNVCRDAS
CCCCCCHHHHHHHHH
23.34-
440PhosphorylationRRRINGLSPEEIRAL
HHHHCCCCHHHHHHC
31.5030266825
473PhosphorylationKKIAKSVSAADLEKY
HHHHHCCCHHHHHHH
25.4926471730

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 KATL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KATL1_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 KATL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KATL1_HUMANKATNAL1physical
25416956
KLC4_HUMANKLC4physical
25416956
CE57L_HUMANCEP57L1physical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KATL1_HUMAN

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Related Literatures of Post-Translational Modification

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