Entity Details

Primary name AT132_HUMAN
Entity type UniProt
Source Source Link

Details

AccessionQ9NQ11
EntryNameAT132_HUMAN
FullNamePolyamine-transporting ATPase 13A2
TaxID9606
Evidenceevidence at protein level
Length1180
SequenceStatuscomplete
DateCreated2001-06-01
DateModified2021-06-02

Ontological Relatives

GenesATP13A2

GO terms

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GOName
GO:0000421 autophagosome membrane
GO:0005524 ATP binding
GO:0005764 lysosome
GO:0005765 lysosomal membrane
GO:0005770 late endosome
GO:0005771 multivesicular body
GO:0005776 autophagosome
GO:0006874 cellular calcium ion homeostasis
GO:0006879 cellular iron ion homeostasis
GO:0006882 cellular zinc ion homeostasis
GO:0006914 autophagy
GO:0007041 lysosomal transport
GO:0008270 zinc ion binding
GO:0010628 positive regulation of gene expression
GO:0010821 regulation of mitochondrion organization
GO:0012506 vesicle membrane
GO:0015417 ABC-type polyamine transporter activity
GO:0016021 integral component of membrane
GO:0016241 regulation of macroautophagy
GO:0016243 regulation of autophagosome size
GO:0016887 ATP hydrolysis activity
GO:0019829 ATPase-coupled cation transmembrane transporter activity
GO:0030003 cellular cation homeostasis
GO:0030133 transport vesicle
GO:0030145 manganese ion binding
GO:0031982 vesicle
GO:0032585 multivesicular body membrane
GO:0033157 regulation of intracellular protein transport
GO:0034220 ion transmembrane transport
GO:0034599 cellular response to oxidative stress
GO:0043005 neuron projection
GO:0043025 neuronal cell body
GO:0043202 lysosomal lumen
GO:0046777 protein autophosphorylation
GO:0050714 positive regulation of protein secretion
GO:0052548 regulation of endopeptidase activity
GO:0055069 zinc ion homeostasis
GO:0055088 lipid homeostasis
GO:0061462 protein localization to lysosome
GO:0061909 autophagosome-lysosome fusion
GO:0070300 phosphatidic acid binding
GO:0071287 cellular response to manganese ion
GO:0071294 cellular response to zinc ion
GO:0080025 phosphatidylinositol-3,5-bisphosphate binding
GO:0097734 extracellular exosome biogenesis
GO:1900180 regulation of protein localization to nucleus
GO:1901215 negative regulation of neuron death
GO:1902047 polyamine transmembrane transport
GO:1903135 cupric ion binding
GO:1903146 regulation of autophagy of mitochondrion
GO:1903543 positive regulation of exosomal secretion
GO:1903710 spermine transmembrane transport
GO:1904714 regulation of chaperone-mediated autophagy
GO:1905037 autophagosome organization
GO:1905103 integral component of lysosomal membrane
GO:1905123 regulation of glucosylceramidase activity
GO:1905165 regulation of lysosomal protein catabolic process
GO:1905166 negative regulation of lysosomal protein catabolic process
GO:1990938 peptidyl-aspartic acid autophosphorylation
GO:2000152 regulation of ubiquitin-specific protease activity

Subcellular Location

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Subcellular Location
Cytoplasmic vesicle
Endosome
Late endosome membrane
Lysosome membrane

Domains

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DomainNameCategoryType
IPR001757 P-type ATPaseFamilyFamily
IPR006544 P-type ATPase, subfamily VFamilyFamily
IPR008250 P-type ATPase, A domain superfamilyFamilyHomologous superfamily
IPR018303 P-type ATPase, phosphorylation sitePTMPTM
IPR023214 HAD superfamilyFamilyHomologous superfamily
IPR023298 P-type ATPase, transmembrane domain superfamilyFamilyHomologous superfamily
IPR023299 P-type ATPase, cytoplasmic domain NFamilyHomologous superfamily
IPR036412 HAD-like superfamilyFamilyHomologous superfamily
IPR044492 P-type ATPase, haloacid dehalogenase domainDomainDomain

Diseases

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Disease IDSourceNameDescription
617225 OMIMSpastic paraplegia 78, autosomal recessive (SPG78)A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. The disease is caused by variants affecting the gene represented in this entry.
606693 OMIMKufor-Rakeb syndrome (KRS)A rare form of autosomal recessive juvenile or early-onset, levodopa-responsive parkinsonism. In addition to typical parkinsonian signs, clinical manifestations of Kufor-Rakeb syndrome include behavioral problems, facial tremor, pyramidal tract dysfunction, supranuclear gaze palsy, and dementia. The disease is caused by variants affecting the gene represented in this entry. KRS has also been referred to as neuronal ceroid lipofuscinosis 12 (CLN12), due to neuronal and glial lipofuscin deposits detected in the cortex, basal nuclei and cerebellum of some patients.

Interactions

49 interactions

InteractorPartnerSourcesPublicationsLink
AT132_HUMANCKLF6_HUMANBioGRID, MINT21900206 details
AT132_HUMANACTB_HUMANIntAct22645275 details
AT132_HUMANSC61B_HUMANBioGRID, IntAct22645275 details
AT132_HUMANPDIA6_HUMANBioGRID, IntAct22645275 details
AT132_HUMANASTER_HUMANBioGRID, IntAct22645275 details
AT132_HUMANDCAF7_HUMANBioGRID, IntAct22645275 details
AT132_HUMANHIPK1_HUMANBioGRID, IntAct22645275 details
AT132_HUMANLRP6_HUMANBioGRID, IntAct22645275 details
AT132_HUMANICAM2_HUMANBioGRID, IntAct22645275 details
AT132_HUMANGPR21_HUMANBioGRID, IntAct22645275 details
AT132_HUMANP_HUMANBioGRID, IntAct22645275 details
AT132_HUMANAT5G2_HUMANBioGRID, IntAct22645275 details
AT132_HUMANBNI3L_HUMANBioGRID, IntAct22645275 details
AT132_HUMANHDAC6_HUMANBioGRID, IntAct22645275 details
AT132_HUMANVAMP2_HUMANBioGRID, IntAct22645275 details
AT132_HUMANNPY1R_HUMANBioGRID, IntAct22645275 details
AT132_HUMANLMAN2_HUMANBioGRID, IntAct22645275 details
AT132_HUMANEMC7_HUMANBioGRID, IntAct22645275 details
AT132_HUMANHSP7C_HUMANBioGRID, IntAct22645275 details
AT132_HUMANFUND2_HUMANBioGRID, IntAct22645275 details
AT132_HUMANSPCS2_HUMANBioGRID, IntAct22645275 details
AT132_HUMANAAK1_HUMANBioGRID, IntAct22645275 details
AT132_HUMANFA8A1_HUMANBioGRID, IntAct22645275 details
AT132_HUMANGAK_HUMANBioGRID, IntAct22645275 details
AT132_HUMANF111B_HUMANBioGRID, IntAct22645275 details
AT132_HUMANUB2J2_HUMANBioGRID, IntAct22645275 details
AT132_HUMANPCMD2_HUMANBioGRID, IntAct22645275 details
AT132_HUMANOSTC_HUMANBioGRID, IntAct22645275 details
AT132_HUMANFKBP8_HUMANBioGRID, IntAct22645275 details
AT132_HUMANCXCR4_HUMANBioGRID, IntAct22645275 details
AT132_HUMANYIF1A_HUMANBioGRID, IntAct22645275 details
AT132_HUMANMYCB2_HUMANBioGRID, IntAct22645275 details
AT132_HUMANACKR3_HUMANBioGRID, IntAct22645275 details
AT132_HUMANPIP30_HUMANBioGRID, IntAct22645275 details
AT132_HUMANCO1A1_HUMANBioGRID, IntAct22645275 details
AT132_HUMANWDR5B_HUMANBioGRID, IntAct22645275 details
AT132_HUMANCYGB_HUMANBioGRID, IntAct22645275 details
AT132_HUMANMEX3B_HUMANBioGRID, IntAct22645275 details
AT132_HUMANTSN14_HUMANBioGRID, IntAct22645275 details
AT132_HUMANGASR_HUMANBioGRID, IntAct22645275 details
AT132_HUMANPCDBA_HUMANBioGRID, IntAct22645275 details
AT132_HUMANSYT11_HUMANBioGRID, IntAct22645275 details
AT132_HUMANPAR1_HUMANBioGRID, IntAct22645275 details
AT132_HUMANNRX1B_HUMANBioGRID22645275 details
AT132_HUMANNRX1A_HUMANBioGRID22645275 details
AT132_HUMANLAMP1_HUMANBioGRID22768177 details
AT132_HUMANRAB5A_HUMANBioGRID22768177 details
AT132_HUMANRAB7A_HUMANBioGRID22768177 details
AT132_HUMANRAB9A_HUMANBioGRID22768177 details