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Protein

Cation-transporting ATPase 13A2

Gene

ATP13A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATPase that plays a role in intracellular cation homeostasis and the maintenance of neuronal integrity (PubMed:22186024). Required for a proper lysosomal and mitochondrial maintenance (PubMed:22296644, PubMed:28137957).3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei5134-aspartylphosphate intermediateBy similarity1
Metal bindingi878MagnesiumBy similarity1
Metal bindingi882MagnesiumBy similarity1

GO - Molecular functioni

  • ATPase activity Source: ParkinsonsUK-UCL
  • ATP binding Source: UniProtKB-KW
  • calcium-transporting ATPase activity Source: GO_Central
  • cation-transporting ATPase activity Source: Reactome
  • cupric ion binding Source: ParkinsonsUK-UCL
  • manganese ion binding Source: ParkinsonsUK-UCL
  • phosphatidic acid binding Source: ParkinsonsUK-UCL
  • phosphatidylinositol-3,5-bisphosphate binding Source: ParkinsonsUK-UCL
  • zinc ion binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • autophagosome organization Source: ParkinsonsUK-UCL
  • cellular calcium ion homeostasis Source: ParkinsonsUK-UCL
  • cellular cation homeostasis Source: ParkinsonsUK-UCL
  • cellular iron ion homeostasis Source: ParkinsonsUK-UCL
  • cellular response to manganese ion Source: ParkinsonsUK-UCL
  • cellular response to oxidative stress Source: ParkinsonsUK-UCL
  • cellular response to zinc ion Source: ParkinsonsUK-UCL
  • cellular zinc ion homeostasis Source: ParkinsonsUK-UCL
  • ion transmembrane transport Source: Reactome
  • negative regulation of lysosomal protein catabolic process Source: ParkinsonsUK-UCL
  • negative regulation of neuron death Source: ParkinsonsUK-UCL
  • peptidyl-aspartic acid autophosphorylation Source: ParkinsonsUK-UCL
  • polyamine import Source: ParkinsonsUK-UCL
  • positive regulation of exosomal secretion Source: ParkinsonsUK-UCL
  • positive regulation of protein secretion Source: ParkinsonsUK-UCL
  • protein autophosphorylation Source: ParkinsonsUK-UCL
  • regulation of autophagosome size Source: ParkinsonsUK-UCL
  • regulation of chaperone-mediated autophagy Source: ParkinsonsUK-UCL
  • regulation of endopeptidase activity Source: ParkinsonsUK-UCL
  • regulation of glucosylceramidase activity Source: Ensembl
  • regulation of intracellular protein transport Source: ParkinsonsUK-UCL
  • regulation of lysosomal protein catabolic process Source: ParkinsonsUK-UCL
  • regulation of macroautophagy Source: ParkinsonsUK-UCL
  • regulation of mitochondrion organization Source: ParkinsonsUK-UCL
  • regulation of mitophagy Source: ParkinsonsUK-UCL
  • zinc ion homeostasis Source: ParkinsonsUK-UCL

Keywordsi

Molecular functionHydrolase
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-936837. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.10.7. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cation-transporting ATPase 13A2 (EC:3.6.3.-)
Gene namesi
Name:ATP13A2Imported
Synonyms:PARK91 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30213. ATP13A2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
Transmembranei13 – 34HelicalSequence analysisAdd BLAST22
Topological domaini35 – 45ExtracellularSequence analysisAdd BLAST11
Transmembranei46 – 66HelicalSequence analysisAdd BLAST21
Topological domaini67 – 230CytoplasmicSequence analysisAdd BLAST164
Transmembranei231 – 253HelicalSequence analysisAdd BLAST23
Topological domaini254 – 256ExtracellularSequence analysis3
Transmembranei257 – 276HelicalSequence analysisAdd BLAST20
Topological domaini277 – 425CytoplasmicSequence analysisAdd BLAST149
Transmembranei426 – 445HelicalSequence analysisAdd BLAST20
Topological domaini446 – 459ExtracellularSequence analysisAdd BLAST14
Transmembranei460 – 480HelicalSequence analysisAdd BLAST21
Topological domaini481 – 932CytoplasmicSequence analysisAdd BLAST452
Transmembranei933 – 952HelicalSequence analysisAdd BLAST20
Topological domaini953 – 963ExtracellularSequence analysisAdd BLAST11
Transmembranei964 – 981HelicalSequence analysisAdd BLAST18
Topological domaini982 – 997CytoplasmicSequence analysisAdd BLAST16
Transmembranei998 – 1018HelicalSequence analysisAdd BLAST21
Topological domaini1019 – 1046ExtracellularSequence analysisAdd BLAST28
Transmembranei1047 – 1066HelicalSequence analysisAdd BLAST20
Topological domaini1067 – 1079CytoplasmicSequence analysisAdd BLAST13
Transmembranei1080 – 1097HelicalSequence analysisAdd BLAST18
Topological domaini1098 – 1113ExtracellularSequence analysisAdd BLAST16
Transmembranei1114 – 1134HelicalSequence analysisAdd BLAST21
Topological domaini1135 – 1180CytoplasmicSequence analysisAdd BLAST46

GO - Cellular componenti

  • autophagosome Source: ParkinsonsUK-UCL
  • integral component of lysosomal membrane Source: ParkinsonsUK-UCL
  • integral component of membrane Source: ParkinsonsUK-UCL
  • integral component of plasma membrane Source: GO_Central
  • late endosome Source: ParkinsonsUK-UCL
  • lysosomal lumen Source: Reactome
  • lysosomal membrane Source: UniProtKB
  • lysosome Source: UniProtKB
  • multivesicular body Source: ParkinsonsUK-UCL
  • multivesicular body membrane Source: ParkinsonsUK-UCL
  • neuronal cell body Source: ParkinsonsUK-UCL
  • neuron projection Source: ParkinsonsUK-UCL
  • transport vesicle Source: ParkinsonsUK-UCL
  • vesicle Source: ParkinsonsUK-UCL
  • vesicle membrane Source: Ensembl

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Kufor-Rakeb syndrome (KRS)10 Publications
The disease is caused by mutations 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.1 Publication
Disease descriptionA 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.
See also OMIM:606693
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05845112T → M in KRS; no effect on stability; no effect on location; decreased ATPase activity. 2 PublicationsCorresponds to variant dbSNP:rs151117874Ensembl.1
Natural variantiVAR_066019182F → L in KRS; decreased protein stability; loss of autophosphorylation; increased degradation by proteasome; novel location to endoplasmic reticulum; loss of lysosomal membrane location. 3 Publications1
Natural variantiVAR_058455504G → R in KRS; decreased protein stability; increased degradation by proteasome; novel location to endoplasmic reticulum; loss of lysosomal membrane location. 2 PublicationsCorresponds to variant dbSNP:rs121918227Ensembl.1
Natural variantiVAR_078056522G → V in KRS; unknown pathological significance. 1 Publication1
Natural variantiVAR_058456533G → R in a patient with early onset Parkinson disease and KRS; decreased ATPase activity; no effect on autophosphorylation; no effect on stability; no effect on location. 3 Publications1
Natural variantiVAR_058458746A → T in KRS; decreased ATPase activity; no effect on stability; no effect on location. 2 PublicationsCorresponds to variant dbSNP:rs147277743Ensembl.1
Natural variantiVAR_070194854M → R in KRS; some patients manifest neuropathologic findings suggestive of neuronal ceroid lipofuscinosis. 1 PublicationCorresponds to variant dbSNP:rs587777053Ensembl.1
Natural variantiVAR_066020877G → R in KRS; found in two affected brothers also carrying C-481 in FBXO7; decreased protein stability; increased degradation by proteasome; novel location to endoplasmic reticulum. 2 PublicationsCorresponds to variant dbSNP:rs144701072Ensembl.1
Natural variantiVAR_0660211059L → R in KRS; the mutant protein is retained in the endoplasmic reticulum. 1 PublicationCorresponds to variant dbSNP:rs137853967Ensembl.1
Spastic paraplegia 78, autosomal recessive (SPG78)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:617225
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078055517T → I in SPG78; no effect on protein stability; loss of autophosphorylation; loss of lysosomal location. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi513D → N: Loss of ATPase function. 1 Publication1

Keywords - Diseasei

Disease mutation, Hereditary spastic paraplegia, Neurodegeneration, Neuronal ceroid lipofuscinosis, Parkinsonism

Organism-specific databases

DisGeNETi23400.
MalaCardsiATP13A2.
MIMi606693. phenotype.
617225. phenotype.
OpenTargetsiENSG00000159363.
Orphaneti306674. Kufor-Rakeb syndrome.
314632. Parkinsonim due to ATP13A2 deficiency.
PharmGKBiPA134897221.

Polymorphism and mutation databases

BioMutaiATP13A2.
DMDMi14285364.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000464231 – 1180Cation-transporting ATPase 13A2Add BLAST1180

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei151PhosphoserineCombined sources1

Post-translational modificationi

Autophosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NQ11.
PaxDbiQ9NQ11.
PeptideAtlasiQ9NQ11.
PRIDEiQ9NQ11.

PTM databases

iPTMnetiQ9NQ11.
PhosphoSitePlusiQ9NQ11.

Expressioni

Tissue specificityi

Expressed in brain; protein levels are markedly increased in brain from subjects with Parkinson disease and subjects with dementia with Lewy bodies. Detected in pyramidal neurons located throughout the cingulate cortex (at protein level). In the substantia nigra, it is found in neuromelanin-positive dopaminergic neurons (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000159363.
CleanExiHS_ATP13A2.
ExpressionAtlasiQ9NQ11. baseline and differential.
GenevisibleiQ9NQ11. HS.

Organism-specific databases

HPAiCAB037038.
CAB037111.
HPA050910.
HPA054717.

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi116973. 71 interactors.
IntActiQ9NQ11. 49 interactors.
MINTiMINT-4781194.
STRINGi9606.ENSP00000327214.

Structurei

3D structure databases

ProteinModelPortaliQ9NQ11.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0208. Eukaryota.
ENOG410XRCA. LUCA.
GeneTreeiENSGT00530000063001.
HOGENOMiHOG000171813.
HOVERGENiHBG065757.
InParanoidiQ9NQ11.
KOiK13526.
OMAiPYCPETH.
OrthoDBiEOG091G01IL.
PhylomeDBiQ9NQ11.
TreeFamiTF300331.

Family and domain databases

Gene3Di3.40.1110.10. 1 hit.
InterProiView protein in InterPro
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006544. P-type_TPase_V.
IPR001757. P_typ_ATPase.
PfamiView protein in Pfam
PF12409. P5-ATPase. 1 hit.
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81653. SSF81653. 1 hit.
SSF81660. SSF81660. 2 hits.
SSF81665. SSF81665. 3 hits.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEiView protein in PROSITE
PS00154. ATPASE_E1_E2. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q9NQ11-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSADSSPLVG STPTGYGTLT IGTSIDPLSS SVSSVRLSGY CGSPWRVIGY
60 70 80 90 100
HVVVWMMAGI PLLLFRWKPL WGVRLRLRPC NLAHAETLVI EIRDKEDSSW
110 120 130 140 150
QLFTVQVQTE AIGEGSLEPS PQSQAEDGRS QAAVGAVPEG AWKDTAQLHK
160 170 180 190 200
SEEAVSVGQK RVLRYYLFQG QRYIWIETQQ AFYQVSLLDH GRSCDDVHRS
210 220 230 240 250
RHGLSLQDQM VRKAIYGPNV ISIPVKSYPQ LLVDEALNPY YGFQAFSIAL
260 270 280 290 300
WLADHYYWYA LCIFLISSIS ICLSLYKTRK QSQTLRDMVK LSMRVCVCRP
310 320 330 340 350
GGEEEWVDSS ELVPGDCLVL PQEGGLMPCD AALVAGECMV NESSLTGESI
360 370 380 390 400
PVLKTALPEG LGPYCAETHR RHTLFCGTLI LQARAYVGPH VLAVVTRTGF
410 420 430 440 450
CTAKGGLVSS ILHPRPINFK FYKHSMKFVA ALSVLALLGT IYSIFILYRN
460 470 480 490 500
RVPLNEIVIR ALDLVTVVVP PALPAAMTVC TLYAQSRLRR QGIFCIHPLR
510 520 530 540 550
INLGGKLQLV CFDKTGTLTE DGLDVMGVVP LKGQAFLPLV PEPRRLPVGP
560 570 580 590 600
LLRALATCHA LSRLQDTPVG DPMDLKMVES TGWVLEEEPA ADSAFGTQVL
610 620 630 640 650
AVMRPPLWEP QLQAMEEPPV PVSVLHRFPF SSALQRMSVV VAWPGATQPE
660 670 680 690 700
AYVKGSPELV AGLCNPETVP TDFAQMLQSY TAAGYRVVAL ASKPLPTVPS
710 720 730 740 750
LEAAQQLTRD TVEGDLSLLG LLVMRNLLKP QTTPVIQALR RTRIRAVMVT
760 770 780 790 800
GDNLQTAVTV ARGCGMVAPQ EHLIIVHATH PERGQPASLE FLPMESPTAV
810 820 830 840 850
NGVKDPDQAA SYTVEPDPRS RHLALSGPTF GIIVKHFPKL LPKVLVQGTV
860 870 880 890 900
FARMAPEQKT ELVCELQKLQ YCVGMCGDGA NDCGALKAAD VGISLSQAEA
910 920 930 940 950
SVVSPFTSSM ASIECVPMVI REGRCSLDTS FSVFKYMALY SLTQFISVLI
960 970 980 990 1000
LYTINTNLGD LQFLAIDLVI TTTVAVLMSR TGPALVLGRV RPPGALLSVP
1010 1020 1030 1040 1050
VLSSLLLQMV LVTGVQLGGY FLTLAQPWFV PLNRTVAAPD NLPNYENTVV
1060 1070 1080 1090 1100
FSLSSFQYLI LAAAVSKGAP FRRPLYTNVP FLVALALLSS VLVGLVLVPG
1110 1120 1130 1140 1150
LLQGPLALRN ITDTGFKLLL LGLVTLNFVG AFMLESVLDQ CLPACLRRLR
1160 1170 1180
PKRASKKRFK QLERELAEQP WPPLPAGPLR
Length:1,180
Mass (Da):128,794
Last modified:June 1, 2001 - v2
Checksum:i98D13745D3B615BE
GO
Isoform B (identifier: Q9NQ11-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.
     805-843: Missing.
     1079-1180: VPFLVALALL...WPPLPAGPLR → ERARPVPPRL...PQLPSVLLSV

Show »
Length:1,158
Mass (Da):125,977
Checksum:i1A7D35DF1CD34396
GO
Isoform 3 (identifier: Q9NQ11-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.

Show »
Length:1,175
Mass (Da):128,323
Checksum:i6418CB82F086E30C
GO

Sequence cautioni

The sequence CAA08912 differs from that shown. Reason: Frameshift at position 1054.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti322Q → R in AAH30267 (PubMed:15489334).Curated1
Sequence conflicti855 – 858APEQ → IPRA in CAA08912 (Ref. 8) Curated4
Sequence conflicti861E → V in CAA08912 (Ref. 8) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05845112T → M in KRS; no effect on stability; no effect on location; decreased ATPase activity. 2 PublicationsCorresponds to variant dbSNP:rs151117874Ensembl.1
Natural variantiVAR_05845249G → S1 PublicationCorresponds to variant dbSNP:rs56379718Ensembl.1
Natural variantiVAR_066019182F → L in KRS; decreased protein stability; loss of autophosphorylation; increased degradation by proteasome; novel location to endoplasmic reticulum; loss of lysosomal membrane location. 3 Publications1
Natural variantiVAR_058453294R → Q1 PublicationCorresponds to variant dbSNP:rs56367069Ensembl.1
Natural variantiVAR_058454389P → L1 PublicationCorresponds to variant dbSNP:rs56275621Ensembl.1
Natural variantiVAR_058455504G → R in KRS; decreased protein stability; increased degradation by proteasome; novel location to endoplasmic reticulum; loss of lysosomal membrane location. 2 PublicationsCorresponds to variant dbSNP:rs121918227Ensembl.1
Natural variantiVAR_078055517T → I in SPG78; no effect on protein stability; loss of autophosphorylation; loss of lysosomal location. 1 Publication1
Natural variantiVAR_078056522G → V in KRS; unknown pathological significance. 1 Publication1
Natural variantiVAR_058456533G → R in a patient with early onset Parkinson disease and KRS; decreased ATPase activity; no effect on autophosphorylation; no effect on stability; no effect on location. 3 Publications1
Natural variantiVAR_058457578V → G1 PublicationCorresponds to variant dbSNP:rs56186751Ensembl.1
Natural variantiVAR_058458746A → T in KRS; decreased ATPase activity; no effect on stability; no effect on location. 2 PublicationsCorresponds to variant dbSNP:rs147277743Ensembl.1
Natural variantiVAR_058459762R → W1 PublicationCorresponds to variant dbSNP:rs55635527Ensembl.1
Natural variantiVAR_058460776V → I1 PublicationCorresponds to variant dbSNP:rs56170027Ensembl.1
Natural variantiVAR_070194854M → R in KRS; some patients manifest neuropathologic findings suggestive of neuronal ceroid lipofuscinosis. 1 PublicationCorresponds to variant dbSNP:rs587777053Ensembl.1
Natural variantiVAR_066020877G → R in KRS; found in two affected brothers also carrying C-481 in FBXO7; decreased protein stability; increased degradation by proteasome; novel location to endoplasmic reticulum. 2 PublicationsCorresponds to variant dbSNP:rs144701072Ensembl.1
Natural variantiVAR_058461946I → F1 PublicationCorresponds to variant dbSNP:rs55708915Ensembl.1
Natural variantiVAR_0660211059L → R in KRS; the mutant protein is retained in the endoplasmic reticulum. 1 PublicationCorresponds to variant dbSNP:rs137853967Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_007310155 – 159Missing in isoform B and isoform 3. 4 Publications5
Alternative sequenceiVSP_007311805 – 843Missing in isoform B. 2 PublicationsAdd BLAST39
Alternative sequenceiVSP_0073121079 – 1180VPFLV…AGPLR → ERARPVPPRLPAPPPAQAGL QEALQAAGTRAGRAALAAAA RRPPEVVQAHGHPRHWNSLP LSHQLDPSPATPPPPPPTSL RLATVYTPPPRPPPPWGSVD YCPLPWTIPRRGGSPQLPSV LLSV in isoform B. 2 PublicationsAdd BLAST102

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL354615 mRNA. Translation: CAB89728.1.
AY461712 mRNA. Translation: AAR23423.1.
AK290210 mRNA. Translation: BAF82899.1.
AL049569 Genomic DNA. Translation: CAI20366.1.
CH471134 Genomic DNA. Translation: EAW94825.1.
CH471134 Genomic DNA. Translation: EAW94827.1.
BC030267 mRNA. Translation: AAH30267.1.
AL833966 mRNA. Translation: CAD38813.2.
AJ009947 mRNA. Translation: CAA08912.1. Frameshift.
CCDSiCCDS175.1. [Q9NQ11-1]
CCDS44072.1. [Q9NQ11-2]
CCDS44073.1. [Q9NQ11-3]
RefSeqiNP_001135445.1. NM_001141973.2. [Q9NQ11-3]
NP_001135446.1. NM_001141974.2. [Q9NQ11-2]
NP_071372.1. NM_022089.3. [Q9NQ11-1]
UniGeneiHs.128866.

Genome annotation databases

EnsembliENST00000326735; ENSP00000327214; ENSG00000159363. [Q9NQ11-1]
ENST00000341676; ENSP00000341115; ENSG00000159363. [Q9NQ11-2]
ENST00000452699; ENSP00000413307; ENSG00000159363. [Q9NQ11-3]
GeneIDi23400.
KEGGihsa:23400.
UCSCiuc001baa.3. human. [Q9NQ11-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiAT132_HUMAN
AccessioniPrimary (citable) accession number: Q9NQ11
Secondary accession number(s): O75700
, Q5JXY1, Q5JXY2, Q6S9Z9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: July 5, 2017
This is version 159 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families