Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NTI2 (AT8A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipid-transporting ATPase IB

EC=3.6.3.1
Alternative name(s):
ATPase class I type 8A member 2
ML-1
P4-ATPase flippase complex alpha subunit ATP8A2
Gene names
Name:ATP8A2
Synonyms:ATPIB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1148 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Involved in regulation of neurite outgrowth; acting in synergy with TMEM30A. Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival.

Catalytic activity

ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).

Enzyme regulation

ATPase activity is stimulated by phosphatidylserine (PS) and minimally by phosphatidylethanolamine (PE). ATPase activity is inhibited by N-ethylmaleimide (NEM) and vanadate. Flippase activity is inhibited by NEM and 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS) By similarity.

Subunit structure

Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. Interacts with TMEM30A to form a flippase complex. Ref.7 Ref.8

Subcellular location

Membrane; Multi-pass membrane protein Potential. Golgi apparatus. Endosome By similarity. Cell projectionciliumphotoreceptor outer segment By similarity. Cell membrane. Note: Localizes to the Golgi and endosomes in photoreceptor cells. Localizes to disk membranes of rod photoreceptor outer segments (ROS) By similarity. Ref.7

Tissue specificity

Strongly expressed in the brain, cerebellum, retina and testis. Ref.6 Ref.9

Involvement in disease

Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 4 (CMARQ4) [MIM:615268]: A congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

A chromosomal aberration disrupting ATP8A2 has been found in a patient with severe mental retardation and major hypotonia. Translocation t(10;13)(p12.1;q12.13) (Ref.6).

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]

Sequence caution

The sequence BAC04396.1 differs from that shown. Reason: Erroneous initiation.

Isoform 2: The sequence AAF40215.2 differs from that shown. Reason: Frameshift at position 522.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentCell membrane
Cell projection
Endosome
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Inferred from electronic annotation. Source: Ensembl

eating behavior

Inferred from electronic annotation. Source: Ensembl

involuntary skeletal muscle contraction

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Traceable author statement Ref.3. Source: ProtInc

neuromuscular process controlling posture

Inferred from electronic annotation. Source: Ensembl

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

skin development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cation-transporting ATPase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

phospholipid-translocating ATPase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NTI2-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q9NTI2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     515-528: MGQEQTFGILNVLE → VSNMRVHISDHLLL
     529-1148: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11481148Phospholipid-transporting ATPase IB
PRO_0000046362

Regions

Topological domain1 – 4444Cytoplasmic Potential
Transmembrane45 – 6622Helical; Potential
Topological domain67 – 715Exoplasmic loop Potential
Transmembrane72 – 9423Helical; Potential
Topological domain95 – 276182Cytoplasmic Potential
Transmembrane277 – 29822Helical; Potential
Topological domain299 – 32325Exoplasmic loop Potential
Transmembrane324 – 34522Helical; Potential
Topological domain346 – 837492Cytoplasmic Potential
Transmembrane838 – 85821Helical; Potential
Topological domain859 – 87012Exoplasmic loop Potential
Transmembrane871 – 89020Helical; Potential
Topological domain891 – 92030Cytoplasmic Potential
Transmembrane921 – 94222Helical; Potential
Topological domain943 – 95614Exoplasmic loop Potential
Transmembrane957 – 97923Helical; Potential
Topological domain980 – 9856Cytoplasmic Potential
Transmembrane986 – 100621Helical; Potential
Topological domain1007 – 102418Exoplasmic loop Potential
Transmembrane1025 – 104925Helical; Potential
Topological domain1050 – 114899Cytoplasmic Potential

Sites

Active site38814-aspartylphosphate intermediate By similarity
Metal binding7811Magnesium By similarity
Metal binding7851Magnesium By similarity

Natural variations

Alternative sequence515 – 52814MGQEQ…LNVLE → VSNMRVHISDHLLL in isoform 2.
VSP_037646
Alternative sequence529 – 1148620Missing in isoform 2.
VSP_037647
Natural variant3361I → M in CMARQ4. Ref.9
VAR_069928
Natural variant10291A → T.
Corresponds to variant rs2296242 [ dbSNP | Ensembl ].
VAR_055543

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: E9F363B568C7EE82

FASTA1,148129,242
        10         20         30         40         50         60 
MSRATSVGDQ LEAPARTIYL NQPHLNKFRD NQISTAKYSV LTFLPRFLYE QIRRAANAFF 

        70         80         90        100        110        120 
LFIALLQQIP DVSPTGRYTT LVPLIIILTI AGIKEIVEDF KRHKADNAVN KKKTIVLRNG 

       130        140        150        160        170        180 
MWHTIMWKEV AVGDIVKVVN GQYLPADVVL LSSSEPQAMC YVETANLDGE TNLKIRQGLS 

       190        200        210        220        230        240 
HTADMQTREV LMKLSGTIEC EGPNRHLYDF TGNLNLDGKS LVALGPDQIL LRGTQLRNTQ 

       250        260        270        280        290        300 
WVFGIVVYTG HDTKLMQNST KAPLKRSNVE KVTNVQILVL FGILLVMALV SSAGALYWNR 

       310        320        330        340        350        360 
SHGEKNWYIK KMDTTSDNFG YNLLTFIILY NNLIPISLLV TLEVVKYTQA LFINWDTDMY 

       370        380        390        400        410        420 
YIGNDTPAMA RTSNLNEELG QVKYLFSDKT GTLTCNIMNF KKCSIAGVTY GHFPELAREP 

       430        440        450        460        470        480 
SSDDFCRMPP PCSDSCDFDD PRLLKNIEDR HPTAPCIQEF LTLLAVCHTV VPEKDGDNII 

       490        500        510        520        530        540 
YQASSPDEAA LVKGAKKLGF VFTARTPFSV IIEAMGQEQT FGILNVLEFS SDRKRMSVIV 

       550        560        570        580        590        600 
RTPSGRLRLY CKGADNVIFE RLSKDSKYME ETLCHLEYFA TEGLRTLCVA YADLSENEYE 

       610        620        630        640        650        660 
EWLKVYQEAS TILKDRAQRL EECYEIIEKN LLLLGATAIE DRLQAGVPET IATLLKAEIK 

       670        680        690        700        710        720 
IWVLTGDKQE TAINIGYSCR LVSQNMALIL LKEDSLDATR AAITQHCTDL GNLLGKENDV 

       730        740        750        760        770        780 
ALIIDGHTLK YALSFEVRRS FLDLALSCKA VICCRVSPLQ KSEIVDVVKK RVKAITLAIG 

       790        800        810        820        830        840 
DGANDVGMIQ TAHVGVGISG NEGMQATNNS DYAIAQFSYL EKLLLVHGAW SYNRVTKCIL 

       850        860        870        880        890        900 
YCFYKNVVLY IIELWFAFVN GFSGQILFER WCIGLYNVIF TALPPFTLGI FERSCTQESM 

       910        920        930        940        950        960 
LRFPQLYKIT QNGEGFNTKV FWGHCINALV HSLILFWFPM KALEHDTVLT SGHATDYLFV 

       970        980        990       1000       1010       1020 
GNIVYTYVVV TVCLKAGLET TAWTKFSHLA VWGSMLTWLV FFGIYSTIWP TIPIAPDMRG 

      1030       1040       1050       1060       1070       1080 
QATMVLSSAH FWLGLFLVPT ACLIEDVAWR AAKHTCKKTL LEEVQELETK SRVLGKAVLR 

      1090       1100       1110       1120       1130       1140 
DSNGKRLNER DRLIKRLGRK TPPTLFRGSS LQQGVPHGYA FSQEEHGAVS QEEVIRAYDT 


TKKKSRKK 

« Hide

Isoform 2 [UniParc].

Checksum: 1CAD4BDC7B38F391
Show »

FASTA52859,296

References

« Hide 'large scale' references
[1]Sun X.L., Milo G.E., Li D.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Changes in levels of normal ML-1 gene transcripts associated with the conversion of human nontumorigenic to tumorigenic phenotypes."
Sun X.L., Li D., Fang J., Noyes I., Casto B., Theil K., Shuler C., Milo G.E.
Gene Expr. 8:129-139(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-1148 (ISOFORM 1).
Tissue: Amygdala and Testis.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-1148 (ISOFORM 1).
Tissue: Amygdala.
[6]"Disruption of the ATP8A2 gene in a patient with a t(10;13) de novo balanced translocation and a severe neurological phenotype."
Cacciagli P., Haddad M.R., Mignon-Ravix C., El-Waly B., Moncla A., Missirian C., Chabrol B., Villard L.
Eur. J. Hum. Genet. 18:1360-1363(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION.
[7]"Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases."
van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A., Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.
J. Biol. Chem. 285:40088-40096(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM30A, SUBCELLULAR LOCATION.
[8]"Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization, and lipid transport activity of the P4-ATPase ATP8A2."
Coleman J.A., Molday R.S.
J. Biol. Chem. 286:17205-17216(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM30A.
[9]"Missense mutation in the ATPase, aminophospholipid transporter protein ATP8A2 is associated with cerebellar atrophy and quadrupedal locomotion."
Onat O.E., Gulsuner S., Bilguvar K., Nazli Basak A., Topaloglu H., Tan M., Tan U., Gunel M., Ozcelik T.
Eur. J. Hum. Genet. 21:281-285(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, VARIANT CMARQ4 MET-336.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF236871 mRNA. Translation: AAF40215.2. Frameshift.
AL138815 expand/collapse EMBL AC list , AL136438, AL138958, AL157366, AL356316, AL669971 Genomic DNA. Translation: CAH70513.1.
AL138958 expand/collapse EMBL AC list , AL136438, AL138815, AL157366, AL356316, AL669971 Genomic DNA. Translation: CAH71291.1.
AL157366 expand/collapse EMBL AC list , AL136438, AL138815, AL138958, AL356316, AL669971 Genomic DNA. Translation: CAH74073.1.
AL356316 expand/collapse EMBL AC list , AL136438, AL138815, AL138958, AL157366, AL669971 Genomic DNA. Translation: CAH70876.1.
AL669971 expand/collapse EMBL AC list , AL136438, AL138815, AL138958, AL157366, AL356316 Genomic DNA. Translation: CAH73647.1.
AL136438 expand/collapse EMBL AC list , AL138815, AL138958, AL157366, AL356316, AL669971 Genomic DNA. Translation: CAH70146.1.
AL137256 mRNA. Translation: CAB70658.1.
AL390129 mRNA. Translation: CAB99084.1.
BX537836 mRNA. Translation: CAD97848.1.
AK094653 mRNA. Translation: BAC04396.1. Different initiation.
PIRT46328.
T51867.
RefSeqNP_057613.4. NM_016529.4.
XP_005266476.1. XM_005266419.1. [Q9NTI2-1]
XP_006719897.1. XM_006719834.1. [Q9NTI2-1]
UniGeneHs.444957.

3D structure databases

ProteinModelPortalQ9NTI2.
SMRQ9NTI2. Positions 95-847.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119718. 2 interactions.
STRING9606.ENSP00000371070.

Polymorphism databases

DMDM30316390.

Proteomic databases

PaxDbQ9NTI2.
PRIDEQ9NTI2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381655; ENSP00000371070; ENSG00000132932.
GeneID51761.
KEGGhsa:51761.
UCSCuc001uql.1. human. [Q9NTI2-3]

Organism-specific databases

CTD51761.
GeneCardsGC13P025946.
HGNCHGNC:13533. ATP8A2.
HPAHPA039926.
MIM605870. gene.
615268. phenotype.
neXtProtNX_Q9NTI2.
Orphanet1766. Dysequilibrium syndrome.
PharmGKBPA25166.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOVERGENHBG050601.
InParanoidQ9NTI2.
KOK14802.
PhylomeDBQ9NTI2.
TreeFamTF300654.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9NTI2.
BgeeQ9NTI2.
CleanExHS_ATP8A2.
GenevestigatorQ9NTI2.

Family and domain databases

Gene3D2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR006539. ATPase_P-typ_Plipid-transp.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PANTHERPTHR24092. PTHR24092. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP8A2. human.
GenomeRNAi51761.
NextBio55870.
PROQ9NTI2.
SOURCESearch...

Entry information

Entry nameAT8A2_HUMAN
AccessionPrimary (citable) accession number: Q9NTI2
Secondary accession number(s): Q9H527 expand/collapse secondary AC list , Q9NPU6, Q9NTL2, Q9NYM3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: April 30, 2003
Last modified: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM