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Protein

Sodium-coupled neutral amino acid transporter 1

Gene

SLC38A1

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

Functioni

Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of glutamine and sodium ions with a stoichiometry of 1:1. May also transport small zwitterionic and aliphatic amino acids with a lower affinity. May supply glutamatergic and GABAergic neurons with glutamine which is required for the synthesis of the neurotransmitters glutamate and GABA.1 Publication

Enzyme regulationi

Inhibited by potassium, choline ions and 2-methylamino-isobutyric acid (MeAIB) (By similarity). Inhibited by lithium and N-methyl-D-glucamine.By similarity1 Publication

Kineticsi

  1. KM=890 µM for 2-methylamino-isobutyric acid (MeAIB) (at pH 8.5)1 Publication

    GO - Molecular functioni

    • amino acid transmembrane transporter activity Source: GO_Central
    • neutral amino acid transmembrane transporter activity Source: UniProtKB
    • sodium:amino acid symporter activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Biological processi

    Amino-acid transport, Ion transport, Sodium transport, Symport, Transport

    Keywords - Ligandi

    Sodium

    Enzyme and pathway databases

    ReactomeiREACT_13639. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
    REACT_13796. Amino acid transport across the plasma membrane.

    Protein family/group databases

    TCDBi2.A.18.6.14. the amino acid/auxin permease (aaap) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sodium-coupled neutral amino acid transporter 1
    Alternative name(s):
    Amino acid transporter A1
    N-system amino acid transporter 2
    Solute carrier family 38 member 1
    System A amino acid transporter 1
    System N amino acid transporter 1
    Gene namesi
    Name:SLC38A1
    Synonyms:ATA1, NAT2, SAT1, SNAT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:13447. SLC38A1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 7474CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei75 – 9723HelicalSequence AnalysisAdd
    BLAST
    Topological domaini98 – 11215ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei113 – 13321HelicalSequence AnalysisAdd
    BLAST
    Topological domaini134 – 14714CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei148 – 16821HelicalSequence AnalysisAdd
    BLAST
    Topological domaini169 – 18820ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei189 – 21123HelicalSequence AnalysisAdd
    BLAST
    Topological domaini212 – 2165CytoplasmicSequence Analysis
    Transmembranei217 – 23721HelicalSequence AnalysisAdd
    BLAST
    Topological domaini238 – 27538ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei276 – 29621HelicalSequence AnalysisAdd
    BLAST
    Topological domaini297 – 31216CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei313 – 33321HelicalSequence AnalysisAdd
    BLAST
    Topological domaini334 – 35017ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei351 – 37121HelicalSequence AnalysisAdd
    BLAST
    Topological domaini372 – 39322CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei394 – 41421HelicalSequence AnalysisAdd
    BLAST
    Topological domaini415 – 4162ExtracellularSequence Analysis
    Transmembranei417 – 43721HelicalSequence AnalysisAdd
    BLAST
    Topological domaini438 – 45215CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei453 – 47321HelicalSequence AnalysisAdd
    BLAST
    Topological domaini474 – 48714ExtracellularSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • extracellular exosome Source: UniProtKB
    • integral component of membrane Source: UniProtKB
    • integral component of plasma membrane Source: GO_Central
    • plasma membrane Source: Reactome
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37772.

    Polymorphism and mutation databases

    BioMutaiSLC38A1.
    DMDMi74733561.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 487487Sodium-coupled neutral amino acid transporter 1PRO_0000310475Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Phosphoserine1 Publication
    Modified residuei28 – 281Phosphoserine1 Publication
    Modified residuei52 – 521Phosphoserine3 Publications
    Modified residuei54 – 541Phosphothreonine3 Publications
    Modified residuei56 – 561Phosphoserine2 Publications
    Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H2H9.
    PaxDbiQ9H2H9.
    PRIDEiQ9H2H9.

    PTM databases

    PhosphoSiteiQ9H2H9.

    Expressioni

    Tissue specificityi

    Expressed in the cerebral cortex by pyramidal and GABAergic neurons, astrocytes and other non-neuronal cells (at protein level). Expressed in placenta, heart, lung, skeletal muscle, spleen, stomach and testis.4 Publications

    Inductioni

    Down-regulated by bacterial lipopolysaccharides (LPS) in glial cells. Down-regulated upon hypoxia.2 Publications

    Gene expression databases

    BgeeiQ9H2H9.
    CleanExiHS_NAT2.
    HS_SAT1.
    HS_SLC38A1.
    ExpressionAtlasiQ9H2H9. baseline and differential.
    GenevisibleiQ9H2H9. HS.

    Organism-specific databases

    HPAiHPA052272.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FATE1Q969F03EBI-9978441,EBI-743099

    Protein-protein interaction databases

    BioGridi123509. 2 interactions.
    IntActiQ9H2H9. 53 interactions.
    STRINGi9606.ENSP00000381634.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H2H9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0814.
    GeneTreeiENSGT00760000119147.
    HOGENOMiHOG000013088.
    HOVERGENiHBG059571.
    InParanoidiQ9H2H9.
    KOiK14990.
    PhylomeDBiQ9H2H9.
    TreeFamiTF328787.

    Family and domain databases

    InterProiIPR013057. AA_transpt_TM.
    [Graphical view]
    PfamiPF01490. Aa_trans. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9H2H9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMHFKSGLEL TELQNMTVPE DDNISNDSND FTEVENGQIN SKFISDRESR
    60 70 80 90 100
    RSLTNSHLEK KKCDEYIPGT TSLGMSVFNL SNAIMGSGIL GLAFALANTG
    110 120 130 140 150
    ILLFLVLLTS VTLLSIYSIN LLLICSKETG CMVYEKLGEQ VFGTTGKFVI
    160 170 180 190 200
    FGATSLQNTG AMLSYLFIVK NELPSAIKFL MGKEETFSAW YVDGRVLVVI
    210 220 230 240 250
    VTFGIILPLC LLKNLGYLGY TSGFSLSCMV FFLIVVIYKK FQIPCIVPEL
    260 270 280 290 300
    NSTISANSTN ADTCTPKYVT FNSKTVYALP TIAFAFVCHP SVLPIYSELK
    310 320 330 340 350
    DRSQKKMQMV SNISFFAMFV MYFLTAIFGY LTFYDNVQSD LLHKYQSKDD
    360 370 380 390 400
    ILILTVRLAV IVAVILTVPV LFFTVRSSLF ELAKKTKFNL CRHTVVTCIL
    410 420 430 440 450
    LVVINLLVIF IPSMKDIFGV VGVTSANMLI FILPSSLYLK ITDQDGDKGT
    460 470 480
    QRIWAALFLG LGVLFSLVSI PLVIYDWACS SSSDEGH
    Length:487
    Mass (Da):54,048
    Last modified:March 1, 2001 - v1
    Checksum:i5CBC96880D7BDE03
    GO

    Sequence cautioni

    The sequence AAG44546.1 differs from that shown. Reason: Frameshift at position 443. Curated
    The sequence BAC11186.1 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071L → P in BAB55394 (PubMed:14702039).Curated
    Sequence conflicti203 – 2031F → V in BAC11310 (PubMed:16303743).Curated
    Sequence conflicti375 – 3751V → D in AAG44546 (Ref. 2) Curated
    Sequence conflicti483 – 4842SD → NG in AAG44546 (Ref. 2) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF271070 mRNA. Translation: AAG39354.1.
    AF247166 mRNA. Translation: AAG44546.1. Frameshift.
    AK027825 mRNA. Translation: BAB55394.1.
    AK074758 mRNA. Translation: BAC11186.1. Different initiation.
    AK074949 mRNA. Translation: BAC11310.1.
    CH471111 Genomic DNA. Translation: EAW57895.1.
    BC010620 mRNA. Translation: AAH10620.1.
    CCDSiCCDS41774.1.
    PIRiJC7328.
    RefSeqiNP_001070952.1. NM_001077484.1.
    NP_001265316.1. NM_001278387.1.
    NP_001265317.1. NM_001278388.1.
    NP_001265318.1. NM_001278389.1.
    NP_109599.3. NM_030674.3.
    UniGeneiHs.533770.

    Genome annotation databases

    EnsembliENST00000398637; ENSP00000381634; ENSG00000111371.
    ENST00000439706; ENSP00000398142; ENSG00000111371.
    ENST00000546893; ENSP00000447853; ENSG00000111371.
    ENST00000549049; ENSP00000449607; ENSG00000111371.
    GeneIDi81539.
    KEGGihsa:81539.
    UCSCiuc001rpa.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF271070 mRNA. Translation: AAG39354.1.
    AF247166 mRNA. Translation: AAG44546.1. Frameshift.
    AK027825 mRNA. Translation: BAB55394.1.
    AK074758 mRNA. Translation: BAC11186.1. Different initiation.
    AK074949 mRNA. Translation: BAC11310.1.
    CH471111 Genomic DNA. Translation: EAW57895.1.
    BC010620 mRNA. Translation: AAH10620.1.
    CCDSiCCDS41774.1.
    PIRiJC7328.
    RefSeqiNP_001070952.1. NM_001077484.1.
    NP_001265316.1. NM_001278387.1.
    NP_001265317.1. NM_001278388.1.
    NP_001265318.1. NM_001278389.1.
    NP_109599.3. NM_030674.3.
    UniGeneiHs.533770.

    3D structure databases

    ProteinModelPortaliQ9H2H9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi123509. 2 interactions.
    IntActiQ9H2H9. 53 interactions.
    STRINGi9606.ENSP00000381634.

    Chemistry

    GuidetoPHARMACOLOGYi1169.

    Protein family/group databases

    TCDBi2.A.18.6.14. the amino acid/auxin permease (aaap) family.

    PTM databases

    PhosphoSiteiQ9H2H9.

    Polymorphism and mutation databases

    BioMutaiSLC38A1.
    DMDMi74733561.

    Proteomic databases

    MaxQBiQ9H2H9.
    PaxDbiQ9H2H9.
    PRIDEiQ9H2H9.

    Protocols and materials databases

    DNASUi81539.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000398637; ENSP00000381634; ENSG00000111371.
    ENST00000439706; ENSP00000398142; ENSG00000111371.
    ENST00000546893; ENSP00000447853; ENSG00000111371.
    ENST00000549049; ENSP00000449607; ENSG00000111371.
    GeneIDi81539.
    KEGGihsa:81539.
    UCSCiuc001rpa.3. human.

    Organism-specific databases

    CTDi81539.
    GeneCardsiGC12M046576.
    HGNCiHGNC:13447. SLC38A1.
    HPAiHPA052272.
    MIMi608490. gene.
    neXtProtiNX_Q9H2H9.
    PharmGKBiPA37772.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0814.
    GeneTreeiENSGT00760000119147.
    HOGENOMiHOG000013088.
    HOVERGENiHBG059571.
    InParanoidiQ9H2H9.
    KOiK14990.
    PhylomeDBiQ9H2H9.
    TreeFamiTF328787.

    Enzyme and pathway databases

    ReactomeiREACT_13639. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
    REACT_13796. Amino acid transport across the plasma membrane.

    Miscellaneous databases

    ChiTaRSiSLC38A1. human.
    GeneWikiiSLC38A1.
    GenomeRNAii81539.
    NextBioi71767.
    PROiQ9H2H9.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9H2H9.
    CleanExiHS_NAT2.
    HS_SAT1.
    HS_SLC38A1.
    ExpressionAtlasiQ9H2H9. baseline and differential.
    GenevisibleiQ9H2H9. HS.

    Family and domain databases

    InterProiIPR013057. AA_transpt_TM.
    [Graphical view]
    PfamiPF01490. Aa_trans. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and functional expression of ATA1, a subtype of amino acid transporter A, from human placenta."
      Wang H., Huang W., Sugawara M., Devoe L.D., Leibach F.H., Prasad P.D., Ganapathy V.
      Biochem. Biophys. Res. Commun. 273:1175-1179(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Hypothalamus.
    3. "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.
      , 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].
      Tissue: Placenta and Teratocarcinoma.
    4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Teratocarcinoma.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye.
    7. "Hypoxia reduces expression and function of system A amino acid transporters in cultured term human trophoblasts."
      Nelson D.M., Smith S.D., Furesz T.C., Sadovsky Y., Ganapathy V., Parvin C.A., Smith C.H.
      Am. J. Physiol. 284:C310-C315(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    8. "Localization of the glutamine transporter SNAT1 in rat cerebral cortex and neighboring structures, with a note on its localization in human cortex."
      Melone M., Quagliano F., Barbaresi P., Varoqui H., Erickson J.D., Conti F.
      Cereb. Cortex 14:562-574(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. "SNAT4 isoform of system A amino acid transporter is expressed in human placenta."
      Desforges M., Lacey H.A., Glazier J.D., Greenwood S.L., Mynett K.J., Speake P.F., Sibley C.P.
      Am. J. Physiol. 290:C305-C312(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Functional expression of a glutamine transporter responsive to down-regulation by lipopolysaccharide through reduced promoter activity in cultured rat neocortical astrocytes."
      Ogura M., Nakamichi N., Takano K., Oikawa H., Kambe Y., Ohno Y., Taniura H., Yoneda Y.
      J. Neurosci. Res. 83:1447-1460(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY LPS.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-28; SER-52; THR-54 AND SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; THR-54 AND SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND THR-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiS38A1_HUMAN
    AccessioniPrimary (citable) accession number: Q9H2H9
    Secondary accession number(s): Q8NC61
    , Q8NCF8, Q96JX2, Q9H2Q2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: March 1, 2001
    Last modified: June 24, 2015
    This is version 107 of the entry and version 1 of the sequence. [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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.