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O43752

- STX6_HUMAN

UniProt

O43752 - STX6_HUMAN

Protein

Syntaxin-6

Gene

STX6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Involved in intracellular vesicle trafficking.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. SNAP receptor activity Source: RefGenome

    GO - Biological processi

    1. endosome organization Source: Ensembl
    2. Golgi vesicle transport Source: InterPro
    3. intracellular protein transport Source: RefGenome
    4. retrograde transport, endosome to Golgi Source: UniProtKB
    5. vesicle fusion Source: UniProtKB

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Syntaxin-6
    Gene namesi
    Name:STX6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11441. STX6.

    Subcellular locationi

    GO - Cellular componenti

    1. clathrin-coated vesicle Source: UniProtKB
    2. early endosome Source: UniProtKB
    3. Golgi apparatus Source: UniProtKB
    4. Golgi membrane Source: UniProtKB-SubCell
    5. integral component of membrane Source: RefGenome
    6. perinuclear region of cytoplasm Source: UniProtKB
    7. plasma membrane Source: UniProtKB
    8. SNARE complex Source: MGI
    9. trans-Golgi network membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36238.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 255254Syntaxin-6PRO_0000210208Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei152 – 1521Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO43752.
    PaxDbiO43752.
    PeptideAtlasiO43752.
    PRIDEiO43752.

    PTM databases

    PhosphoSiteiO43752.

    Expressioni

    Gene expression databases

    ArrayExpressiO43752.
    BgeeiO43752.
    CleanExiHS_STX6.
    GenevestigatoriO43752.

    Organism-specific databases

    HPAiHPA038557.
    HPA038558.

    Interactioni

    Subunit structurei

    Binds EEA1. Interacts with VPS45A. Interacts with MARCH2 and MARCH3 By similarity. Interacts with GOPC. Identified in a complex containing STX6, STX12, VAMP4 and VTI1A.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi115522. 13 interactions.
    DIPiDIP-44224N.
    IntActiO43752. 9 interactions.
    MINTiMINT-5002256.
    STRINGi9606.ENSP00000258301.

    Structurei

    Secondary structure

    1
    255
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 3327
    Turni35 – 373
    Helixi40 – 7334
    Helixi75 – 784
    Helixi82 – 10726
    Helixi173 – 22957

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NPSX-ray2.50D169-234[»]
    4J2CX-ray1.80A/C3-110[»]
    ProteinModelPortaliO43752.
    SMRiO43752. Positions 2-108, 170-232.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43752.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 234233CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei235 – 25521Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini163 – 22563t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili41 – 7434Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the syntaxin family.Curated
    Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG46901.
    HOGENOMiHOG000237350.
    HOVERGENiHBG007194.
    InParanoidiO43752.
    KOiK08498.
    OMAiQVVREMK.
    OrthoDBiEOG7JHM7F.
    PhylomeDBiO43752.
    TreeFamiTF313254.

    Family and domain databases

    InterProiIPR015260. Syntaxin-6_N.
    IPR006012. Syntaxin/epimorphin_CS.
    IPR010989. t-SNARE.
    IPR000727. T_SNARE_dom.
    [Graphical view]
    PfamiPF05739. SNARE. 1 hit.
    PF09177. Syntaxin-6_N. 1 hit.
    [Graphical view]
    SMARTiSM00397. t_SNARE. 1 hit.
    [Graphical view]
    SUPFAMiSSF47661. SSF47661. 1 hit.
    PROSITEiPS00914. SYNTAXIN. 1 hit.
    PS50192. T_SNARE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43752-1) [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

    MSMEDPFFVV KGEVQKAVNT AQGLFQRWTE LLQDPSTATR EEIDWTTNEL    50
    RNNLRSIEWD LEDLDETISI VEANPRKFNL DATELSIRKA FITSTRQVVR 100
    DMKDQMSTSS VQALAERKNR QALLGDSGSQ NWSTGTTDKY GRLDRELQRA 150
    NSHFIEEQQA QQQLIVEQQD EQLELVSGSI GVLKNMSQRI GGELEEQAVM 200
    LEDFSHELES TQSRLDNVMK KLAKVSHMTS DRRQWCAIAI LFAVLLVVLI 250
    LFLVL 255
    Length:255
    Mass (Da):29,176
    Last modified:June 1, 1998 - v1
    Checksum:iCC05C025DE1FE89E
    GO
    Isoform 2 (identifier: O43752-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: Missing.

    Show »
    Length:154
    Mass (Da):17,434
    Checksum:i63C26276F286C7E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771K → R in CAG46654. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 101101Missing in isoform 2. 1 PublicationVSP_054763Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002078 mRNA. Translation: CAA05177.1.
    CR541856 mRNA. Translation: CAG46654.1.
    CR541873 mRNA. Translation: CAG46671.1.
    AK299063 mRNA. Translation: BAG61129.1.
    AK312440 mRNA. Translation: BAG35349.1.
    AL356267, AL162431 Genomic DNA. Translation: CAH72301.1.
    AL162431, AL356267 Genomic DNA. Translation: CAH74088.1.
    CH471067 Genomic DNA. Translation: EAW91091.1.
    BC009944 mRNA. Translation: AAH09944.1.
    CCDSiCCDS1341.1. [O43752-1]
    CCDS65738.1. [O43752-2]
    RefSeqiNP_001273139.1. NM_001286210.1. [O43752-2]
    NP_005810.1. NM_005819.5. [O43752-1]
    XP_005244881.1. XM_005244824.1. [O43752-2]
    UniGeneiHs.518417.
    Hs.737037.

    Genome annotation databases

    EnsembliENST00000258301; ENSP00000258301; ENSG00000135823. [O43752-1]
    ENST00000542060; ENSP00000440188; ENSG00000135823. [O43752-2]
    GeneIDi10228.
    KEGGihsa:10228.
    UCSCiuc010pnr.2. human. [O43752-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002078 mRNA. Translation: CAA05177.1 .
    CR541856 mRNA. Translation: CAG46654.1 .
    CR541873 mRNA. Translation: CAG46671.1 .
    AK299063 mRNA. Translation: BAG61129.1 .
    AK312440 mRNA. Translation: BAG35349.1 .
    AL356267 , AL162431 Genomic DNA. Translation: CAH72301.1 .
    AL162431 , AL356267 Genomic DNA. Translation: CAH74088.1 .
    CH471067 Genomic DNA. Translation: EAW91091.1 .
    BC009944 mRNA. Translation: AAH09944.1 .
    CCDSi CCDS1341.1. [O43752-1 ]
    CCDS65738.1. [O43752-2 ]
    RefSeqi NP_001273139.1. NM_001286210.1. [O43752-2 ]
    NP_005810.1. NM_005819.5. [O43752-1 ]
    XP_005244881.1. XM_005244824.1. [O43752-2 ]
    UniGenei Hs.518417.
    Hs.737037.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NPS X-ray 2.50 D 169-234 [» ]
    4J2C X-ray 1.80 A/C 3-110 [» ]
    ProteinModelPortali O43752.
    SMRi O43752. Positions 2-108, 170-232.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115522. 13 interactions.
    DIPi DIP-44224N.
    IntActi O43752. 9 interactions.
    MINTi MINT-5002256.
    STRINGi 9606.ENSP00000258301.

    PTM databases

    PhosphoSitei O43752.

    Proteomic databases

    MaxQBi O43752.
    PaxDbi O43752.
    PeptideAtlasi O43752.
    PRIDEi O43752.

    Protocols and materials databases

    DNASUi 10228.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258301 ; ENSP00000258301 ; ENSG00000135823 . [O43752-1 ]
    ENST00000542060 ; ENSP00000440188 ; ENSG00000135823 . [O43752-2 ]
    GeneIDi 10228.
    KEGGi hsa:10228.
    UCSCi uc010pnr.2. human. [O43752-1 ]

    Organism-specific databases

    CTDi 10228.
    GeneCardsi GC01M180941.
    HGNCi HGNC:11441. STX6.
    HPAi HPA038557.
    HPA038558.
    MIMi 603944. gene.
    neXtProti NX_O43752.
    PharmGKBi PA36238.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46901.
    HOGENOMi HOG000237350.
    HOVERGENi HBG007194.
    InParanoidi O43752.
    KOi K08498.
    OMAi QVVREMK.
    OrthoDBi EOG7JHM7F.
    PhylomeDBi O43752.
    TreeFami TF313254.

    Miscellaneous databases

    ChiTaRSi STX6. human.
    EvolutionaryTracei O43752.
    GeneWikii STX6.
    GenomeRNAii 10228.
    NextBioi 35474275.
    PROi O43752.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43752.
    Bgeei O43752.
    CleanExi HS_STX6.
    Genevestigatori O43752.

    Family and domain databases

    InterProi IPR015260. Syntaxin-6_N.
    IPR006012. Syntaxin/epimorphin_CS.
    IPR010989. t-SNARE.
    IPR000727. T_SNARE_dom.
    [Graphical view ]
    Pfami PF05739. SNARE. 1 hit.
    PF09177. Syntaxin-6_N. 1 hit.
    [Graphical view ]
    SMARTi SM00397. t_SNARE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47661. SSF47661. 1 hit.
    PROSITEi PS00914. SYNTAXIN. 1 hit.
    PS50192. T_SNARE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Co-expression of several human syntaxin genes in neutrophils and differentiating HL-60 cells: variant isoforms and detection of syntaxin 1."
      Martin-Martin B., Nabokina S.M., Lazo P.A., Mollinedo F.
      J. Leukoc. Biol. 65:397-406(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Muscle.
    7. "Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6."
      Charest A., Lane K., McMahon K., Housman D.E.
      J. Biol. Chem. 276:29456-29465(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH GOPC.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies."
      Zwilling D., Cypionka A., Pohl W.H., Fasshauer D., Walla P.J., Wahl M.C., Jahn R.
      EMBO J. 26:9-18(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 47-117 IN COMPLEX WITH STX12; VTI1A AND VAMP4, SUBUNIT.

    Entry informationi

    Entry nameiSTX6_HUMAN
    AccessioniPrimary (citable) accession number: O43752
    Secondary accession number(s): B2R652
    , B4DR17, Q5VY08, Q6FH83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 127 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3