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P31153

- METK2_HUMAN

UniProt

P31153 - METK2_HUMAN

Protein

S-adenosylmethionine synthase isoform type-2

Gene

MAT2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of S-adenosylmethionine from methionine and ATP.

    Catalytic activityi

    ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.

    Cofactori

    Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity.By similarity
    Binds 1 potassium ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi31 – 311MagnesiumBy similarity
    Metal bindingi57 – 571PotassiumBy similarity
    Binding sitei159 – 1591ATPSequence Analysis
    Metal bindingi283 – 2831PotassiumBy similarity
    Metal bindingi291 – 2911MagnesiumBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi131 – 1366ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. methionine adenosyltransferase activity Source: UniProt
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. methylation Source: Reactome
    3. one-carbon metabolic process Source: UniProtKB-KW
    4. S-adenosylmethionine biosynthetic process Source: UniProt
    5. small molecule metabolic process Source: Reactome
    6. sulfur amino acid metabolic process Source: Reactome
    7. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

    Enzyme and pathway databases

    ReactomeiREACT_115639. Sulfur amino acid metabolism.
    REACT_6946. Methylation.
    UniPathwayiUPA00315; UER00080.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosylmethionine synthase isoform type-2 (EC:2.5.1.6)
    Short name:
    AdoMet synthase 2
    Alternative name(s):
    Methionine adenosyltransferase 2
    Short name:
    MAT 2
    Methionine adenosyltransferase II
    Short name:
    MAT-II
    Gene namesi
    Name:MAT2A
    Synonyms:AMS2, MATA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6904. MAT2A.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. methionine adenosyltransferase complex Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30647.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 395395S-adenosylmethionine synthase isoform type-2PRO_0000174435Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei81 – 811N6-acetyllysine1 Publication
    Modified residuei114 – 1141Phosphoserine1 Publication

    Post-translational modificationi

    The alpha' subunit is a post-translationally modified version of MAT2A.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP31153.
    PaxDbiP31153.
    PeptideAtlasiP31153.
    PRIDEiP31153.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00010157.

    PTM databases

    PhosphoSiteiP31153.

    Expressioni

    Gene expression databases

    ArrayExpressiP31153.
    BgeeiP31153.
    CleanExiHS_MAT2A.
    GenevestigatoriP31153.

    Organism-specific databases

    HPAiCAB009968.
    HPA043028.

    Interactioni

    Subunit structurei

    Heterotetramer composed of 2 catalytic alpha subunits (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B).1 Publication

    Protein-protein interaction databases

    BioGridi110314. 22 interactions.
    IntActiP31153. 17 interactions.
    STRINGi9606.ENSP00000303147.

    Structurei

    Secondary structure

    1
    395
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 259
    Helixi30 – 4819
    Beta strandi53 – 619
    Beta strandi64 – 729
    Helixi79 – 9012
    Helixi95 – 973
    Turni101 – 1033
    Beta strandi104 – 1118
    Helixi115 – 1217
    Turni122 – 1243
    Helixi127 – 1293
    Beta strandi132 – 1343
    Beta strandi136 – 1438
    Helixi152 – 16918
    Beta strandi176 – 19116
    Beta strandi194 – 20916
    Helixi215 – 22410
    Helixi227 – 2304
    Helixi233 – 2353
    Beta strandi241 – 2455
    Helixi254 – 2563
    Turni266 – 2738
    Helixi290 – 30718
    Beta strandi312 – 3209
    Beta strandi328 – 3336
    Helixi342 – 35211
    Helixi357 – 3648
    Turni365 – 3673
    Helixi371 – 3744
    Beta strandi375 – 3773
    Beta strandi379 – 3824
    Helixi386 – 3883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P02X-ray1.21A1-395[»]
    ProteinModelPortaliP31153.
    SMRiP31153. Positions 16-395.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31153.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AdoMet synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0192.
    HOGENOMiHOG000245710.
    HOVERGENiHBG001562.
    InParanoidiP31153.
    KOiK00789.
    OMAiDETEESM.
    PhylomeDBiP31153.
    TreeFamiTF300511.

    Family and domain databases

    HAMAPiMF_00086. S_AdoMet_synth1.
    InterProiIPR022631. ADOMET_SYNTHASE_CS.
    IPR022630. S-AdoMet_synt_C.
    IPR022629. S-AdoMet_synt_central.
    IPR022628. S-AdoMet_synt_N.
    IPR002133. S-AdoMet_synthetase.
    IPR022636. S-AdoMet_synthetase_sfam.
    [Graphical view]
    PANTHERiPTHR11964. PTHR11964. 1 hit.
    PfamiPF02773. S-AdoMet_synt_C. 1 hit.
    PF02772. S-AdoMet_synt_M. 1 hit.
    PF00438. S-AdoMet_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000497. MAT. 1 hit.
    SUPFAMiSSF55973. SSF55973. 3 hits.
    TIGRFAMsiTIGR01034. metK. 1 hit.
    PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
    PS00377. ADOMET_SYNTHASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P31153-1) [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

    MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP    50
    DAKVACETVA KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD 100
    YKTCNVLVAL EQQSPDIAQG VHLDRNEEDI GAGDQGLMFG YATDETEECM 150
    PLTIVLAHKL NAKLAELRRN GTLPWLRPDS KTQVTVQYMQ DRGAVLPIRV 200
    HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT IYHLQPSGRF 250
    VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW 300
    VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK 350
    KNFDLRPGVI VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY 395
    Length:395
    Mass (Da):43,661
    Last modified:July 1, 1993 - v1
    Checksum:i2E7D1B91CC4F7BDD
    GO
    Isoform 2 (identifier: P31153-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-63: Missing.
         363-395: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:299
    Mass (Da):32,965
    Checksum:i3E3903C0EFD85F00
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6363Missing in isoform 2. 1 PublicationVSP_056186Add
    BLAST
    Alternative sequencei363 – 39533Missing in isoform 2. 1 PublicationVSP_056187Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68836 mRNA. Translation: CAA48726.1.
    DQ083239 mRNA. Translation: AAY85355.1.
    AK291126 mRNA. Translation: BAF83815.1.
    AK297758 mRNA. Translation: BAG60107.1.
    AK316411 mRNA. Translation: BAH14782.1.
    AC016753 Genomic DNA. Translation: AAY24339.1.
    CH471053 Genomic DNA. Translation: EAW99511.1.
    CH471053 Genomic DNA. Translation: EAW99513.1.
    BC001686 mRNA. Translation: AAH01686.1.
    BC001854 mRNA. Translation: AAH01854.1.
    CCDSiCCDS1977.1.
    PIRiS27257.
    RefSeqiNP_005902.1. NM_005911.5.
    UniGeneiHs.516157.

    Genome annotation databases

    EnsembliENST00000306434; ENSP00000303147; ENSG00000168906.
    ENST00000409017; ENSP00000386353; ENSG00000168906.
    GeneIDi4144.
    KEGGihsa:4144.
    UCSCiuc002spr.3. human.

    Polymorphism databases

    DMDMi400245.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68836 mRNA. Translation: CAA48726.1 .
    DQ083239 mRNA. Translation: AAY85355.1 .
    AK291126 mRNA. Translation: BAF83815.1 .
    AK297758 mRNA. Translation: BAG60107.1 .
    AK316411 mRNA. Translation: BAH14782.1 .
    AC016753 Genomic DNA. Translation: AAY24339.1 .
    CH471053 Genomic DNA. Translation: EAW99511.1 .
    CH471053 Genomic DNA. Translation: EAW99513.1 .
    BC001686 mRNA. Translation: AAH01686.1 .
    BC001854 mRNA. Translation: AAH01854.1 .
    CCDSi CCDS1977.1.
    PIRi S27257.
    RefSeqi NP_005902.1. NM_005911.5.
    UniGenei Hs.516157.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2P02 X-ray 1.21 A 1-395 [» ]
    ProteinModelPortali P31153.
    SMRi P31153. Positions 16-395.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110314. 22 interactions.
    IntActi P31153. 17 interactions.
    STRINGi 9606.ENSP00000303147.

    Chemistry

    DrugBanki DB00134. L-Methionine.
    DB00118. S-Adenosylmethionine.

    PTM databases

    PhosphoSitei P31153.

    Polymorphism databases

    DMDMi 400245.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00010157.

    Proteomic databases

    MaxQBi P31153.
    PaxDbi P31153.
    PeptideAtlasi P31153.
    PRIDEi P31153.

    Protocols and materials databases

    DNASUi 4144.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306434 ; ENSP00000303147 ; ENSG00000168906 .
    ENST00000409017 ; ENSP00000386353 ; ENSG00000168906 .
    GeneIDi 4144.
    KEGGi hsa:4144.
    UCSCi uc002spr.3. human.

    Organism-specific databases

    CTDi 4144.
    GeneCardsi GC02P085766.
    H-InvDB HIX0117562.
    HGNCi HGNC:6904. MAT2A.
    HPAi CAB009968.
    HPA043028.
    MIMi 601468. gene.
    neXtProti NX_P31153.
    PharmGKBi PA30647.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0192.
    HOGENOMi HOG000245710.
    HOVERGENi HBG001562.
    InParanoidi P31153.
    KOi K00789.
    OMAi DETEESM.
    PhylomeDBi P31153.
    TreeFami TF300511.

    Enzyme and pathway databases

    UniPathwayi UPA00315 ; UER00080 .
    Reactomei REACT_115639. Sulfur amino acid metabolism.
    REACT_6946. Methylation.

    Miscellaneous databases

    ChiTaRSi MAT2A. human.
    EvolutionaryTracei P31153.
    GenomeRNAii 4144.
    NextBioi 16276.
    PROi P31153.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31153.
    Bgeei P31153.
    CleanExi HS_MAT2A.
    Genevestigatori P31153.

    Family and domain databases

    HAMAPi MF_00086. S_AdoMet_synth1.
    InterProi IPR022631. ADOMET_SYNTHASE_CS.
    IPR022630. S-AdoMet_synt_C.
    IPR022629. S-AdoMet_synt_central.
    IPR022628. S-AdoMet_synt_N.
    IPR002133. S-AdoMet_synthetase.
    IPR022636. S-AdoMet_synthetase_sfam.
    [Graphical view ]
    PANTHERi PTHR11964. PTHR11964. 1 hit.
    Pfami PF02773. S-AdoMet_synt_C. 1 hit.
    PF02772. S-AdoMet_synt_M. 1 hit.
    PF00438. S-AdoMet_synt_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000497. MAT. 1 hit.
    SUPFAMi SSF55973. SSF55973. 3 hits.
    TIGRFAMsi TIGR01034. metK. 1 hit.
    PROSITEi PS00376. ADOMET_SYNTHASE_1. 1 hit.
    PS00377. ADOMET_SYNTHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and developmental expression of a human kidney S-adenosylmethionine synthetase."
      Horikawa S., Tsukada K.
      FEBS Lett. 312:37-41(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    2. "Activation of a novel isoform of methionine adenosyl transferase 2A and increased S-adenosylmethionine turnover in lung epithelial cells exposed to hyperoxia."
      Panayiotidis M.I., Stabler S.P., Ahmad A., Pappa A., Legros L.H. Jr., Hernandez-Saavedra D., Schneider B.K., Allen R.H., Vasiliou V., McCord J.M., Kotb M., White C.W.
      Free Radic. Biol. Med. 40:348-358(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung.
    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: Testis.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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. "Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II)."
      LeGros H.L., Halim A.-B., Geller A.M., Kotb M.
      J. Biol. Chem. 275:2359-2366(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMETK2_HUMAN
    AccessioniPrimary (citable) accession number: P31153
    Secondary accession number(s): A8K511
    , B4DN45, D6W5L1, Q53SP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 151 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 2
      Human chromosome 2: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3