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O14556

- G3PT_HUMAN

UniProt

O14556 - G3PT_HUMAN

Protein

Glyceraldehyde-3-phosphate dehydrogenase, testis-specific

Gene

GAPDHS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility By similarity.By similarity

    Catalytic activityi

    D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei106 – 1061NAD1 Publication
    Binding sitei151 – 1511NAD; via carbonyl oxygen1 Publication
    Binding sitei173 – 1731NAD1 Publication
    Binding sitei193 – 1931NAD1 Publication
    Active sitei224 – 2241Nucleophile1 PublicationPROSITE-ProRule annotation
    Sitei251 – 2511Activates thiol group during catalysis
    Binding sitei254 – 2541Glyceraldehyde 3-phosphateBy similarity
    Binding sitei306 – 3061Glyceraldehyde 3-phosphateBy similarity
    Binding sitei388 – 3881NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi85 – 862NAD1 Publication

    GO - Molecular functioni

    1. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
    2. NAD binding Source: InterPro
    3. NADP binding Source: InterPro
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. gluconeogenesis Source: Reactome
    3. glucose metabolic process Source: Reactome
    4. glycolytic process Source: Reactome
    5. positive regulation of glycolytic process Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. spermatid development Source: Ensembl
    8. sperm motility Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02793-MONOMER.
    ReactomeiREACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    UniPathwayiUPA00109; UER00184.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (EC:1.2.1.12)
    Alternative name(s):
    Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2
    Short name:
    GAPDH-2
    Spermatogenic glyceraldehyde-3-phosphate dehydrogenase
    Gene namesi
    Name:GAPDHS
    Synonyms:GAPD2, GAPDH2, GAPDS
    ORF Names:HSD-35, HSD35
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:24864. GAPDHS.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. motile cilium Source: Ensembl
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134934259.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 408408Glyceraldehyde-3-phosphate dehydrogenase, testis-specificPRO_0000145502Add
    BLAST

    Proteomic databases

    MaxQBiO14556.
    PaxDbiO14556.
    PeptideAtlasiO14556.
    PRIDEiO14556.

    PTM databases

    PhosphoSiteiO14556.

    Expressioni

    Tissue specificityi

    Testis specific.

    Gene expression databases

    ArrayExpressiO14556.
    BgeeiO14556.
    CleanExiHS_GAPDHS.
    GenevestigatoriO14556.

    Organism-specific databases

    HPAiHPA042666.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation.3 Publications

    Protein-protein interaction databases

    BioGridi117681. 3 interactions.
    IntActiO14556. 2 interactions.
    MINTiMINT-1515577.
    STRINGi9606.ENSP00000222286.

    Structurei

    Secondary structure

    1
    408
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi77 – 815
    Helixi85 – 9612
    Beta strandi100 – 1056
    Helixi111 – 1199
    Turni122 – 1243
    Beta strandi131 – 1344
    Beta strandi137 – 1404
    Beta strandi143 – 1486
    Helixi153 – 1553
    Helixi158 – 1614
    Beta strandi165 – 1684
    Beta strandi170 – 1723
    Helixi176 – 1849
    Beta strandi188 – 1947
    Beta strandi197 – 1993
    Turni204 – 2063
    Helixi208 – 2103
    Turni213 – 2153
    Beta strandi217 – 2204
    Helixi224 – 24017
    Beta strandi242 – 25211
    Beta strandi257 – 2615
    Helixi268 – 2714
    Turni274 – 2763
    Beta strandi279 – 2813
    Helixi285 – 2928
    Helixi294 – 2963
    Turni297 – 2993
    Beta strandi300 – 3089
    Beta strandi313 – 32311
    Helixi327 – 33913
    Turni340 – 3456
    Beta strandi346 – 3494
    Helixi355 – 3584
    Beta strandi364 – 3685
    Turni369 – 3713
    Beta strandi373 – 3764
    Beta strandi379 – 3868
    Helixi390 – 40718

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H9EX-ray1.72O/P69-407[»]
    3PFWX-ray2.15O/P69-407[»]
    ProteinModelPortaliO14556.
    SMRiO14556. Positions 74-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14556.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 7373Testis-specific N-terminal extensionAdd
    BLAST
    Regioni223 – 2253Glyceraldehyde 3-phosphate bindingBy similarity
    Regioni283 – 2842Glyceraldehyde 3-phosphate bindingBy similarity

    Domaini

    The testis-specific N-terminal extension mediates tight association with the cytoskeletal fibrous sheath of the spermatozoa flagellum, possibly via interchain disulfide-bonding of Cys-21 with sheath components.1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0057.
    HOGENOMiHOG000071678.
    HOVERGENiHBG000227.
    InParanoidiO14556.
    KOiK10705.
    OMAiNDKWGIE.
    OrthoDBiEOG7Q5HDF.
    PhylomeDBiO14556.
    TreeFamiTF300533.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR020831. GlycerAld/Erythrose_P_DH.
    IPR020830. GlycerAld_3-P_DH_AS.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006424. Glyceraldehyde-3-P_DH_1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR10836. PTHR10836. 1 hit.
    PfamiPF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000149. GAP_DH. 1 hit.
    PRINTSiPR00078. G3PDHDRGNASE.
    SMARTiSM00846. Gp_dh_N. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
    PROSITEiPS00071. GAPDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O14556-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKRDIVLTN VTVVQLLRQP CPVTRAPPPP EPKAEVEPQP QPEPTPVREE    50
    IKPPPPPLPP HPATPPPKMV SVARELTVGI NGFGRIGRLV LRACMEKGVK 100
    VVAVNDPFID PEYMVYMFKY DSTHGRYKGS VEFRNGQLVV DNHEISVYQC 150
    KEPKQIPWRA VGSPYVVEST GVYLSIQAAS DHISAGAQRV VISAPSPDAP 200
    MFVMGVNEND YNPGSMNIVS NASCTTNCLA PLAKVIHERF GIVEGLMTTV 250
    HSYTATQKTV DGPSRKAWRD GRGAHQNIIP ASTGAAKAVT KVIPELKGKL 300
    TGMAFRVPTP DVSVVDLTCR LAQPAPYSAI KEAVKAAAKG PMAGILAYTE 350
    DEVVSTDFLG DTHSSIFDAK AGIALNDNFV KLISWYDNEY GYSHRVVDLL 400
    RYMFSRDK 408
    Length:408
    Mass (Da):44,501
    Last modified:May 30, 2000 - v2
    Checksum:i301F71C768CD95D8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti220 – 2201S → SVRAHLGCFS in AAB64181. (PubMed:15057824)Curated
    Sequence conflicti273 – 2731G → V in AAQ75383. 1 PublicationCurated
    Sequence conflicti343 – 3431A → R in AAF87970. (PubMed:10714828)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti110 – 1101D → N.
    Corresponds to variant rs2285514 [ dbSNP | Ensembl ].
    VAR_049219

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005371 mRNA. Translation: CAA06501.1.
    AF216641
    , AF216631, AF216632, AF216633, AF216634, AF216635, AF216636, AF216637, AF216638, AF216639, AF216640 Genomic DNA. Translation: AAF87970.1.
    AY306129 mRNA. Translation: AAQ75383.1.
    AK314980 mRNA. Translation: BAG37479.1.
    AC002389 Genomic DNA. Translation: AAB64181.1.
    BC036373 mRNA. Translation: AAH36373.1.
    CCDSiCCDS12465.1.
    RefSeqiNP_055179.1. NM_014364.4.
    UniGeneiHs.248017.

    Genome annotation databases

    EnsembliENST00000222286; ENSP00000222286; ENSG00000105679.
    GeneIDi26330.
    KEGGihsa:26330.
    UCSCiuc002oaf.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005371 mRNA. Translation: CAA06501.1 .
    AF216641
    , AF216631 , AF216632 , AF216633 , AF216634 , AF216635 , AF216636 , AF216637 , AF216638 , AF216639 , AF216640 Genomic DNA. Translation: AAF87970.1 .
    AY306129 mRNA. Translation: AAQ75383.1 .
    AK314980 mRNA. Translation: BAG37479.1 .
    AC002389 Genomic DNA. Translation: AAB64181.1 .
    BC036373 mRNA. Translation: AAH36373.1 .
    CCDSi CCDS12465.1.
    RefSeqi NP_055179.1. NM_014364.4.
    UniGenei Hs.248017.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3H9E X-ray 1.72 O/P 69-407 [» ]
    3PFW X-ray 2.15 O/P 69-407 [» ]
    ProteinModelPortali O14556.
    SMRi O14556. Positions 74-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117681. 3 interactions.
    IntActi O14556. 2 interactions.
    MINTi MINT-1515577.
    STRINGi 9606.ENSP00000222286.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei O14556.

    Proteomic databases

    MaxQBi O14556.
    PaxDbi O14556.
    PeptideAtlasi O14556.
    PRIDEi O14556.

    Protocols and materials databases

    DNASUi 26330.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222286 ; ENSP00000222286 ; ENSG00000105679 .
    GeneIDi 26330.
    KEGGi hsa:26330.
    UCSCi uc002oaf.1. human.

    Organism-specific databases

    CTDi 26330.
    GeneCardsi GC19P036024.
    HGNCi HGNC:24864. GAPDHS.
    HPAi HPA042666.
    MIMi 609169. gene.
    neXtProti NX_O14556.
    PharmGKBi PA134934259.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0057.
    HOGENOMi HOG000071678.
    HOVERGENi HBG000227.
    InParanoidi O14556.
    KOi K10705.
    OMAi NDKWGIE.
    OrthoDBi EOG7Q5HDF.
    PhylomeDBi O14556.
    TreeFami TF300533.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00184 .
    BioCyci MetaCyc:HS02793-MONOMER.
    Reactomei REACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.

    Miscellaneous databases

    EvolutionaryTracei O14556.
    GeneWikii GAPDHS.
    GenomeRNAii 26330.
    NextBioi 48663.
    PROi O14556.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14556.
    Bgeei O14556.
    CleanExi HS_GAPDHS.
    Genevestigatori O14556.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR020831. GlycerAld/Erythrose_P_DH.
    IPR020830. GlycerAld_3-P_DH_AS.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006424. Glyceraldehyde-3-P_DH_1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10836. PTHR10836. 1 hit.
    Pfami PF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000149. GAP_DH. 1 hit.
    PRINTSi PR00078. G3PDHDRGNASE.
    SMARTi SM00846. Gp_dh_N. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01534. GAPDH-I. 1 hit.
    PROSITEi PS00071. GAPDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of human testis-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDH-2) cDNA."
      McLaughlin E.A., Hall L.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    2. "Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells."
      Welch J.E., Brown P.L., O'Brien D.A., Magyar P.L., Bunch D.O., Mori C., Eddy E.M.
      J. Androl. 21:328-338(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "A new spermatogenesis-related gene."
      Zhao H., Miao S.Y., Zhang X.D., Liang G., Qiao Y., Wang L.F.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    4. "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: Testis.
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      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: Testis.
    7. "Novel function of beta-arrestin2 in the nucleus of mature spermatozoa."
      Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.
      J. Cell Sci. 119:3047-3056(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB2.
    8. "Investigation of glyceraldehyde-3-phosphate dehydrogenase from human sperms."
      Shchutskaya Y.Y., Elkina Y.L., Kuravsky M.L., Bragina E.E., Schmalhausen E.V.
      Biochemistry (Mosc.) 73:185-191(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN N-TERMINAL EXTENSION, SUBUNIT.
    9. "Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS."
      Chaikuad A., Shafqat N., Al-Mokhtar R., Cameron G., Clarke A.R., Brady R.L., Oppermann U., Frayne J., Yue W.W.
      Biochem. J. 435:401-409(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 69-407 IN COMPLEX WITH NAD AND GLYCEROL, ACTIVE SITE, SUBUNIT.

    Entry informationi

    Entry nameiG3PT_HUMAN
    AccessioniPrimary (citable) accession number: O14556
    Secondary accession number(s): B2RC82
    , O60823, Q6JTT9, Q9HCU6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 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 19
      Human chromosome 19: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3