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P23297

- S10A1_HUMAN

UniProt

P23297 - S10A1_HUMAN

Protein

Protein S100-A1

Gene

S100A1

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

    Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi20 – 33141; low affinityAdd
    BLAST
    Calcium bindingi63 – 74122; high affinityAdd
    BLAST

    GO - Molecular functioni

    1. ATPase binding Source: UniProtKB
    2. calcium ion binding Source: ProtInc
    3. identical protein binding Source: IntAct
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. S100 protein binding Source: UniProtKB

    GO - Biological processi

    1. intracellular signal transduction Source: UniProtKB
    2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    3. positive regulation of voltage-gated calcium channel activity Source: Ensembl
    4. regulation of heart contraction Source: UniProtKB
    5. substantia nigra development Source: UniProt

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein S100-A1
    Alternative name(s):
    S-100 protein alpha chain
    S-100 protein subunit alpha
    S100 calcium-binding protein A1
    Gene namesi
    Name:S100A1
    Synonyms:S100A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10486. S100A1.

    Subcellular locationi

    GO - Cellular componenti

    1. M band Source: Ensembl
    2. neuron projection Source: Ensembl
    3. nucleus Source: UniProtKB
    4. protein complex Source: UniProtKB
    5. sarcoplasmic reticulum Source: UniProtKB
    6. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34898.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 9493Protein S100-A1PRO_0000143961Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei86 – 861S-nitrosocysteine1 Publication

    Keywords - PTMi

    S-nitrosylation

    Proteomic databases

    MaxQBiP23297.
    PaxDbiP23297.
    PRIDEiP23297.

    Expressioni

    Tissue specificityi

    Highly prevalent in heart. Also found in lesser quantities in skeletal muscle and brain.

    Gene expression databases

    ArrayExpressiP23297.
    BgeeiP23297.
    CleanExiHS_S100A1.
    GenevestigatoriP23297.

    Organism-specific databases

    HPAiCAB002599.
    HPA006462.

    Interactioni

    Subunit structurei

    Dimer of either two alpha chains, or two beta chains, or one alpha and one beta chain. Also forms heterodimers with S100P. Interacts with AGER and CAPZA1. Interacts with FKBP4. Interacts with RYR1 and RYR2. Interacts with CACYBP in a calcium-dependent manner. Interacts with PPP5C (via TPR repeats); the interaction is calcium-dependent and modulates PPP5C activity.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-743686,EBI-743686
    MDM2Q009872EBI-743686,EBI-389668
    S100BP042717EBI-743686,EBI-458391
    S100PP258157EBI-743686,EBI-743700
    TP53P046372EBI-743686,EBI-366083

    Protein-protein interaction databases

    BioGridi112179. 18 interactions.
    IntActiP23297. 8 interactions.
    MINTiMINT-1543322.
    STRINGi9606.ENSP00000292169.

    Structurei

    Secondary structure

    1
    94
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 2017
    Beta strandi22 – 243
    Beta strandi26 – 305
    Helixi31 – 4111
    Helixi45 – 484
    Helixi52 – 6413
    Turni65 – 673
    Beta strandi68 – 703
    Helixi72 – 8716
    Turni88 – 903

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L0PNMR-A/B1-94[»]
    2LHLNMR-A/B2-94[»]
    2LLSNMR-A/B2-94[»]
    2LLTNMR-A/B2-94[»]
    2LLUNMR-A/B2-94[»]
    2LP2NMR-A/B2-94[»]
    2LP3NMR-A/B2-94[»]
    2LUXNMR-A/B2-94[»]
    2M3WNMR-A/B2-94[»]
    ProteinModelPortaliP23297.
    SMRiP23297. Positions 2-94.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 4836EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini50 – 8536EF-hand 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the S-100 family.Curated
    Contains 2 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG277258.
    HOGENOMiHOG000246968.
    HOVERGENiHBG001479.
    InParanoidiP23297.
    PhylomeDBiP23297.
    TreeFamiTF332727.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR028486. S100-A1.
    IPR001751. S100/CaBP-9k_CS.
    IPR013787. S100_Ca-bd_sub.
    [Graphical view]
    PANTHERiPTHR11639:SF66. PTHR11639:SF66. 1 hit.
    PfamiPF00036. EF-hand_1. 1 hit.
    PF01023. S_100. 1 hit.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS00303. S100_CABP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23297-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKELLQT ELSGFLDAQK   50
    DVDAVDKVMK ELDENGDGEV DFQEYVVLVA ALTVACNNFF WENS 94
    Length:94
    Mass (Da):10,546
    Last modified:January 23, 2007 - v2
    Checksum:iAD5E53AF326B25D2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58079 mRNA. Translation: CAA41107.1.
    AK312152 mRNA. Translation: BAG35086.1.
    BT006938 mRNA. Translation: AAP35584.1.
    AB451316 mRNA. Translation: BAG70130.1.
    AB451446 mRNA. Translation: BAG70260.1.
    AL162258 Genomic DNA. Translation: CAI19677.1.
    CH471121 Genomic DNA. Translation: EAW53302.1.
    BC014392 mRNA. Translation: AAH14392.1.
    CCDSiCCDS1047.1.
    PIRiA44470. BCHUIA.
    RefSeqiNP_006262.1. NM_006271.1.
    UniGeneiHs.515715.

    Genome annotation databases

    EnsembliENST00000292169; ENSP00000292169; ENSG00000160678.
    GeneIDi6271.
    KEGGihsa:6271.
    UCSCiuc001fck.1. human.

    Polymorphism databases

    DMDMi134136.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58079 mRNA. Translation: CAA41107.1 .
    AK312152 mRNA. Translation: BAG35086.1 .
    BT006938 mRNA. Translation: AAP35584.1 .
    AB451316 mRNA. Translation: BAG70130.1 .
    AB451446 mRNA. Translation: BAG70260.1 .
    AL162258 Genomic DNA. Translation: CAI19677.1 .
    CH471121 Genomic DNA. Translation: EAW53302.1 .
    BC014392 mRNA. Translation: AAH14392.1 .
    CCDSi CCDS1047.1.
    PIRi A44470. BCHUIA.
    RefSeqi NP_006262.1. NM_006271.1.
    UniGenei Hs.515715.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L0P NMR - A/B 1-94 [» ]
    2LHL NMR - A/B 2-94 [» ]
    2LLS NMR - A/B 2-94 [» ]
    2LLT NMR - A/B 2-94 [» ]
    2LLU NMR - A/B 2-94 [» ]
    2LP2 NMR - A/B 2-94 [» ]
    2LP3 NMR - A/B 2-94 [» ]
    2LUX NMR - A/B 2-94 [» ]
    2M3W NMR - A/B 2-94 [» ]
    ProteinModelPortali P23297.
    SMRi P23297. Positions 2-94.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112179. 18 interactions.
    IntActi P23297. 8 interactions.
    MINTi MINT-1543322.
    STRINGi 9606.ENSP00000292169.

    Chemistry

    DrugBanki DB00768. Olopatadine.

    Polymorphism databases

    DMDMi 134136.

    Proteomic databases

    MaxQBi P23297.
    PaxDbi P23297.
    PRIDEi P23297.

    Protocols and materials databases

    DNASUi 6271.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000292169 ; ENSP00000292169 ; ENSG00000160678 .
    GeneIDi 6271.
    KEGGi hsa:6271.
    UCSCi uc001fck.1. human.

    Organism-specific databases

    CTDi 6271.
    GeneCardsi GC01P153600.
    HGNCi HGNC:10486. S100A1.
    HPAi CAB002599.
    HPA006462.
    MIMi 176940. gene.
    neXtProti NX_P23297.
    PharmGKBi PA34898.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG277258.
    HOGENOMi HOG000246968.
    HOVERGENi HBG001479.
    InParanoidi P23297.
    PhylomeDBi P23297.
    TreeFami TF332727.

    Miscellaneous databases

    GeneWikii S100_calcium-binding_protein_A1.
    GenomeRNAii 6271.
    NextBioi 24339.
    PROi P23297.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23297.
    Bgeei P23297.
    CleanExi HS_S100A1.
    Genevestigatori P23297.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR028486. S100-A1.
    IPR001751. S100/CaBP-9k_CS.
    IPR013787. S100_Ca-bd_sub.
    [Graphical view ]
    PANTHERi PTHR11639:SF66. PTHR11639:SF66. 1 hit.
    Pfami PF00036. EF-hand_1. 1 hit.
    PF01023. S_100. 1 hit.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS00303. S100_CABP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart."
      Engelkamp D., Schaefer B.W., Erne P., Heizmann C.W.
      Biochemistry 31:10258-10264(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    2. "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: Caudate nucleus.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Skin.
    8. "CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family."
      Filipek A., Jastrzebska B., Nowotny M., Kuznicki J.
      J. Biol. Chem. 277:28848-28852(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CACYBP.
    9. Cited for: INTERACTION WITH S100P.
    10. "S100A1 and calmodulin compete for the same binding site on ryanodine receptor."
      Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J.
      J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RYR1 AND RYR2.
    11. "S100 proteins regulate the interaction of Hsp90 with cyclophilin 40 and FKBP52 through their tetratricopeptide repeats."
      Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.
      FEBS Lett. 584:1119-1125(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FKBP4.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "S100 proteins modulate protein phosphatase 5 function: a link between CA2+ signal transduction and protein dephosphorylation."
      Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H., Tokuda M., Kobayashi R.
      J. Biol. Chem. 287:13787-13798(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PPP5C.
    14. Cited for: STRUCTURE BY NMR, SUBUNIT.
    15. "Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein."
      Lenarcic Zivkovic M., Zareba-Koziol M., Zhukova L., Poznanski J., Zhukov I., Wyslouch-Cieszynska A.
      J. Biol. Chem. 287:40457-40470(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-94, S-NITROSYLATION AT CYS-86.

    Entry informationi

    Entry nameiS10A1_HUMAN
    AccessioniPrimary (citable) accession number: P23297
    Secondary accession number(s): B2R5D9, Q5T7Y3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 144 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 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