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P09486

- SPRC_HUMAN

UniProt

P09486 - SPRC_HUMAN

Protein

SPARC

Gene

SPARC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca2+ with a low affinity and an EF-hand loop that binds a Ca2+ ion with a high affinity.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi274 – 28512Add
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: ProtInc
    2. collagen binding Source: ProtInc
    3. extracellular matrix binding Source: Ensembl
    4. protein binding Source: IntAct

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. bone development Source: Ensembl
    3. cellular response to growth factor stimulus Source: Ensembl
    4. extracellular matrix organization Source: Reactome
    5. heart development Source: Ensembl
    6. inner ear development Source: Ensembl
    7. lung development Source: Ensembl
    8. ossification Source: ProtInc
    9. platelet activation Source: Reactome
    10. platelet degranulation Source: Reactome
    11. regulation of cell proliferation Source: Ensembl
    12. response to cadmium ion Source: Ensembl
    13. response to calcium ion Source: Ensembl
    14. response to cAMP Source: Ensembl
    15. response to cytokine Source: Ensembl
    16. response to ethanol Source: Ensembl
    17. response to glucocorticoid Source: Ensembl
    18. response to gravity Source: Ensembl
    19. response to L-ascorbic acid Source: Ensembl
    20. response to lead ion Source: Ensembl
    21. response to lipopolysaccharide Source: Ensembl
    22. response to peptide hormone Source: Ensembl
    23. signal transduction Source: InterPro

    Keywords - Ligandi

    Calcium, Copper, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_163906. ECM proteoglycans.
    REACT_164002. Scavenging by Class H Receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SPARC
    Alternative name(s):
    Basement-membrane protein 40
    Short name:
    BM-40
    Osteonectin
    Short name:
    ON
    Secreted protein acidic and rich in cysteine
    Gene namesi
    Name:SPARC
    Synonyms:ON
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:11219. SPARC.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrixbasement membrane 4 Publications
    Note: In or around the basement membrane.

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB-SubCell
    2. endocytic vesicle lumen Source: Reactome
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: Ensembl
    5. nucleus Source: Ensembl
    6. platelet alpha granule lumen Source: Reactome
    7. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi166 – 1661R → A, L or K: Strongly reduced collagen binding. 1 Publication
    Mutagenesisi173 – 1731N → A or Q: Strongly reduced collagen binding. 1 Publication
    Mutagenesisi259 – 2591L → A: Loss of collagen binding. 1 Publication
    Mutagenesisi262 – 2621M → A: Strongly reduced collagen binding. 1 Publication
    Mutagenesisi263 – 2631E → A: Loss of collagen binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA36055.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17172 PublicationsAdd
    BLAST
    Chaini18 – 303286SPARCPRO_0000020304Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi72 ↔ 831 PublicationPROSITE-ProRule annotation
    Disulfide bondi77 ↔ 931 PublicationPROSITE-ProRule annotation
    Disulfide bondi95 ↔ 1301 PublicationPROSITE-ProRule annotation
    Disulfide bondi101 ↔ 1231 PublicationPROSITE-ProRule annotation
    Disulfide bondi112 ↔ 1491 PublicationPROSITE-ProRule annotation
    Glycosylationi116 – 1161N-linked (GlcNAc...)2 Publications
    Disulfide bondi155 ↔ 2651 PublicationPROSITE-ProRule annotation
    Disulfide bondi273 ↔ 2891 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP09486.
    PaxDbiP09486.
    PeptideAtlasiP09486.
    PRIDEiP09486.

    2D gel databases

    OGPiP09486.

    PTM databases

    PhosphoSiteiP09486.

    Miscellaneous databases

    PMAP-CutDBP09486.

    Expressioni

    Developmental stagei

    Expressed at high levels in tissues undergoing morphogenesis, remodeling and wound repair.

    Gene expression databases

    ArrayExpressiP09486.
    BgeeiP09486.
    CleanExiHS_SPARC.
    GenevestigatoriP09486.

    Organism-specific databases

    HPAiCAB002306.
    HPA002989.
    HPA003020.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    fafQ2TV774EBI-2800983,EBI-6405263From a different organism.

    Protein-protein interaction databases

    BioGridi112560. 9 interactions.
    DIPiDIP-46426N.
    IntActiP09486. 4 interactions.
    MINTiMINT-3006855.
    STRINGi9606.ENSP00000231061.

    Structurei

    Secondary structure

    1
    303
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni71 – 744
    Beta strandi81 – 855
    Beta strandi91 – 955
    Helixi98 – 1003
    Helixi107 – 1093
    Beta strandi111 – 1133
    Turni114 – 1163
    Beta strandi118 – 1214
    Helixi122 – 13110
    Turni132 – 1343
    Helixi136 – 1405
    Beta strandi143 – 1486
    Helixi157 – 18125
    Beta strandi183 – 1886
    Helixi190 – 20112
    Helixi213 – 22210
    Helixi224 – 2274
    Helixi228 – 23811
    Beta strandi244 – 2474
    Turni249 – 2524
    Helixi253 – 2564
    Turni257 – 2593
    Helixi260 – 2623
    Helixi263 – 2653
    Helixi266 – 2738
    Beta strandi278 – 2825
    Helixi283 – 2897
    Helixi294 – 2963
    Helixi299 – 3013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BMOX-ray3.10A/B71-303[»]
    1NUBX-ray2.80A/B71-303[»]
    1SRAX-ray2.00A153-303[»]
    2V53X-ray3.20A70-303[»]
    ProteinModelPortaliP09486.
    SMRiP09486. Positions 71-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09486.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini71 – 9323Follistatin-likeAdd
    BLAST
    Domaini89 – 15163Kazal-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini261 – 29636EF-handAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi22 – 6948Asp/Glu-rich (acidic; binds calcium)Add
    BLAST

    Sequence similaritiesi

    Belongs to the SPARC family.Curated
    Contains 1 EF-hand domain.Curated
    Contains 1 follistatin-like domain.Curated
    Contains 1 Kazal-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG147672.
    HOVERGENiHBG002746.
    InParanoidiP09486.
    OMAiCFGIKEK.
    OrthoDBiEOG738059.
    PhylomeDBiP09486.
    TreeFamiTF319356.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR003645. Fol_N.
    IPR015369. Follistatin/Osteonectin_EGF.
    IPR002350. Kazal_dom.
    IPR001999. Osteonectin_CS.
    IPR019577. SPARC/Testican_Ca-bd-dom.
    [Graphical view]
    PfamiPF09289. FOLN. 1 hit.
    PF00050. Kazal_1. 1 hit.
    PF10591. SPARC_Ca_bdg. 1 hit.
    [Graphical view]
    SMARTiSM00274. FOLN. 1 hit.
    SM00280. KAZAL. 1 hit.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS51465. KAZAL_2. 1 hit.
    PS00612. OSTEONECTIN_1. 1 hit.
    PS00613. OSTEONECTIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P09486-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRAWIFFLLC LAGRALAAPQ QEALPDETEV VEETVAEVTE VSVGANPVQV    50
    EVGEFDDGAE ETEEEVVAEN PCQNHHCKHG KVCELDENNT PMCVCQDPTS 100
    CPAPIGEFEK VCSNDNKTFD SSCHFFATKC TLEGTKKGHK LHLDYIGPCK 150
    YIPPCLDSEL TEFPLRMRDW LKNVLVTLYE RDEDNNLLTE KQKLRVKKIH 200
    ENEKRLEAGD HPVELLARDF EKNYNMYIFP VHWQFGQLDQ HPIDGYLSHT 250
    ELAPLRAPLI PMEHCTTRFF ETCDLDNDKY IALDEWAGCF GIKQKDIDKD 300
    LVI 303
    Length:303
    Mass (Da):34,632
    Last modified:July 1, 1989 - v1
    Checksum:iB914599F79705945
    GO

    Sequence cautioni

    The sequence AAA60993.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 432SV → PT AA sequence (PubMed:3597437)Curated
    Sequence conflicti205 – 2051R → L in AAA60993. (PubMed:2790009)Curated
    Sequence conflicti269 – 2691F → L in AAA60993. (PubMed:2790009)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191P → S.
    Corresponds to variant rs6874468 [ dbSNP | Ensembl ].
    VAR_050431
    Natural varianti70 – 701N → S.
    Corresponds to variant rs13359508 [ dbSNP | Ensembl ].
    VAR_059530

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00755 mRNA. Translation: CAA68724.1.
    J03040 mRNA. Translation: AAA60570.1.
    M25746
    , M25738, M25739, M25740, M25741, M25742, M25743, M25744, M25745 Genomic DNA. Translation: AAA60993.1. Sequence problems.
    CR456799 mRNA. Translation: CAG33080.1.
    CH471062 Genomic DNA. Translation: EAW61668.1.
    CH471062 Genomic DNA. Translation: EAW61669.1.
    CH471062 Genomic DNA. Translation: EAW61670.1.
    CH471062 Genomic DNA. Translation: EAW61672.1.
    BC004974 mRNA. Translation: AAH04974.1.
    BC008011 mRNA. Translation: AAH08011.1.
    BC072457 mRNA. Translation: AAH72457.1.
    AL709729 mRNA. No translation available.
    CCDSiCCDS4318.1.
    PIRiA32821. GEHUN.
    RefSeqiNP_003109.1. NM_003118.3.
    UniGeneiHs.111779.

    Genome annotation databases

    EnsembliENST00000231061; ENSP00000231061; ENSG00000113140.
    GeneIDi6678.
    KEGGihsa:6678.
    UCSCiuc003lui.4. human.

    Polymorphism databases

    DMDMi129283.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Osteonectin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00755 mRNA. Translation: CAA68724.1 .
    J03040 mRNA. Translation: AAA60570.1 .
    M25746
    , M25738 , M25739 , M25740 , M25741 , M25742 , M25743 , M25744 , M25745 Genomic DNA. Translation: AAA60993.1 . Sequence problems.
    CR456799 mRNA. Translation: CAG33080.1 .
    CH471062 Genomic DNA. Translation: EAW61668.1 .
    CH471062 Genomic DNA. Translation: EAW61669.1 .
    CH471062 Genomic DNA. Translation: EAW61670.1 .
    CH471062 Genomic DNA. Translation: EAW61672.1 .
    BC004974 mRNA. Translation: AAH04974.1 .
    BC008011 mRNA. Translation: AAH08011.1 .
    BC072457 mRNA. Translation: AAH72457.1 .
    AL709729 mRNA. No translation available.
    CCDSi CCDS4318.1.
    PIRi A32821. GEHUN.
    RefSeqi NP_003109.1. NM_003118.3.
    UniGenei Hs.111779.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BMO X-ray 3.10 A/B 71-303 [» ]
    1NUB X-ray 2.80 A/B 71-303 [» ]
    1SRA X-ray 2.00 A 153-303 [» ]
    2V53 X-ray 3.20 A 70-303 [» ]
    ProteinModelPortali P09486.
    SMRi P09486. Positions 71-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112560. 9 interactions.
    DIPi DIP-46426N.
    IntActi P09486. 4 interactions.
    MINTi MINT-3006855.
    STRINGi 9606.ENSP00000231061.

    Chemistry

    DrugBanki DB00102. Becaplermin.

    PTM databases

    PhosphoSitei P09486.

    Polymorphism databases

    DMDMi 129283.

    2D gel databases

    OGPi P09486.

    Proteomic databases

    MaxQBi P09486.
    PaxDbi P09486.
    PeptideAtlasi P09486.
    PRIDEi P09486.

    Protocols and materials databases

    DNASUi 6678.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000231061 ; ENSP00000231061 ; ENSG00000113140 .
    GeneIDi 6678.
    KEGGi hsa:6678.
    UCSCi uc003lui.4. human.

    Organism-specific databases

    CTDi 6678.
    GeneCardsi GC05M151021.
    HGNCi HGNC:11219. SPARC.
    HPAi CAB002306.
    HPA002989.
    HPA003020.
    MIMi 182120. gene.
    neXtProti NX_P09486.
    PharmGKBi PA36055.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147672.
    HOVERGENi HBG002746.
    InParanoidi P09486.
    OMAi CFGIKEK.
    OrthoDBi EOG738059.
    PhylomeDBi P09486.
    TreeFami TF319356.

    Enzyme and pathway databases

    Reactomei REACT_163906. ECM proteoglycans.
    REACT_164002. Scavenging by Class H Receptors.

    Miscellaneous databases

    ChiTaRSi SPARC. human.
    EvolutionaryTracei P09486.
    GeneWikii Osteonectin.
    GenomeRNAii 6678.
    NextBioi 26041.
    PMAP-CutDB P09486.
    PROi P09486.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09486.
    Bgeei P09486.
    CleanExi HS_SPARC.
    Genevestigatori P09486.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR003645. Fol_N.
    IPR015369. Follistatin/Osteonectin_EGF.
    IPR002350. Kazal_dom.
    IPR001999. Osteonectin_CS.
    IPR019577. SPARC/Testican_Ca-bd-dom.
    [Graphical view ]
    Pfami PF09289. FOLN. 1 hit.
    PF00050. Kazal_1. 1 hit.
    PF10591. SPARC_Ca_bdg. 1 hit.
    [Graphical view ]
    SMARTi SM00274. FOLN. 1 hit.
    SM00280. KAZAL. 1 hit.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS51465. KAZAL_2. 1 hit.
    PS00612. OSTEONECTIN_1. 1 hit.
    PS00613. OSTEONECTIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and complete amino acid sequences of human and murine basement membrane protein BM-40 (SPARC, osteonectin)."
      Lankat-Buttgereit B., Mann K., Deutzmann R., Timpl R., Krieg T.
      FEBS Lett. 236:352-356(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Placenta.
    2. "Molecular analysis of the cDNA for human SPARC/osteonectin/BM-40: sequence, expression, and localization of the gene to chromosome 5q31-q33."
      Swaroop A., Hogan B.L.M., Francke U.
      Genomics 2:37-47(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Structure of human osteonectin based upon analysis of cDNA and genomic sequences."
      Villarreal X.C., Mann K.G., Long G.L.
      Biochemistry 28:6483-6491(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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: Muscle, PNS and Skin.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-154.
    9. "Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone."
      Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.
      J. Biol. Chem. 262:9702-9708(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-53, CHARACTERIZATION.
    10. "Human platelet osteonectin: release, surface expression, and partial characterization."
      Kelm R.J. Jr., Mann K.G.
      Blood 75:1105-1113(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-41, CHARACTERIZATION, SUBCELLULAR LOCATION.
    11. "Osteonectin/SPARC/BM-40 in human decidua and carcinoma, tissues characterized by de novo formation of basement membrane."
      Wewer U.M., Albrechtsen R., Fisher L.W., Young M.F., Termine J.D.
      Am. J. Pathol. 132:345-355(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Immunolocalization of SPARC, tenascin, and thrombospondin in pulmonary fibrosis."
      Kuhn C., Mason R.J.
      Am. J. Pathol. 147:1759-1769(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "BM-40 (osteonectin, SPARC) is expressed both in the epidermal and in the dermal compartment of adult human skin."
      Hunzelmann N., Hafner M., Anders S., Krieg T., Nischt R.
      J. Invest. Dermatol. 110:122-126(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "Structure of a novel extracellular Ca(2+)-binding module in BM-40."
      Hohenester E., Maurer P., Hahoenadl C., Timpl R., Jansonius J.N., Engel J.
      Nat. Struct. Biol. 3:67-73(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-303.
    15. "Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40."
      Hohenester E., Maurer P., Timpl R.
      EMBO J. 16:3778-3786(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 71-303 IN COMPLEX WITH CALCIUM IONS, GLYCOSYLATION AT ASN-116, DISULFIDE BONDS.
    16. "Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin."
      Sasaki T., Hohenester E., Gohring W., Timpl R.
      EMBO J. 17:1625-1634(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 71-303 IN COMPLEX WITH CALCIUM IONS, GLYCOSYLATION AT ASN-116, INTERACTION WITH COLLAGEN, MUTAGENESIS OF ARG-166; ASN-173; LEU-259; MET-262 AND GLU-263.

    Entry informationi

    Entry nameiSPRC_HUMAN
    AccessioniPrimary (citable) accession number: P09486
    Secondary accession number(s): D3DQH9, Q6IBK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 166 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3