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P09486

- SPRC_HUMAN

UniProt

P09486 - SPRC_HUMAN

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Protein

SPARC

Gene

SPARC

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

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: UniProtKB
  2. collagen binding Source: UniProtKB
  3. extracellular matrix binding Source: Ensembl

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. negative regulation of angiogenesis Source: UniProtKB
  9. negative regulation of endothelial cell proliferation Source: UniProtKB
  10. ossification Source: Ensembl
  11. platelet activation Source: Reactome
  12. platelet degranulation Source: Reactome
  13. positive regulation of endothelial cell migration Source: UniProtKB
  14. regulation of cell morphogenesis Source: UniProtKB
  15. response to cadmium ion Source: Ensembl
  16. response to calcium ion Source: Ensembl
  17. response to cAMP Source: Ensembl
  18. response to cytokine Source: Ensembl
  19. response to ethanol Source: Ensembl
  20. response to glucocorticoid Source: Ensembl
  21. response to gravity Source: Ensembl
  22. response to L-ascorbic acid Source: Ensembl
  23. response to lead ion Source: Ensembl
  24. response to lipopolysaccharide Source: Ensembl
  25. response to peptide hormone Source: Ensembl
  26. signal transduction Source: InterPro
Complete GO annotation...

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-KW
  2. cell surface Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. endocytic vesicle lumen Source: Reactome
  5. extracellular region Source: UniProtKB
  6. extracellular space Source: Ensembl
  7. nuclear matrix Source: UniProtKB
  8. platelet alpha granule Source: UniProtKB
  9. platelet alpha granule lumen Source: Reactome
  10. platelet alpha granule membrane Source: UniProtKB
Complete GO annotation...

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

BgeeiP09486.
CleanExiHS_SPARC.
ExpressionAtlasiP09486. baseline and differential.
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. 10 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 – 744Combined sources
Beta strandi81 – 855Combined sources
Beta strandi91 – 955Combined sources
Helixi98 – 1003Combined sources
Helixi107 – 1093Combined sources
Beta strandi111 – 1133Combined sources
Turni114 – 1163Combined sources
Beta strandi118 – 1214Combined sources
Helixi122 – 13110Combined sources
Turni132 – 1343Combined sources
Helixi136 – 1405Combined sources
Beta strandi143 – 1486Combined sources
Helixi157 – 18125Combined sources
Beta strandi183 – 1886Combined sources
Helixi190 – 20112Combined sources
Helixi213 – 22210Combined sources
Helixi224 – 2274Combined sources
Helixi228 – 23811Combined sources
Beta strandi244 – 2474Combined sources
Turni249 – 2524Combined sources
Helixi253 – 2564Combined sources
Turni257 – 2593Combined sources
Helixi260 – 2623Combined sources
Helixi263 – 2653Combined sources
Helixi266 – 2738Combined sources
Beta strandi278 – 2825Combined sources
Helixi283 – 2897Combined sources
Helixi294 – 2963Combined sources
Helixi299 – 3013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00510000046787.
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

        10         20         30         40         50
MRAWIFFLLC LAGRALAAPQ QEALPDETEV VEETVAEVTE VSVGANPVQV
60 70 80 90 100
EVGEFDDGAE ETEEEVVAEN PCQNHHCKHG KVCELDENNT PMCVCQDPTS
110 120 130 140 150
CPAPIGEFEK VCSNDNKTFD SSCHFFATKC TLEGTKKGHK LHLDYIGPCK
160 170 180 190 200
YIPPCLDSEL TEFPLRMRDW LKNVLVTLYE RDEDNNLLTE KQKLRVKKIH
210 220 230 240 250
ENEKRLEAGD HPVELLARDF EKNYNMYIFP VHWQFGQLDQ HPIDGYLSHT
260 270 280 290 300
ELAPLRAPLI PMEHCTTRFF ETCDLDNDKY IALDEWAGCF GIKQKDIDKD

LVI
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 10 interactions.
DIPi DIP-46426N.
IntActi P09486. 4 interactions.
MINTi MINT-3006855.
STRINGi 9606.ENSP00000231061.

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.
GeneTreei ENSGT00510000046787.
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

Bgeei P09486.
CleanExi HS_SPARC.
ExpressionAtlasi P09486. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 168 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