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P02743

- SAMP_HUMAN

UniProt

P02743 - SAMP_HUMAN

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Protein

Serum amyloid P-component

Gene

APCS

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

Functioni

Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.

Cofactori

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi77 – 771Calcium 1
Metal bindingi78 – 781Calcium 1
Metal bindingi155 – 1551Calcium 1
Metal bindingi155 – 1551Calcium 2
Metal bindingi156 – 1561Calcium 1; via carbonyl oxygen
Metal bindingi157 – 1571Calcium 1
Metal bindingi157 – 1571Calcium 2
Metal bindingi167 – 1671Calcium 2

GO - Molecular functioni

  1. calcium ion binding Source: BHF-UCL
  2. carbohydrate binding Source: UniProtKB-KW
  3. complement component C1q binding Source: BHF-UCL
  4. unfolded protein binding Source: ProtInc
  5. virion binding Source: BHF-UCL

GO - Biological processi

  1. acute-phase response Source: ProtInc
  2. chaperone-mediated protein complex assembly Source: ProtInc
  3. innate immune response Source: BHF-UCL
  4. negative regulation of acute inflammatory response Source: BHF-UCL
  5. negative regulation of exo-alpha-sialidase activity Source: BHF-UCL
  6. negative regulation of glycoprotein metabolic process Source: BHF-UCL
  7. negative regulation of monocyte differentiation Source: BHF-UCL
  8. negative regulation of viral entry into host cell Source: BHF-UCL
  9. negative regulation of viral process Source: BHF-UCL
  10. negative regulation of wound healing Source: BHF-UCL
  11. protein folding Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_75925. Amyloids.

Protein family/group databases

TCDBi1.C.92.1.2. the pentraxin (pentraxin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Serum amyloid P-component
Short name:
SAP
Alternative name(s):
9.5S alpha-1-glycoprotein
Cleaved into the following chain:
Gene namesi
Name:APCS
Synonyms:PTX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:584. APCS.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProtKB
  5. nucleus Source: UniProt
  6. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Secreted

Pathology & Biotechi

Involvement in diseasei

SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits.

Organism-specific databases

PharmGKBiPA24877.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19192 PublicationsAdd
BLAST
Chaini20 – 223204Serum amyloid P-componentPRO_0000023540Add
BLAST
Chaini20 – 222203Serum amyloid P-component(1-203)PRO_0000023541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...)2 PublicationsCAR_000169
Disulfide bondi55 ↔ 1141 Publication

Post-translational modificationi

N-glycosylated with a complex biantennary oligosaccharide chain with a sialic acid at the end (disialo-SAP). Monosialo-SAP as well as asioalo-SAP are also detected (PubMed:15174148).3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP02743.
PeptideAtlasiP02743.
PRIDEiP02743.

2D gel databases

DOSAC-COBS-2DPAGEP02743.
OGPiP02743.
REPRODUCTION-2DPAGEIPI00022391.
P02743.
SWISS-2DPAGEP02743.

PTM databases

PhosphoSiteiP02743.
UniCarbKBiP02743.

Expressioni

Tissue specificityi

Found in serum and urine.1 Publication

Gene expression databases

BgeeiP02743.
CleanExiHS_APCS.
ExpressionAtlasiP02743. baseline.
GenevestigatoriP02743.

Organism-specific databases

HPAiCAB007817.
HPA053294.

Interactioni

Subunit structurei

Homopentamer. Pentaxin (or pentraxin) have a discoid arrangement of 5 non-covalently bound subunits.

Protein-protein interaction databases

BioGridi106822. 13 interactions.
DIPiDIP-46911N.
IntActiP02743. 5 interactions.
MINTiMINT-4723480.
STRINGi9606.ENSP00000255040.

Structurei

Secondary structure

1
223
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 305Combined sources
Beta strandi38 – 414Combined sources
Beta strandi49 – 5911Combined sources
Beta strandi66 – 738Combined sources
Beta strandi76 – 8611Combined sources
Beta strandi89 – 946Combined sources
Beta strandi97 – 1026Combined sources
Beta strandi111 – 1188Combined sources
Turni119 – 1213Combined sources
Beta strandi123 – 1286Combined sources
Beta strandi149 – 1546Combined sources
Beta strandi157 – 1604Combined sources
Helixi165 – 1673Combined sources
Beta strandi171 – 18111Combined sources
Helixi185 – 1939Combined sources
Beta strandi200 – 2034Combined sources
Helixi204 – 2063Combined sources
Beta strandi209 – 2146Combined sources
Beta strandi216 – 2194Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYKX-ray2.20A/B/C/D/E20-223[»]
1LGNX-ray2.80A/B/C/D/E20-223[»]
1SACX-ray2.00A/B/C/D/E20-223[»]
2A3WX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T20-223[»]
2A3XX-ray3.00A/B/C/D/E/F/G/H/I/J20-223[»]
2A3YX-ray2.00A/B/C/D/E20-223[»]
2W08X-ray1.70A/B/C/D/E20-223[»]
3D5OX-ray2.80A/B/C/D/E20-223[»]
3KQRX-ray1.50A/B/C/D/E20-223[»]
4AVSX-ray1.40A/B/C/D/E20-223[»]
4AVTX-ray3.20A/B/C/D/E/F/G/H/I/J20-223[»]
4AVVX-ray1.60A/B/C/D/E20-223[»]
4AYUX-ray1.50A/B/C/D/E20-223[»]
ProteinModelPortaliP02743.
SMRiP02743. Positions 20-223.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02743.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 223204PentaxinAdd
BLAST

Sequence similaritiesi

Belongs to the pentaxin family.Curated
Contains 1 pentaxin domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG44770.
HOGENOMiHOG000247043.
HOVERGENiHBG005405.
InParanoidiP02743.
OMAiAEFWING.
OrthoDBiEOG71RXMB.
PhylomeDBiP02743.
TreeFamiTF330208.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001759. Pentaxin.
[Graphical view]
PfamiPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSiPR00895. PENTAXIN.
SMARTiSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00289. PENTAXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02743-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKPLLWISV LTSLLEAFAH TDLSGKVFVF PRESVTDHVN LITPLEKPLQ
60 70 80 90 100
NFTLCFRAYS DLSRAYSLFS YNTQGRDNEL LVYKERVGEY SLYIGRHKVT
110 120 130 140 150
SKVIEKFPAP VHICVSWESS SGIAEFWING TPLVKKGLRQ GYFVEAQPKI
160 170 180 190 200
VLGQEQDSYG GKFDRSQSFV GEIGDLYMWD SVLPPENILS AYQGTPLPAN
210 220
ILDWQALNYE IRGYVIIKPL VWV
Length:223
Mass (Da):25,387
Last modified:February 1, 1995 - v2
Checksum:i6C88A515FE88B393
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011S → P in AAA60302. (PubMed:2987268)Curated

Mass spectrometryi

Molecular mass is 25462.5±1.1 Da from positions 20 - 223. Determined by ESI. 2 Publications
Molecular mass is 25463±3 Da from positions 20 - 223. Determined by MALDI. 2 Publications
Molecular mass is 1285.78 Da from positions 213 - 223. Determined by MALDI. 1 Publication
Molecular mass is 1186.71 Da from positions 213 - 222. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411G → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_035814
Natural varianti155 – 1551E → G.
VAR_006054
Natural varianti158 – 1581S → G.
VAR_006055

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00097 Genomic DNA. Translation: BAA00060.1.
M10944 mRNA. Translation: AAA60302.1.
X04608 mRNA. Translation: CAA28275.1.
CR450313 mRNA. Translation: CAG29309.1.
AL445528 Genomic DNA. Translation: CAH73651.1.
BT006750 mRNA. Translation: AAP35396.1.
BC007039 mRNA. Translation: AAH07039.1.
BC007058 mRNA. Translation: AAH07058.1.
CCDSiCCDS1186.1.
PIRiA25503. YLHUP.
RefSeqiNP_001630.1. NM_001639.3.
UniGeneiHs.507080.

Genome annotation databases

EnsembliENST00000255040; ENSP00000255040; ENSG00000132703.
GeneIDi325.
KEGGihsa:325.
UCSCiuc001ftv.3. human.

Polymorphism databases

DMDMi730704.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Serum amyloid P component entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00097 Genomic DNA. Translation: BAA00060.1 .
M10944 mRNA. Translation: AAA60302.1 .
X04608 mRNA. Translation: CAA28275.1 .
CR450313 mRNA. Translation: CAG29309.1 .
AL445528 Genomic DNA. Translation: CAH73651.1 .
BT006750 mRNA. Translation: AAP35396.1 .
BC007039 mRNA. Translation: AAH07039.1 .
BC007058 mRNA. Translation: AAH07058.1 .
CCDSi CCDS1186.1.
PIRi A25503. YLHUP.
RefSeqi NP_001630.1. NM_001639.3.
UniGenei Hs.507080.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GYK X-ray 2.20 A/B/C/D/E 20-223 [» ]
1LGN X-ray 2.80 A/B/C/D/E 20-223 [» ]
1SAC X-ray 2.00 A/B/C/D/E 20-223 [» ]
2A3W X-ray 2.20 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 20-223 [» ]
2A3X X-ray 3.00 A/B/C/D/E/F/G/H/I/J 20-223 [» ]
2A3Y X-ray 2.00 A/B/C/D/E 20-223 [» ]
2W08 X-ray 1.70 A/B/C/D/E 20-223 [» ]
3D5O X-ray 2.80 A/B/C/D/E 20-223 [» ]
3KQR X-ray 1.50 A/B/C/D/E 20-223 [» ]
4AVS X-ray 1.40 A/B/C/D/E 20-223 [» ]
4AVT X-ray 3.20 A/B/C/D/E/F/G/H/I/J 20-223 [» ]
4AVV X-ray 1.60 A/B/C/D/E 20-223 [» ]
4AYU X-ray 1.50 A/B/C/D/E 20-223 [» ]
ProteinModelPortali P02743.
SMRi P02743. Positions 20-223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106822. 13 interactions.
DIPi DIP-46911N.
IntActi P02743. 5 interactions.
MINTi MINT-4723480.
STRINGi 9606.ENSP00000255040.

Chemistry

ChEMBLi CHEMBL4929.

Protein family/group databases

TCDBi 1.C.92.1.2. the pentraxin (pentraxin) family.

PTM databases

PhosphoSitei P02743.
UniCarbKBi P02743.

Polymorphism databases

DMDMi 730704.

2D gel databases

DOSAC-COBS-2DPAGE P02743.
OGPi P02743.
REPRODUCTION-2DPAGE IPI00022391.
P02743.
SWISS-2DPAGE P02743.

Proteomic databases

PaxDbi P02743.
PeptideAtlasi P02743.
PRIDEi P02743.

Protocols and materials databases

DNASUi 325.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000255040 ; ENSP00000255040 ; ENSG00000132703 .
GeneIDi 325.
KEGGi hsa:325.
UCSCi uc001ftv.3. human.

Organism-specific databases

CTDi 325.
GeneCardsi GC01P159557.
HGNCi HGNC:584. APCS.
HPAi CAB007817.
HPA053294.
MIMi 104770. gene.
neXtProti NX_P02743.
PharmGKBi PA24877.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG44770.
HOGENOMi HOG000247043.
HOVERGENi HBG005405.
InParanoidi P02743.
OMAi AEFWING.
OrthoDBi EOG71RXMB.
PhylomeDBi P02743.
TreeFami TF330208.

Enzyme and pathway databases

Reactomei REACT_75925. Amyloids.

Miscellaneous databases

ChiTaRSi APCS. human.
EvolutionaryTracei P02743.
GeneWikii Serum_amyloid_P_component.
GenomeRNAii 325.
NextBioi 1333.
PROi P02743.
SOURCEi Search...

Gene expression databases

Bgeei P02743.
CleanExi HS_APCS.
ExpressionAtlasi P02743. baseline.
Genevestigatori P02743.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR001759. Pentaxin.
[Graphical view ]
Pfami PF00354. Pentaxin. 1 hit.
[Graphical view ]
PRINTSi PR00895. PENTAXIN.
SMARTi SM00159. PTX. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00289. PENTAXIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human serum amyloid P component. cDNA isolation, complete sequence of pre-serum amyloid P component, and localization of the gene to chromosome 1."
    Mantzouranis E.C., Dowton S.B., Whitehead A.S., Edge M.D., Bruns G.A.P., Colten H.R.
    J. Biol. Chem. 260:7752-7756(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation and characterization of the complete complementary and genomic DNA sequences of human serum amyloid P component."
    Ohnishi S., Maeda S., Shimada K., Arao T.
    J. Biochem. 100:849-858(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
    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. "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: Skeletal muscle.
  7. "The primary structure of human tissue amyloid P component from a patient with primary idiopathic amyloidosis."
    Prelli F., Pras M., Frangione B.
    J. Biol. Chem. 260:12895-12898(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-223.
  8. "Human plasma P component: isolation and characterization."
    Thompson A.R., Enfield D.L.
    Biochemistry 17:4304-4311(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-49.
  9. "Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure."
    Pepys M.B., Rademacher T.W., Amatayakul-Chantler S., Williams P., Noble G.E., Hutchinson W.L., Hawkins P.N., Nelson S.R., Gallimore J.R., Herbert J., Hutton T., Dwek R.A.
    Proc. Natl. Acad. Sci. U.S.A. 91:5602-5606(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATE, MASS SPECTROMETRY.
  10. "Proteomic characterization of novel serum amyloid P component variants from human plasma and urine."
    Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W.
    Proteomics 4:1825-1829(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, MASS SPECTROMETRY.
  11. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51.
    Tissue: Plasma.
  12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51.
    Tissue: Liver.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  15. "Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP."
    Hohenester E., Hutchinson W.L., Pepys M.B., Wood S.P.
    J. Mol. Biol. 269:570-578(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-141.

Entry informationi

Entry nameiSAMP_HUMAN
AccessioniPrimary (citable) accession number: P02743
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 172 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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