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P02743

- SAMP_HUMAN

UniProt

P02743 - SAMP_HUMAN

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Protein
Serum amyloid P-component
Gene
APCS, PTX2
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

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. complement component C1q binding Source: BHF-UCL
  3. unfolded protein binding Source: ProtInc
  4. virion binding Source: BHF-UCL
Complete GO annotation...

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: UniProt
  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 Publications
Add
BLAST
Chaini20 – 223204Serum amyloid P-component
PRO_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 Publications
CAR_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 (1 Publication).1 Publication

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.
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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP02743.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the pentaxin family.
Contains 1 pentaxin domain.

Keywords - Domaini

Signal

Phylogenomic databases

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

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
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

MNKPLLWISV LTSLLEAFAH TDLSGKVFVF PRESVTDHVN LITPLEKPLQ    50
NFTLCFRAYS DLSRAYSLFS YNTQGRDNEL LVYKERVGEY SLYIGRHKVT 100
SKVIEKFPAP VHICVSWESS SGIAEFWING TPLVKKGLRQ GYFVEAQPKI 150
VLGQEQDSYG GKFDRSQSFV GEIGDLYMWD SVLPPENILS AYQGTPLPAN 200
ILDWQALNYE IRGYVIIKPL VWV 223
Length:223
Mass (Da):25,387
Last modified:February 1, 1995 - v2
Checksum:i6C88A515FE88B393
GO

Mass spectrometryi

Molecular mass is 25462.5±1.1 Da from positions 20 - 223. Determined by ESI. 1 Publication
Molecular mass is 25463±3 Da from positions 20 - 223. Determined by MALDI. 1 Publication
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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011S → P in AAA60302. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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...

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

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

Gene expression databases

Bgeei P02743.
CleanExi HS_APCS.
Genevestigatori P02743.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
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: September 3, 2014
This is version 169 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

Similar proteinsi