Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P02741 (CRP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 176. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-reactive protein

Cleaved into the following chain:

  1. C-reactive protein(1-205)
Gene names
Name:CRP
Synonyms:PTX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells.

Cofactor

Binds 2 calcium ions per subunit.

Subunit structure

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

Subcellular location

Secreted.

Tissue specificity

Found in plasma.

Induction

The concentration of CRP in plasma increases greatly during acute phase response to tissue injury, infection or other inflammatory stimuli. It is induced by IL1/interleukin-1 and IL6//interleukin-6.

Miscellaneous

This protein owes its name to its ability precipitate pneumococcal C-polysaccharide in the presence of calcium.

Sequence similarities

Belongs to the pentaxin family.

Contains 1 pentaxin domain.

Mass spectrometry

Molecular mass is 23028 Da from positions 19 - 224. Determined by MALDI. Ref.15

Molecular mass is 22930 Da from positions 19 - 223. Determined by MALDI. Ref.15

Ontologies

Keywords
   Biological processAcute phase
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Traceable author statement PubMed 2477488. Source: BHF-UCL

aging

Inferred from electronic annotation. Source: Ensembl

cellular response to calcium ion

Inferred from electronic annotation. Source: Ensembl

complement activation, classical pathway

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-positive bacterium

Traceable author statement PubMed 2477488. Source: BHF-UCL

inflammatory response

Traceable author statement PubMed 10408362. Source: ProtInc

negative regulation of lipid storage

Inferred from direct assay PubMed 18322245. Source: BHF-UCL

negative regulation of macrophage derived foam cell differentiation

Inferred from direct assay PubMed 18322245. Source: BHF-UCL

opsonization

Traceable author statement PubMed 2477488. Source: BHF-UCL

positive regulation of dendrite development

Inferred from electronic annotation. Source: Ensembl

protein polymerization

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to lead ion

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

filopodium

Inferred from electronic annotation. Source: Ensembl

growth cone

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

cholesterol binding

Inferred from electronic annotation. Source: Ensembl

choline binding

Traceable author statement PubMed 2477488. Source: BHF-UCL

complement component C1q binding

Inferred from direct assay PubMed 23544079. Source: BHF-UCL

low-density lipoprotein particle binding

Inferred from direct assay PubMed 18322245. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 17785206. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FCGR2CP319952EBI-1395983,EBI-1396036

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P02741-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P02741-2)

The sequence of this isoform differs from the canonical sequence as follows:
     67-199: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.13
Chain19 – 224206C-reactive protein
PRO_0000023526
Chain19 – 223205C-reactive protein(1-205)
PRO_0000023527

Regions

Domain19 – 224206Pentaxin

Sites

Metal binding781Calcium 1
Metal binding791Calcium 1
Metal binding1561Calcium 1
Metal binding1561Calcium 2
Metal binding1571Calcium 1; via carbonyl oxygen
Metal binding1581Calcium 1
Metal binding1581Calcium 2
Metal binding1681Calcium 2

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid Ref.13
Disulfide bond54 ↔ 115 Ref.13

Natural variations

Alternative sequence67 – 199133Missing in isoform 2.
VSP_004656

Experimental info

Sequence conflict491K → G AA sequence Ref.14
Sequence conflict521T → G AA sequence Ref.14
Sequence conflict67 – 8216YSIFS…DNEIL → TVFSRMPPRDKTMRFF in CAA39671. Ref.4
Sequence conflict80 – 9819Missing AA sequence Ref.13
Sequence conflict1701L → V in AAA52074. Ref.12

Secondary structure

....................................... 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 669228636A8544F6

FASTA22425,039
        10         20         30         40         50         60 
MEKLLCFLVL TSLSHAFGQT DMSRKAFVFP KESDTSYVSL KAPLTKPLKA FTVCLHFYTE 

        70         80         90        100        110        120 
LSSTRGYSIF SYATKRQDNE ILIFWSKDIG YSFTVGGSEI LFEVPEVTVA PVHICTSWES 

       130        140        150        160        170        180 
ASGIVEFWVD GKPRVRKSLK KGYTVGAEAS IILGQEQDSF GGNFEGSQSL VGDIGNVNMW 

       190        200        210        220 
DFVLSPDEIN TIYLGGPFSP NVLNWRALKY EVQGEVFTKP QLWP 

« Hide

Isoform 2 [UniParc].

Checksum: A5E24599540DAA05
Show »

FASTA9110,415

References

« Hide 'large scale' references
[1]"Genomic DNA sequence for human C-reactive protein."
Lei K.-J., Liu T., Zon G., Soravia E., Liu T.-Y., Goldman N.D.
J. Biol. Chem. 260:13377-13383(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of genomic and complementary DNA sequence of human C-reactive protein, and comparison with the complementary DNA sequence of serum amyloid P component."
Woo P., Korenberg J.R., Whitehead A.S.
J. Biol. Chem. 260:13384-13388(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Extrahepetic transcription of human C-reactive protein."
Murphy T.M., Baum L., Beaman K.
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]Tenchini M.L., Marchetti L., Bossi E., Malcovati M., Lorenzetti R.
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[5]"Controlled gene expression using acute phase response elements."
Harraghy N.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Urinary bladder.
[7]SeattleSNPs variation discovery resource
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"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. expand/collapse author list , 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].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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] (ISOFORMS 1 AND 2).
Tissue: Liver.
[11]"Biosynthesis and postsynthetic processing of human C-reactive protein."
Tucci A., Goldberger G., Whitehead A.S., Kay R.M., Woods D.E., Colten H.R.
J. Immunol. 131:2416-2419(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-26.
[12]"Isolation of human C-reactive protein complementary DNA and localization of the gene to chromosome 1."
Whitehead A.S., Bruns G.A.P., Markham A.F., Colten H.R., Woods D.E.
Science 221:69-71(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-175.
[13]"Primary structure of human C-reactive protein."
Oliveira E.B., Gotschlich E.C., Liu T.-Y.
J. Biol. Chem. 254:489-502(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-224, PYROGLUTAMATE FORMATION AT GLN-19.
[14]"Partial amino-acid sequences of human and rabbit C-reactive proteins: homology with immunoglobulins and histocompatibility antigens."
Osmand A.P., Gewurz H., Friedenson B.
Proc. Natl. Acad. Sci. U.S.A. 74:1214-1218(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-55.
[15]"Selected expression profiling of full-length proteins and their variants in human plasma."
Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W.
Clin. Proteomics 1:7-16(2004)
Cited for: MASS SPECTROMETRY.
[16]"Comparative analyses of pentraxins: implications for protomer assembly and ligand binding."
Srinivasan N., White H.E., Emsley J., Wood S.P., Pepys M.B., Blundell T.L.
Structure 2:1017-1027(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[17]"Three dimensional structure of human C-reactive protein."
Shrive A.K., Cheetham G.M.T., Holden D., Myles D.A.A., Turnell W.G., Volanakis J.E., Pepys M.B., Bloomer A.C., Greenhough T.J.
Nat. Struct. Biol. 3:346-353(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[18]"The physiological structure of human C-reactive protein and its complex with phosphocholine."
Thompson D., Pepys M.B., Wood S.P.
Structure 7:169-177(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Wikipedia

C-reactive protein entry

SeattleSNPs
Protein Spotlight

No more Christmas pudding? - Issue 30 of January 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11880 Genomic DNA. Translation: AAB59526.1.
M11725 Genomic DNA. Translation: AAA52075.1.
X56692 mRNA. Translation: CAA40020.1.
X56214 mRNA. Translation: CAA39671.1.
AF442818 Genomic DNA. Translation: AAL48218.2.
AK289443 mRNA. Translation: BAF82132.1.
AF449713 Genomic DNA. Translation: AAL40835.1.
AL445528 Genomic DNA. Translation: CAH73654.1.
AL445528 Genomic DNA. Translation: CAH73656.1.
CH471121 Genomic DNA. Translation: EAW52778.1.
CH471121 Genomic DNA. Translation: EAW52779.1.
CH471121 Genomic DNA. Translation: EAW52780.1.
BC020766 mRNA. Translation: AAH20766.1.
BC125135 mRNA. Translation: AAI25136.1.
M35163 mRNA. Translation: AAA52076.1.
K00518 mRNA. Translation: AAA52074.1.
CCDSCCDS30911.1. [P02741-1]
PIRCJHU. A24515.
RefSeqNP_000558.2. NM_000567.2. [P02741-1]
UniGeneHs.709456.
Hs.76452.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B09X-ray2.50A/B/C/D/E19-224[»]
1CRVmodel-A/B/C/D/E19-224[»]
1GNHX-ray3.00A/B/C/D/E/F/G/H/I/J19-224[»]
1LJ7X-ray3.15A/B/C/D/E/F/G/H/I/J19-224[»]
3L2YX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T19-224[»]
3PVNX-ray1.98A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T19-224[»]
3PVOX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T19-224[»]
ProteinModelPortalP02741.
SMRP02741. Positions 19-224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107791. 13 interactions.
DIPDIP-39125N.
IntActP02741. 9 interactions.
MINTMINT-1206167.
STRING9606.ENSP00000255030.

Chemistry

DrugBankDB01076. Atorvastatin.
DB01393. Bezafibrate.

PTM databases

PhosphoSiteP02741.

Polymorphism databases

DMDM117486.

2D gel databases

DOSAC-COBS-2DPAGEP02741.
SWISS-2DPAGEP02741.

Proteomic databases

PaxDbP02741.
PeptideAtlasP02741.
PRIDEP02741.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255030; ENSP00000255030; ENSG00000132693. [P02741-1]
ENST00000368112; ENSP00000357093; ENSG00000132693. [P02741-2]
GeneID1401.
KEGGhsa:1401.
UCSCuc001ftw.3. human. [P02741-1]
uc001ftx.1. human. [P02741-2]

Organism-specific databases

CTD1401.
GeneCardsGC01M159682.
H-InvDBHIX0028720.
HGNCHGNC:2367. CRP.
HPACAB005036.
HPA027367.
HPA027396.
MIM123260. gene.
neXtProtNX_P02741.
PharmGKBPA120.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG113288.
HOGENOMHOG000247043.
HOVERGENHBG005405.
InParanoidP02741.
KOK16143.
OMAWRALKYE.
OrthoDBEOG71RXMB.
PhylomeDBP02741.
TreeFamTF330208.

Gene expression databases

ArrayExpressP02741.
BgeeP02741.
CleanExHS_CRP.
GenevestigatorP02741.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001759. Pentaxin.
[Graphical view]
PfamPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSPR00895. PENTAXIN.
SMARTSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00289. PENTAXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCRP. human.
EvolutionaryTraceP02741.
GeneWikiC-reactive_protein.
GenomeRNAi1401.
NextBio5737.
PROP02741.
SOURCESearch...

Entry information

Entry nameCRP_HUMAN
AccessionPrimary (citable) accession number: P02741
Secondary accession number(s): A8K078 expand/collapse secondary AC list , D3DVD9, D3DVE0, Q08AK3, Q8WW75
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: July 9, 2014
This is version 176 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM