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P99999 (CYC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c
Gene names
Name:CYCS
Synonyms:CYC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length105 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.

Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.

Subcellular location

Mitochondrion intermembrane space. Note: Loosely associated with the inner membrane.

Post-translational modification

Binds 1 heme group per subunit.

Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration By similarity.

Involvement in disease

Thrombocytopenia 4 (THC4) [MIM:612004]: Thrombocytopenia is defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

Sequence similarities

Belongs to the cytochrome c family.

Ontologies

Keywords
   Biological processApoptosis
Electron transport
Respiratory chain
Transport
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandHeme
Iron
Metal-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c

Traceable author statement PubMed 9267021. Source: UniProtKB

apoptotic DNA fragmentation

Inferred from mutant phenotype PubMed 8689682. Source: UniProtKB

apoptotic process

Traceable author statement. Source: Reactome

cellular metabolic process

Traceable author statement. Source: Reactome

cellular respiration

Traceable author statement PubMed 10383829. Source: UniProtKB

dephosphorylation

Traceable author statement PubMed 8206937. Source: GOC

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

respiratory electron transport chain

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from mutant phenotype PubMed 8689682. Source: UniProtKB

mitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrial intermembrane space

Traceable author statement PubMed 8689682. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

nucleus

Inferred from direct assay. Source: LIFEdb

protein phosphatase type 2A complex

Traceable author statement PubMed 8206937. Source: UniProtKB

respiratory chain

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionelectron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity

Inferred from direct assay PubMed 8689682. Source: UniProtKB

heme binding

Traceable author statement Ref.11. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 9267021. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APAF1O147276EBI-446479,EBI-446492

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9 Ref.10
Chain2 – 105104Cytochrome c
PRO_0000108218

Sites

Metal binding191Iron (heme axial ligand)
Metal binding811Iron (heme axial ligand)
Binding site151Heme (covalent)
Binding site181Heme (covalent)

Amino acid modifications

Modified residue21N-acetylglycine Ref.9
Modified residue491Phosphotyrosine By similarity
Modified residue981Phosphotyrosine By similarity

Natural variations

Natural variant421G → S in THC4; increases the pro-apoptotic function by triggering caspase activation more efficiently than wild-type; does not affect the redox function. Ref.15
VAR_044450
Natural variant561K → R.
Corresponds to variant rs11548795 [ dbSNP | Ensembl ].
VAR_048850
Natural variant661M → L in 10% of the molecules.
VAR_002204

Experimental info

Sequence conflict181C → Y in AAH15130. Ref.8
Sequence conflict411T → I in AAH68464. Ref.8

Secondary structure

.................. 105
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P99999 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8EE9689E0102506B

FASTA10511,749
        10         20         30         40         50         60 
MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGIIW 

        70         80         90        100 
GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE 

« Hide

References

« Hide 'large scale' references
[1]"The human somatic cytochrome c gene: two classes of processed pseudogenes demarcate a period of rapid molecular evolution."
Evans M.J., Scarpulla R.C.
Proc. Natl. Acad. Sci. U.S.A. 85:9625-9629(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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].
[3]"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].
Tissue: Cerebellum.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala.
[5]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Bone marrow, Brain, Kidney, Lung, Skeletal muscle, Skin, Testis and Urinary bladder.
[9]"The amino acid sequence of human heart cytochrome c."
Matsubara H., Smith E.L.
J. Biol. Chem. 237:3575-3576(1962) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-105, ACETYLATION AT GLY-2.
Tissue: Heart.
[10]"Human heart cytochrome c. Chymotryptic peptides, tryptic peptides, and the complete amino acid sequence."
Matsubara H., Smith E.L.
J. Biol. Chem. 238:2732-2753(1963) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-105.
Tissue: Heart.
[11]"Cytochrome c in the apoptotic and antioxidant cascades."
Skulachev V.P.
FEBS Lett. 423:275-280(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN APOPTOSIS.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Solution structure of reduced recombinant human cytochrome c."
Jeng W.-Y., Shiu J.-H., Tsai Y.-H., Chuang W.-J.
Submitted (FEB-2003) to the PDB data bank
Cited for: STRUCTURE BY NMR.
[15]"A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia."
Morison I.M., Cramer Borde E.M.C., Cheesman E.J., Cheong P.L., Holyoake A.J., Fichelson S., Weeks R.J., Lo A., Davies S.M.K., Wilbanks S.M., Fagerlund R.D., Ludgate M.W., da Silva Tatley F.M., Coker M.S.A., Bockett N.A., Hughes G., Pippig D.A., Smith M.P., Capron C., Ledgerwood E.C.
Nat. Genet. 40:387-389(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THC4 SER-42, IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF VARIANT THC4 SER-42, X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF VARIANT THC4 SER-42 AND WILD TYPE.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Protein Spotlight

An unexpected place - Issue 88 of November 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22877 Genomic DNA. Translation: AAA35732.1.
BT006946 mRNA. Translation: AAP35592.1.
AK311836 mRNA. Translation: BAG34778.1.
AL713681 mRNA. Translation: CAD28485.1.
AC007487 Genomic DNA. Translation: AAQ96844.1.
CH236948 Genomic DNA. Translation: EAL24239.1.
CH471073 Genomic DNA. Translation: EAW93822.1.
BC005299 mRNA. Translation: AAH05299.1.
BC008475 mRNA. Translation: AAH08475.1.
BC008477 mRNA. Translation: AAH08477.1.
BC009578 mRNA. Translation: AAH09578.1.
BC009579 mRNA. Translation: AAH09579.1.
BC009582 mRNA. Translation: AAH09582.1.
BC009587 mRNA. Translation: AAH09587.1.
BC009602 mRNA. Translation: AAH09602.1.
BC009607 mRNA. Translation: AAH09607.1.
BC014359 mRNA. Translation: AAH14359.1.
BC014361 mRNA. Translation: AAH14361.1.
BC015130 mRNA. Translation: AAH15130.1.
BC016006 mRNA. Translation: AAH16006.1.
BC021994 mRNA. Translation: AAH21994.1.
BC022330 mRNA. Translation: AAH22330.1.
BC067222 mRNA. Translation: AAH67222.1.
BC068464 mRNA. Translation: AAH68464.1.
BC070156 mRNA. Translation: AAH70156.1.
BC070346 mRNA. Translation: AAH70346.1.
BC071761 mRNA. Translation: AAH71761.1.
CCDSCCDS5393.1.
PIRCCHU. A31764.
RefSeqNP_061820.1. NM_018947.5.
UniGeneHs.437060.
Hs.617193.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J3SNMR-A2-105[»]
3NWVX-ray1.90A/B/C/D2-105[»]
3ZCFX-ray1.65A/B/C/D2-105[»]
3ZOOX-ray1.35A/B/C/D2-105[»]
ProteinModelPortalP99999.
SMRP99999. Positions 2-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119922. 21 interactions.
DIPDIP-29683N.
IntActP99999. 7 interactions.
MINTMINT-3023956.
STRING9606.ENSP00000307786.

Chemistry

DrugBankDB01065. Melatonin.
DB01017. Minocycline.

PTM databases

PhosphoSiteP99999.

Polymorphism databases

DMDM42560196.

Proteomic databases

MaxQBP99999.
PaxDbP99999.
PeptideAtlasP99999.
PRIDEP99999.

Protocols and materials databases

DNASU54205.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305786; ENSP00000307786; ENSG00000172115.
ENST00000409409; ENSP00000386270; ENSG00000172115.
ENST00000409764; ENSP00000387279; ENSG00000172115.
GeneID54205.
KEGGhsa:54205.
UCSCuc003sxl.3. human.

Organism-specific databases

CTD54205.
GeneCardsGC07M025158.
HGNCHGNC:19986. CYCS.
HPACAB004222.
CAB005126.
CAB018597.
MIM123970. gene.
612004. phenotype.
neXtProtNX_P99999.
Orphanet168629. Autosomal thrombocytopenia with normal platelets.
PharmGKBPA134981636.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3474.
HOGENOMHOG000009762.
HOVERGENHBG003023.
InParanoidP99999.
KOK08738.
OMACHNLKEG.
OrthoDBEOG761BWX.
PhylomeDBP99999.
TreeFamTF300226.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_120956. Cellular responses to stress.
REACT_200751. Organelle biogenesis and maintenance.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressP99999.
BgeeP99999.
CleanExHS_CYCS.
GenevestigatorP99999.

Family and domain databases

Gene3D1.10.760.10. 1 hit.
InterProIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
IPR003088. Cyt_c_dom.
[Graphical view]
PANTHERPTHR11961. PTHR11961. 1 hit.
PfamPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSPR00604. CYTCHRMECIAB.
SUPFAMSSF46626. SSF46626. 1 hit.
PROSITEPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCYCS. human.
EvolutionaryTraceP99999.
GeneWikiCytochrome_c.
GenomeRNAi54205.
NextBio56526.
PROP99999.
SOURCESearch...

Entry information

Entry nameCYC_HUMAN
AccessionPrimary (citable) accession number: P99999
Secondary accession number(s): A4D166 expand/collapse secondary AC list , B2R4I1, P00001, Q6NUR2, Q6NX69, Q96BV4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 126 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM