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P05156 (CFAI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement factor I

EC=3.4.21.45
Alternative name(s):
C3B/C4B inactivator
Gene names
Name:CFI
Synonyms:IF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for cleaving the alpha-chains of C4b and C3b in the presence of the cofactors C4-binding protein and factor H respectively.

Catalytic activity

Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage.

Subunit structure

Heterodimer of a light and heavy chains; disulfide-linked. The fully processed and mature protein circulates as a zymogen, and is allosterically activated by substrate-induced remodeling of the active site. Ref.11

Subcellular location

Secretedextracellular space.

Tissue specificity

Plasma.

Involvement in disease

Hemolytic uremic syndrome atypical 3 (AHUS3) [MIM:612923]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype. Ref.14 Ref.15 Ref.17 Ref.18

Complement factor I deficiency (CFI deficiency) [MIM:610984]: Autosomal recessive condition associated with a propensity to pyogenic infections.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Macular degeneration, age-related, 13 (ARMD13) [MIM:615439]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.19

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 Kazal-like domain.

Contains 2 LDL-receptor class A domains.

Contains 1 peptidase S1 domain.

Contains 1 SRCR domain.

Sequence caution

The sequence CAA68416.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 583565Complement factor I
PRO_0000027568
Chain19 – 335317Complement factor I heavy chain
PRO_0000027569
Chain340 – 583244Complement factor I light chain
PRO_0000027570

Regions

Domain55 – 10854Kazal-like
Domain114 – 21299SRCR
Domain213 – 25745LDL-receptor class A 1
Domain258 – 29437LDL-receptor class A 2
Domain340 – 574235Peptidase S1
Calcium binding239 – 253151 Ref.11
Calcium binding276 – 290152 Ref.11

Sites

Active site3801Charge relay system By similarity
Active site4291Charge relay system By similarity
Active site5251Charge relay system By similarity

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) Ref.7
Glycosylation1031N-linked (GlcNAc...) (complex) Ref.7 Ref.8 Ref.9 Ref.10
Glycosylation1771N-linked (GlcNAc...) Ref.7
Glycosylation4641N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation4941N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Ref.7
Disulfide bond33 ↔ 255 Ref.11
Disulfide bond43 ↔ 54 Ref.11
Disulfide bond48 ↔ 59 Ref.11
Disulfide bond61 ↔ 93 Ref.11
Disulfide bond67 ↔ 86 Ref.11
Disulfide bond75 ↔ 106 Ref.11
Disulfide bond141 ↔ 181 Ref.11
Disulfide bond154 ↔ 214 Ref.11
Disulfide bond186 ↔ 196 Ref.11
Disulfide bond229 ↔ 247 Ref.11
Disulfide bond259 ↔ 271 Ref.11
Disulfide bond266 ↔ 284 Ref.11
Disulfide bond278 ↔ 293 Ref.11
Disulfide bond327 ↔ 453Interchain (between heavy and light chains) Ref.11
Disulfide bond365 ↔ 381 Ref.11
Disulfide bond373 ↔ 444 Ref.11
Disulfide bond467 ↔ 531 Ref.11
Disulfide bond495 ↔ 510 Ref.11
Disulfide bond521 ↔ 550 Ref.11

Natural variations

Natural variant641P → L in AHUS3. Ref.18
VAR_063665
Natural variant1191G → R in AHUS3 and ARMD13; the mutant is both expressed and secreted at lower levels than wild-type protein; mediates C3 degradation to a lesser extent than that of controls. Ref.18 Ref.19
VAR_063666
Natural variant1831H → R in AHUS3. Ref.18
Corresponds to variant rs75612300 [ dbSNP | Ensembl ].
VAR_063667
Natural variant1881G → A. Ref.19
VAR_070843
Natural variant2431G → D in CFI deficiency. Ref.16
VAR_034907
Natural variant2871G → R in AHUS3. Ref.18
Corresponds to variant rs182078921 [ dbSNP | Ensembl ].
VAR_063668
Natural variant3001T → A. Ref.1 Ref.2
Corresponds to variant rs11098044 [ dbSNP | Ensembl ].
VAR_034908
Natural variant3171R → W in AHUS3. Ref.15
VAR_063669
Natural variant3401I → T in AHUS3. Ref.17
VAR_030343
Natural variant4161I → L in AHUS3. Ref.18
Corresponds to variant rs61733901 [ dbSNP | Ensembl ].
VAR_063670
Natural variant4181H → L in CFI deficiency. Ref.12
VAR_026757
Natural variant5191D → N in AHUS3. Ref.15
VAR_063671
Natural variant5221K → T in AHUS3. Ref.18
VAR_063672
Natural variant5241D → V in AHUS3. Ref.14
VAR_030344

Experimental info

Sequence conflict5581V → F in AAA52455. Ref.2

Secondary structure

........................................................................................... 583
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05156 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: F06070EFE6B572A1

FASTA58365,750
        10         20         30         40         50         60 
MKLLHVFLLF LCFHLRFCKV TYTSQEDLVE KKCLAKKYTH LSCDKVFCQP WQRCIEGTCV 

        70         80         90        100        110        120 
CKLPYQCPKN GTAVCATNRR SFPTYCQQKS LECLHPGTKF LNNGTCTAEG KFSVSLKHGN 

       130        140        150        160        170        180 
TDSEGIVEVK LVDQDKTMFI CKSSWSMREA NVACLDLGFQ QGADTQRRFK LSDLSINSTE 

       190        200        210        220        230        240 
CLHVHCRGLE TSLAECTFTK RRTMGYQDFA DVVCYTQKAD SPMDDFFQCV NGKYISQMKA 

       250        260        270        280        290        300 
CDGINDCGDQ SDELCCKACQ GKGFHCKSGV CIPSQYQCNG EVDCITGEDE VGCAGFASVT 

       310        320        330        340        350        360 
QEETEILTAD MDAERRRIKS LLPKLSCGVK NRMHIRRKRI VGGKRAQLGD LPWQVAIKDA 

       370        380        390        400        410        420 
SGITCGGIYI GGCWILTAAH CLRASKTHRY QIWTTVVDWI HPDLKRIVIE YVDRIIFHEN 

       430        440        450        460        470        480 
YNAGTYQNDI ALIEMKKDGN KKDCELPRSI PACVPWSPYL FQPNDTCIVS GWGREKDNER 

       490        500        510        520        530        540 
VFSLQWGEVK LISNCSKFYG NRFYEKEMEC AGTYDGSIDA CKGDSGGPLV CMDANNVTYV 

       550        560        570        580 
WGVVSWGENC GKPEFPGVYT KVANYFDWIS YHVGRPFISQ YNV 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones."
Catterall C.F., Lyons A., Sim R.M., Day A.J., Harris T.J.R.
Biochem. J. 242:849-856(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-300.
Tissue: Liver.
[2]"Human complement factor I: analysis of cDNA-derived primary structure and assignment of its gene to chromosome 4."
Goldberger G., Bruns G.A.P., Rits M., Edge M.D., Kwiatkowski D.J.
J. Biol. Chem. 262:10065-10071(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-300.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Cloning and characterization of the promoter for the human complement factor I (C3b/C4b inactivator) gene."
Minta J.O., Fung M., Turner S., Eren R., Zemach L., Rits M., Goldberger G.
Gene 208:17-24(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
Tissue: Liver.
[5]"Beta-sheet secondary structure of an LDL receptor domain from complement factor I by consensus structure predictions and spectroscopy."
Ullman C.G., Haris P.I., Smith K.F., Sim R.B., Emery V.C., Perkins S.J.
FEBS Lett. 371:199-203(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 258-269.
[6]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464.
Tissue: Plasma.
[7]"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-70; ASN-103; ASN-177; ASN-464 AND ASN-536.
Tissue: Plasma.
[8]"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-103.
Tissue: Liver.
[9]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-103.
[10]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[11]"Structural basis for complement factor I control and its disease-associated sequence polymorphisms."
Roversi P., Johnson S., Caesar J.J., McLean F., Leath K.J., Tsiftsoglou S.A., Morgan B.P., Harris C.L., Sim R.B., Lea S.M.
Proc. Natl. Acad. Sci. U.S.A. 108:12839-12844(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 19-583, CALCIUM-BINDING, SUBUNIT, DISULFIDE BONDS.
[12]"The molecular basis of hereditary complement factor I deficiency."
Vyse T.J., Morley B.J., Bartok I., Theodoridis E.L., Davies K.A., Webster A.D.B., Walport M.J.
J. Clin. Invest. 97:925-933(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CFI DEFICIENCY LEU-418.
[13]"Molecular characterization of homozygous hereditary factor I deficiency."
Baracho G.V., Nudelman V., Isaac L.
Clin. Exp. Immunol. 131:280-286(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CFI DEFICIENCY.
[14]"Complement factor I: a susceptibility gene for atypical haemolytic uraemic syndrome."
Fremeaux-Bacchi V., Dragon-Durey M.-A., Blouin J., Vigneau C., Kuypers D., Boudailliez B., Loirat C., Rondeau E., Fridman W.H.
J. Med. Genet. 41:E84-E84(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AHUS3 VAL-524.
[15]"Genetics of HUS: the impact of MCP, CFH, and IF mutations on clinical presentation, response to treatment, and outcome."
The international registry of recurrent and familial HUS/TTP
Caprioli J., Noris M., Brioschi S., Pianetti G., Castelletti F., Bettinaglio P., Mele C., Bresin E., Cassis L., Gamba S., Porrati F., Bucchioni S., Monteferrante G., Fang C.J., Liszewski M.K., Kavanagh D., Atkinson J.P., Remuzzi G.
Blood 108:1267-1279(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AHUS3 TRP-317 AND ASN-519.
[16]"Primary glomerulonephritis with isolated C3 deposits: a new entity which shares common genetic risk factors with haemolytic uraemic syndrome."
Servais A., Fremeaux-Bacchi V., Lequintrec M., Salomon R., Blouin J., Knebelmann B., Gruenfeld J.-P., Lesavre P., Noeel L.-H., Fakhouri F.
J. Med. Genet. 44:193-199(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CFI DEFICIENCY ASP-243.
[17]"A missense mutation in factor I (IF) predisposes to atypical haemolytic uraemic syndrome."
Geelen J., van den Dries K., Roos A., van de Kar N., de Kat Angelino C., Klasen I., Monnens L., van den Heuvel L.
Pediatr. Nephrol. 22:371-375(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AHUS3 THR-340.
[18]"Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome."
Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.
Hum. Mutat. 31:E1445-E1460(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AHUS3 LEU-64; ARG-119; ARG-183; ARG-287; LEU-416 AND THR-522.
[19]"A functional variant in the CFI gene confers a high risk of age-related macular degeneration."
van de Ven J.P., Nilsson S.C., Tan P.L., Buitendijk G.H., Ristau T., Mohlin F.C., Nabuurs S.B., Schoenmaker-Koller F.E., Smailhodzic D., Campochiaro P.A., Zack D.J., Duvvari M.R., Bakker B., Paun C.C., Boon C.J., Uitterlinden A.G., Liakopoulos S., Klevering B.J. expand/collapse author list , Fauser S., Daha M.R., Katsanis N., Klaver C.C., Blom A.M., Hoyng C.B., den Hollander A.I.
Nat. Genet. 45:813-817(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARMD13 ARG-119, VARIANT ALA-188, CHARACTERIZATION VARIANT ARMD13 ARG-119.
+Additional computationally mapped references.

Web resources

CFIbase

CFI mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00318 mRNA. Translation: CAA68416.1. Different initiation.
J02770 mRNA. Translation: AAA52455.1.
AC126283 Genomic DNA. No translation available.
AF005095 Genomic DNA. Translation: AAC08733.2.
PIRA29154.
RefSeqNP_000195.2. NM_000204.3.
UniGeneHs.312485.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XRCX-ray2.69A/B/C/D19-583[»]
ProteinModelPortalP05156.
SMRP05156. Positions 27-583.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109652. 2 interactions.
STRING9606.ENSP00000378130.

Protein family/group databases

MEROPSS01.199.

PTM databases

PhosphoSiteP05156.

Polymorphism databases

DMDM317373341.

2D gel databases

SWISS-2DPAGEP05156.

Proteomic databases

PaxDbP05156.
PeptideAtlasP05156.
PRIDEP05156.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394634; ENSP00000378130; ENSG00000205403.
GeneID3426.
KEGGhsa:3426.
UCSCuc003hzq.3. human.

Organism-specific databases

CTD3426.
GeneCardsGC04M110661.
HGNCHGNC:5394. CFI.
HPACAB016777.
HPA001143.
HPA024061.
MIM217030. gene.
610984. phenotype.
612923. phenotype.
615439. phenotype.
neXtProtNX_P05156.
Orphanet279. Age-related macular degeneration.
93580. Atypical hemolytic uremic syndrome with I factor anomaly.
244275. De novo thrombotic microangiopathy after kidney transplantation.
244242. HELLP syndrome.
200418. Immunodeficiency with factor I anomaly.
PharmGKBPA29641.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000060288.
HOVERGENHBG005311.
KOK01333.
PhylomeDBP05156.
TreeFamTF330647.

Enzyme and pathway databases

BRENDA3.4.21.45. 2681.
ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP05156.
BgeeP05156.
CleanExHS_CFI.
GenevestigatorP05156.

Family and domain databases

Gene3D3.10.250.10. 1 hit.
4.10.400.10. 2 hits.
InterProIPR003884. FacI_MAC.
IPR002350. Kazal_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00057. Ldl_recept_a. 2 hits.
PF00530. SRCR. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00057. FIMAC. 1 hit.
SM00192. LDLa. 2 hits.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 2 hits.
PROSITEPS51465. KAZAL_2. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 2 hits.
PS50287. SRCR_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05156.
GeneWikiComplement_factor_I.
GenomeRNAi3426.
NextBio13512.
PROP05156.
SOURCESearch...

Entry information

Entry nameCFAI_HUMAN
AccessionPrimary (citable) accession number: P05156
Secondary accession number(s): O60442
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 159 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

Peptidase families

Classification of peptidase families and list of 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 4

Human chromosome 4: entries, gene names and cross-references to MIM