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P00746

- CFAD_HUMAN

UniProt

P00746 - CFAD_HUMAN

Protein

Complement factor D

Gene

CFD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 5 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.

    Catalytic activityi

    Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei66 – 661Charge relay system
    Active sitei114 – 1141Charge relay system
    Active sitei208 – 2081Charge relay system

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: ProtInc
    2. serine-type peptidase activity Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. complement activation Source: Reactome
    3. complement activation, alternative pathway Source: Reactome
    4. innate immune response Source: Reactome
    5. platelet activation Source: Reactome
    6. platelet degranulation Source: Reactome
    7. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Complement alternate pathway, Immunity, Innate immunity

    Enzyme and pathway databases

    BRENDAi3.4.21.46. 2681.
    ReactomeiREACT_8001. Alternative complement activation.

    Protein family/group databases

    MEROPSiS01.191.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement factor D (EC:3.4.21.46)
    Alternative name(s):
    Adipsin
    C3 convertase activator
    Properdin factor D
    Gene namesi
    Name:CFD
    Synonyms:DF, PFD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2771. CFD.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Complement factor D deficiency (CFDD) [MIM:613912]: An immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti213 – 2131V → G in CFDD. 1 Publication
    VAR_034866
    Natural varianti214 – 2141C → R in CFDD. 1 Publication
    VAR_034867

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi613912. phenotype.
    Orphaneti169467. Recurrent Neisseria infections due to factor D deficiency.
    PharmGKBiPA142.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 255Activation peptideSequence AnalysisPRO_0000027560
    Chaini26 – 253228Complement factor DPRO_0000027561Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi51 ↔ 67
    Disulfide bondi148 ↔ 214
    Disulfide bondi179 ↔ 195
    Disulfide bondi204 ↔ 229

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiP00746.
    PRIDEiP00746.

    PTM databases

    PhosphoSiteiP00746.

    Expressioni

    Gene expression databases

    ArrayExpressiP00746.
    BgeeiP00746.
    CleanExiHS_CFD.
    GenevestigatoriP00746.

    Organism-specific databases

    HPAiCAB016383.

    Interactioni

    Protein-protein interaction databases

    BioGridi108039. 3 interactions.
    IntActiP00746. 2 interactions.
    STRINGi9606.ENSP00000332139.

    Structurei

    Secondary structure

    1
    253
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 323
    Beta strandi40 – 456
    Beta strandi48 – 5710
    Beta strandi60 – 634
    Helixi65 – 684
    Beta strandi72 – 743
    Beta strandi76 – 816
    Beta strandi83 – 875
    Beta strandi93 – 10210
    Helixi108 – 1136
    Beta strandi116 – 1227
    Beta strandi127 – 1293
    Beta strandi147 – 1548
    Turni156 – 1594
    Beta strandi167 – 1748
    Helixi176 – 1794
    Turni182 – 1876
    Beta strandi193 – 1964
    Beta strandi200 – 2023
    Turni205 – 2095
    Beta strandi211 – 2144
    Beta strandi217 – 2226
    Beta strandi226 – 2283
    Beta strandi231 – 2333
    Beta strandi236 – 2405
    Helixi241 – 2444
    Helixi245 – 2528

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BIOX-ray1.50A26-253[»]
    1DFPX-ray2.40A/B26-253[»]
    1DICX-ray1.80A26-253[»]
    1DSTX-ray2.00A26-253[»]
    1DSUX-ray2.00A/B26-253[»]
    1FDPX-ray2.10A/B/C/D19-253[»]
    1HFDX-ray2.30A26-253[»]
    2XW9X-ray1.20A26-253[»]
    2XWAX-ray2.80A/B26-253[»]
    2XWBX-ray3.49I/J26-253[»]
    4CBNX-ray1.80A/B26-253[»]
    4CBOX-ray1.80A/B26-253[»]
    4D9RX-ray2.42A/B26-253[»]
    ProteinModelPortaliP00746.
    SMRiP00746. Positions 26-253.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00746.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 253228Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOVERGENiHBG013304.
    InParanoidiP00746.
    KOiK01334.
    OrthoDBiEOG7MKW6Q.
    PhylomeDBiP00746.
    TreeFamiTF333630.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00746-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHSWERLAVL VLLGAAACAA PPRGRILGGR EAEAHARPYM ASVQLNGAHL    50
    CGGVLVAEQW VLSAAHCLED AADGKVQVLL GAHSLSQPEP SKRLYDVLRA 100
    VPHPDSQPDT IDHDLLLLQL SEKATLGPAV RPLPWQRVDR DVAPGTLCDV 150
    AGWGIVNHAG RRPDSLQHVL LPVLDRATCN RRTHHDGAIT ERLMCAESNR 200
    RDSCKGDSGG PLVCGGVLEG VVTSGSRVCG NRKKPGIYTR VASYAAWIDS 250
    VLA 253
    Length:253
    Mass (Da):27,033
    Last modified:September 11, 2007 - v5
    Checksum:i78B06C209DEEA362
    GO

    Sequence cautioni

    The sequence AAA35527.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211P → R in AAA35527. (PubMed:1374388)Curated
    Sequence conflicti26 – 261I → M in AAA35527. (PubMed:1374388)Curated
    Sequence conflicti35 – 351H → F AA sequence (PubMed:6987665)Curated
    Sequence conflicti40 – 401M → V AA sequence (PubMed:6987665)Curated
    Sequence conflicti49 – 491H → E AA sequence (PubMed:6363133)Curated
    Sequence conflicti49 – 491H → E AA sequence (PubMed:6821372)Curated
    Sequence conflicti52 – 521G → A in AAA35527. (PubMed:1374388)Curated
    Sequence conflicti59 – 591Q → R in AAA35527. (PubMed:1374388)Curated
    Sequence conflicti63 – 631S → T AA sequence (PubMed:6363133)Curated
    Sequence conflicti73 – 731D → G AA sequence (PubMed:6363133)Curated
    Sequence conflicti83 – 864HSLS → THLP AA sequence (PubMed:6383466)Curated
    Sequence conflicti83 – 842HS → ST AA sequence (PubMed:6363133)Curated
    Sequence conflicti94 – 952Missing AA sequence (PubMed:6363133)Curated
    Sequence conflicti96 – 961D → E AA sequence (PubMed:6363133)Curated
    Sequence conflicti136 – 1361Q → G AA sequence (PubMed:6363133)Curated
    Sequence conflicti178 – 19114TCNRR…GAITE → KCRLYDVL AA sequence (PubMed:6363133)CuratedAdd
    BLAST
    Sequence conflicti243 – 2431S → T AA sequence (PubMed:6383466)Curated
    Sequence conflicti250 – 2501S → H AA sequence (PubMed:6383466)Curated
    Sequence conflicti250 – 2501Missing AA sequence (PubMed:6363133)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti213 – 2131V → G in CFDD. 1 Publication
    VAR_034866
    Natural varianti214 – 2141C → R in CFDD. 1 Publication
    VAR_034867
    Natural varianti248 – 2481I → M.
    Corresponds to variant rs2230216 [ dbSNP | Ensembl ].
    VAR_034868

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ313463 mRNA. Translation: CAC48304.1.
    AK300963 mRNA. Translation: BAG62588.1.
    CH471139 Genomic DNA. Translation: EAW69588.1.
    BC034529 mRNA. Translation: AAH34529.1.
    BC040146 mRNA. Translation: AAH40146.1.
    BC051001 mRNA. Translation: AAH51001.1.
    BC057807 mRNA. Translation: AAH57807.1.
    M84526 mRNA. Translation: AAA35527.1. Different initiation.
    CCDSiCCDS12046.1.
    PIRiA40197. DBHU.
    RefSeqiNP_001919.2. NM_001928.2.
    UniGeneiHs.155597.

    Genome annotation databases

    EnsembliENST00000327726; ENSP00000332139; ENSG00000197766.
    GeneIDi1675.
    KEGGihsa:1675.
    UCSCiuc002lqc.3. human.

    Polymorphism databases

    DMDMi158515408.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    CFDbase

    CFD mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ313463 mRNA. Translation: CAC48304.1 .
    AK300963 mRNA. Translation: BAG62588.1 .
    CH471139 Genomic DNA. Translation: EAW69588.1 .
    BC034529 mRNA. Translation: AAH34529.1 .
    BC040146 mRNA. Translation: AAH40146.1 .
    BC051001 mRNA. Translation: AAH51001.1 .
    BC057807 mRNA. Translation: AAH57807.1 .
    M84526 mRNA. Translation: AAA35527.1 . Different initiation.
    CCDSi CCDS12046.1.
    PIRi A40197. DBHU.
    RefSeqi NP_001919.2. NM_001928.2.
    UniGenei Hs.155597.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BIO X-ray 1.50 A 26-253 [» ]
    1DFP X-ray 2.40 A/B 26-253 [» ]
    1DIC X-ray 1.80 A 26-253 [» ]
    1DST X-ray 2.00 A 26-253 [» ]
    1DSU X-ray 2.00 A/B 26-253 [» ]
    1FDP X-ray 2.10 A/B/C/D 19-253 [» ]
    1HFD X-ray 2.30 A 26-253 [» ]
    2XW9 X-ray 1.20 A 26-253 [» ]
    2XWA X-ray 2.80 A/B 26-253 [» ]
    2XWB X-ray 3.49 I/J 26-253 [» ]
    4CBN X-ray 1.80 A/B 26-253 [» ]
    4CBO X-ray 1.80 A/B 26-253 [» ]
    4D9R X-ray 2.42 A/B 26-253 [» ]
    ProteinModelPortali P00746.
    SMRi P00746. Positions 26-253.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108039. 3 interactions.
    IntActi P00746. 2 interactions.
    STRINGi 9606.ENSP00000332139.

    Chemistry

    ChEMBLi CHEMBL2176771.

    Protein family/group databases

    MEROPSi S01.191.

    PTM databases

    PhosphoSitei P00746.

    Polymorphism databases

    DMDMi 158515408.

    Proteomic databases

    PaxDbi P00746.
    PRIDEi P00746.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327726 ; ENSP00000332139 ; ENSG00000197766 .
    GeneIDi 1675.
    KEGGi hsa:1675.
    UCSCi uc002lqc.3. human.

    Organism-specific databases

    CTDi 1675.
    GeneCardsi GC19P000859.
    HGNCi HGNC:2771. CFD.
    HPAi CAB016383.
    MIMi 134350. gene.
    613912. phenotype.
    neXtProti NX_P00746.
    Orphaneti 169467. Recurrent Neisseria infections due to factor D deficiency.
    PharmGKBi PA142.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG013304.
    InParanoidi P00746.
    KOi K01334.
    OrthoDBi EOG7MKW6Q.
    PhylomeDBi P00746.
    TreeFami TF333630.

    Enzyme and pathway databases

    BRENDAi 3.4.21.46. 2681.
    Reactomei REACT_8001. Alternative complement activation.

    Miscellaneous databases

    EvolutionaryTracei P00746.
    GenomeRNAii 1675.
    NextBioi 6892.
    PROi P00746.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00746.
    Bgeei P00746.
    CleanExi HS_CFD.
    Genevestigatori P00746.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Relle M.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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.
      , 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: Small intestine.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Placenta, Skin, Spleen and Testis.
    5. "Human adipsin is identical to complement factor D and is expressed at high levels in adipose tissue."
      White R.T., Damm D., Hancock N., Rosen B.S., Lowell B.B., Usher P., Flier J.S., Spiegelman B.M.
      J. Biol. Chem. 267:9210-9213(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-253.
    6. "Amino acid sequence of human D of the alternative complement pathway."
      Niemann M.A., Bhown A.S., Bennett J.C., Volanakis J.E.
      Biochemistry 23:2482-2486(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-252.
    7. "Amino acid sequence of human factor D of the complement system. Similarity in sequence between factor D and proteases of non-plasma origin."
      Johnson D.M.A., Gagnon J., Reid K.B.M.
      FEBS Lett. 166:347-351(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-252.
    8. "Partial amino acid sequence of human factor D: homology with serine proteases."
      Volanakis J.E., Bhown A.S., Bennett J.C., Mole J.E.
      Proc. Natl. Acad. Sci. U.S.A. 77:1116-1119(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-82.
    9. "Active site amino acid sequence of human factor D."
      Davis A.E. III
      Proc. Natl. Acad. Sci. U.S.A. 77:4938-4942(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-78.
    10. "Factor D of the alternative pathway of human complement. Purification, alignment and N-terminal amino acid sequences of the major cyanogen bromide fragments, and localization of the serine residue at the active site."
      Johnson D.M.A., Gagnon J., Reid K.B.M.
      Biochem. J. 187:863-874(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-61 AND 194-220.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    12. "Crystal structure of a complement factor D mutant expressing enhanced catalytic activity."
      Kim S., Narayana S.V., Volanakis J.E.
      J. Biol. Chem. 270:24399-24405(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    13. "Deficient alternative complement pathway activation due to factor D deficiency by 2 novel mutations in the complement factor D gene in a family with meningococcal infections."
      Sprong T., Roos D., Weemaes C., Neeleman C., Geesing C.L., Mollnes T.E., van Deuren M.
      Blood 107:4865-4870(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CFDD DEFICIENCY GLY-213 AND ARG-214.

    Entry informationi

    Entry nameiCFAD_HUMAN
    AccessioniPrimary (citable) accession number: P00746
    Secondary accession number(s): B4DV76
    , Q5U5S1, Q86VJ5, Q8N4E0, Q8WZB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 160 of the entry and version 5 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 19
      Human chromosome 19: 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. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3