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P00746

- CFAD_HUMAN

UniProt

P00746 - CFAD_HUMAN

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Protein

Complement factor D

Gene

CFD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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: UniProtKB
  4. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

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

BgeeiP00746.
CleanExiHS_CFD.
ExpressionAtlasiP00746. baseline and differential.
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 – 323Combined sources
Beta strandi40 – 456Combined sources
Beta strandi48 – 5710Combined sources
Beta strandi60 – 634Combined sources
Helixi65 – 684Combined sources
Beta strandi72 – 743Combined sources
Beta strandi76 – 816Combined sources
Beta strandi83 – 875Combined sources
Beta strandi93 – 10210Combined sources
Helixi108 – 1136Combined sources
Beta strandi116 – 1227Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi147 – 1548Combined sources
Turni156 – 1594Combined sources
Beta strandi167 – 1748Combined sources
Helixi176 – 1794Combined sources
Turni182 – 1876Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi200 – 2023Combined sources
Turni205 – 2095Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi236 – 2405Combined sources
Helixi241 – 2444Combined sources
Helixi245 – 2528Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118895.
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

        10         20         30         40         50
MHSWERLAVL VLLGAAACAA PPRGRILGGR EAEAHARPYM ASVQLNGAHL
60 70 80 90 100
CGGVLVAEQW VLSAAHCLED AADGKVQVLL GAHSLSQPEP SKRLYDVLRA
110 120 130 140 150
VPHPDSQPDT IDHDLLLLQL SEKATLGPAV RPLPWQRVDR DVAPGTLCDV
160 170 180 190 200
AGWGIVNHAG RRPDSLQHVL LPVLDRATCN RRTHHDGAIT ERLMCAESNR
210 220 230 240 250
RDSCKGDSGG PLVCGGVLEG VVTSGSRVCG NRKKPGIYTR VASYAAWIDS

VLA
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.Curated

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:
EMBLi
GenBanki
DDBJi
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.
ENST00000617994; ENSP00000478745; ENSG00000274619.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

BindingDBi P00746.
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 .
ENST00000617994 ; ENSP00000478745 ; ENSG00000274619 .
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.
GeneTreei ENSGT00760000118895.
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

ChiTaRSi CFD. human.
EvolutionaryTracei P00746.
GenomeRNAii 1675.
NextBioi 6892.
PROi P00746.
SOURCEi Search...

Gene expression databases

Bgeei P00746.
CleanExi HS_CFD.
ExpressionAtlasi P00746. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 162 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