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Protein

N(G),N(G)-dimethylarginine dimethylaminohydrolase 1

Gene

DDAH1

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

Functioni

Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.

Catalytic activityi

N(omega),N(omega)-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline.2 Publications

Enzyme regulationi

Inhibited by zinc ions (By similarity). Enzyme purified in the absence of 1,10-phenanthroline contains on average 0.4 zinc atoms per subunit. Inhibited by 4-hydroxy-nonenal through the formation of a covalent adduct with His-173. Competitively inhibited by N(5)-iminopropyl-ornithine.By similarity2 Publications

Kineticsi

  1. KM=69 µM for asymmetric dimethylarginine (ADMA)2 Publications
  2. KM=54 µM for monomethyl-L-arginine (MMA)2 Publications
  3. KM=3.1 µM for S-methyl-L-thiocitrulline2 Publications
  1. Vmax=356 nmol/min/mg enzyme with ADMA2 Publications
  2. Vmax=154 nmol/min/mg enzyme with NMA2 Publications

pH dependencei

Optimum pH is 8.5.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301Substrate; via carbonyl oxygen
Binding sitei73 – 731Substrate
Binding sitei98 – 981Substrate
Binding sitei145 – 1451Substrate
Active sitei173 – 1731Proton donor1 Publication
Binding sitei268 – 2681Substrate; via carbonyl oxygen
Active sitei274 – 2741Nucleophile1 Publication
Metal bindingi274 – 2741ZincBy similarity

GO - Molecular functioni

  • amino acid binding Source: Ensembl
  • catalytic activity Source: ProtInc
  • dimethylargininase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • arginine catabolic process Source: ProtInc
  • citrulline metabolic process Source: UniProtKB
  • nitric oxide mediated signal transduction Source: ProtInc
  • positive regulation of angiogenesis Source: Ensembl
  • positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  • regulation of systemic arterial blood pressure Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.3.18. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (EC:3.5.3.18)
Short name:
DDAH-1
Short name:
Dimethylarginine dimethylaminohydrolase 1
Alternative name(s):
DDAHI
Dimethylargininase-1
Gene namesi
Name:DDAH1
Synonyms:DDAH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2715. DDAH1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301L → A: Reduces enzyme activity and affinity for asymmetric dimethylarginine about 12-fold. 1 Publication
Mutagenesisi78 – 781E → A: Reduces enzyme activity about 1000-fold, and affinity for asymmetric dimethylarginine about 100-fold. 1 Publication
Mutagenesisi271 – 2711L → G: Reduces enzyme activity about 10-fold, and affinity for asymmetric dimethylarginine about 7-fold. 1 Publication

Organism-specific databases

PharmGKBiPA27185.

Chemistry

DrugBankiDB00155. L-Citrulline.

Polymorphism and mutation databases

BioMutaiDDAH1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 285284N(G),N(G)-dimethylarginine dimethylaminohydrolase 1PRO_0000171118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei222 – 2221S-nitrosocysteineBy similarity
Modified residuei274 – 2741S-nitrosocysteineBy similarity

Keywords - PTMi

Acetylation, S-nitrosylation

Proteomic databases

MaxQBiO94760.
PaxDbiO94760.
PeptideAtlasiO94760.
PRIDEiO94760.

2D gel databases

REPRODUCTION-2DPAGEIPI00220342.

PTM databases

PhosphoSiteiO94760.

Expressioni

Tissue specificityi

Detected in brain, liver, kidney and pancreas, and at low levels in skeletal muscle.1 Publication

Gene expression databases

BgeeiO94760.
CleanExiHS_DDAH1.
ExpressionAtlasiO94760. baseline and differential.
GenevisibleiO94760. HS.

Organism-specific databases

HPAiHPA006308.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi117114. 7 interactions.
IntActiO94760. 2 interactions.
STRINGi9606.ENSP00000284031.

Structurei

Secondary structure

1
285
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196Combined sources
Helixi25 – 284Combined sources
Helixi40 – 5516Combined sources
Turni56 – 583Combined sources
Beta strandi61 – 655Combined sources
Turni72 – 754Combined sources
Helixi77 – 804Combined sources
Beta strandi81 – 844Combined sources
Beta strandi87 – 904Combined sources
Helixi96 – 1016Combined sources
Helixi102 – 1109Combined sources
Turni111 – 1133Combined sources
Beta strandi115 – 1184Combined sources
Helixi128 – 1303Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi138 – 1458Combined sources
Helixi148 – 15710Combined sources
Turni158 – 1603Combined sources
Beta strandi163 – 1675Combined sources
Helixi174 – 1763Combined sources
Beta strandi177 – 1826Combined sources
Beta strandi185 – 1895Combined sources
Helixi192 – 20312Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi210 – 2167Combined sources
Helixi217 – 2204Combined sources
Beta strandi223 – 2275Combined sources
Turni228 – 2303Combined sources
Beta strandi231 – 2377Combined sources
Turni239 – 2413Combined sources
Helixi243 – 2519Combined sources
Beta strandi255 – 2606Combined sources
Helixi263 – 2664Combined sources
Turni267 – 2693Combined sources
Helixi273 – 2753Combined sources
Beta strandi277 – 2793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JAIX-ray2.30A/B2-285[»]
2JAJX-ray2.00A/B2-285[»]
3I2EX-ray2.03A/B1-285[»]
3I4AX-ray1.90A/B1-285[»]
3P8EX-ray2.49A/B1-285[»]
3P8PX-ray2.50A/B1-285[»]
ProteinModelPortaliO94760.
SMRiO94760. Positions 8-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94760.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni78 – 792Substrate binding

Sequence similaritiesi

Belongs to the DDAH family.Curated

Phylogenomic databases

eggNOGiCOG1834.
GeneTreeiENSGT00390000009331.
HOGENOMiHOG000161035.
HOVERGENiHBG055937.
InParanoidiO94760.
KOiK01482.
OMAiMAYPEYP.
OrthoDBiEOG73V6KV.
PhylomeDBiO94760.
TreeFamiTF314737.

Family and domain databases

InterProiIPR003198. Amidino_trans.
[Graphical view]
PfamiPF02274. Amidinotransf. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O94760-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAGLGHPAAF GRATHAVVRA LPESLGQHAL RSAKGEEVDV ARAERQHQLY
60 70 80 90 100
VGVLGSKLGL QVVELPADES LPDCVFVEDV AVVCEETALI TRPGAPSRRK
110 120 130 140 150
EVDMMKEALE KLQLNIVEMK DENATLDGGD VLFTGREFFV GLSKRTNQRG
160 170 180 190 200
AEILADTFKD YAVSTVPVAD GLHLKSFCSM AGPNLIAIGS SESAQKALKI
210 220 230 240 250
MQQMSDHRYD KLTVPDDIAA NCIYLNIPNK GHVLLHRTPE EYPESAKVYE
260 270 280
KLKDHMLIPV SMSELEKVDG LLTCCSVLIN KKVDS
Length:285
Mass (Da):31,122
Last modified:January 23, 2007 - v3
Checksum:iCD8875DF267EF39B
GO
Isoform 2 (identifier: O94760-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-103: Missing.

Show »
Length:182
Mass (Da):20,189
Checksum:i0612A4D0E824A1EE
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 103103Missing in isoform 2. 1 PublicationVSP_043813Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001915 mRNA. Translation: BAA37117.1.
BX648145 mRNA. Translation: CAI45988.1.
AC092807 Genomic DNA. No translation available.
AL078459 Genomic DNA. No translation available.
AL360219 Genomic DNA. No translation available.
CH471097 Genomic DNA. Translation: EAW73199.1.
BC033680 mRNA. Translation: AAH33680.1.
BC043235 mRNA. Translation: AAH43235.2.
CCDSiCCDS44170.1. [O94760-2]
CCDS705.1. [O94760-1]
RefSeqiNP_001127917.1. NM_001134445.1. [O94760-2]
NP_036269.1. NM_012137.3. [O94760-1]
XP_005270766.1. XM_005270709.2. [O94760-2]
XP_005270767.1. XM_005270710.2. [O94760-2]
XP_006710607.1. XM_006710544.1. [O94760-2]
UniGeneiHs.713411.

Genome annotation databases

EnsembliENST00000284031; ENSP00000284031; ENSG00000153904.
ENST00000426972; ENSP00000411189; ENSG00000153904. [O94760-2]
ENST00000535924; ENSP00000439045; ENSG00000153904. [O94760-2]
ENST00000539042; ENSP00000438604; ENSG00000153904.
GeneIDi23576.
KEGGihsa:23576.
UCSCiuc001dlb.3. human. [O94760-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001915 mRNA. Translation: BAA37117.1.
BX648145 mRNA. Translation: CAI45988.1.
AC092807 Genomic DNA. No translation available.
AL078459 Genomic DNA. No translation available.
AL360219 Genomic DNA. No translation available.
CH471097 Genomic DNA. Translation: EAW73199.1.
BC033680 mRNA. Translation: AAH33680.1.
BC043235 mRNA. Translation: AAH43235.2.
CCDSiCCDS44170.1. [O94760-2]
CCDS705.1. [O94760-1]
RefSeqiNP_001127917.1. NM_001134445.1. [O94760-2]
NP_036269.1. NM_012137.3. [O94760-1]
XP_005270766.1. XM_005270709.2. [O94760-2]
XP_005270767.1. XM_005270710.2. [O94760-2]
XP_006710607.1. XM_006710544.1. [O94760-2]
UniGeneiHs.713411.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JAIX-ray2.30A/B2-285[»]
2JAJX-ray2.00A/B2-285[»]
3I2EX-ray2.03A/B1-285[»]
3I4AX-ray1.90A/B1-285[»]
3P8EX-ray2.49A/B1-285[»]
3P8PX-ray2.50A/B1-285[»]
ProteinModelPortaliO94760.
SMRiO94760. Positions 8-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117114. 7 interactions.
IntActiO94760. 2 interactions.
STRINGi9606.ENSP00000284031.

Chemistry

BindingDBiO94760.
ChEMBLiCHEMBL6036.
DrugBankiDB00155. L-Citrulline.

PTM databases

PhosphoSiteiO94760.

Polymorphism and mutation databases

BioMutaiDDAH1.

2D gel databases

REPRODUCTION-2DPAGEIPI00220342.

Proteomic databases

MaxQBiO94760.
PaxDbiO94760.
PeptideAtlasiO94760.
PRIDEiO94760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284031; ENSP00000284031; ENSG00000153904.
ENST00000426972; ENSP00000411189; ENSG00000153904. [O94760-2]
ENST00000535924; ENSP00000439045; ENSG00000153904. [O94760-2]
ENST00000539042; ENSP00000438604; ENSG00000153904.
GeneIDi23576.
KEGGihsa:23576.
UCSCiuc001dlb.3. human. [O94760-1]

Organism-specific databases

CTDi23576.
GeneCardsiGC01M085785.
HGNCiHGNC:2715. DDAH1.
HPAiHPA006308.
MIMi604743. gene.
neXtProtiNX_O94760.
PharmGKBiPA27185.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1834.
GeneTreeiENSGT00390000009331.
HOGENOMiHOG000161035.
HOVERGENiHBG055937.
InParanoidiO94760.
KOiK01482.
OMAiMAYPEYP.
OrthoDBiEOG73V6KV.
PhylomeDBiO94760.
TreeFamiTF314737.

Enzyme and pathway databases

BRENDAi3.5.3.18. 2681.

Miscellaneous databases

ChiTaRSiDDAH1. human.
EvolutionaryTraceiO94760.
GenomeRNAii23576.
NextBioi46178.
PROiO94760.
SOURCEiSearch...

Gene expression databases

BgeeiO94760.
CleanExiHS_DDAH1.
ExpressionAtlasiO94760. baseline and differential.
GenevisibleiO94760. HS.

Family and domain databases

InterProiIPR003198. Amidino_trans.
[Graphical view]
PfamiPF02274. Amidinotransf. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, cDNA cloning and expression of human NG,NG-dimethylarginine dimethylaminohydrolase."
    Kimoto M., Miyatake S., Sasagawa T., Yamashita H., Okita M., Oka T., Ogawa T., Tsuji H.
    Eur. J. Biochem. 258:863-868(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-12 AND 35-50, ABSENCE OF BOUND ZINC, ACETYLATION AT ALA-2.
    Tissue: Kidney and Liver.
  2. "Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases."
    Leiper J.M., Santa Maria J., Chubb A., MacAllister R.J., Charles I.G., Whitley G.S., Vallance P.
    Biochem. J. 343:209-214(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Endometrial cancer.
  4. "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.
    , 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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Colon, Kidney, Stomach and Testis.
  7. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 20-31; 46-57; 112-136; 150-196; 212-230 AND 268-281, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  8. "Mechanism of 4-HNE mediated inhibition of hDDAH-1: implications in NO regulation."
    Forbes S.P., Druhan L.J., Guzman J.E., Parinandi N., Zhang L., Green-Church K.B., Cardounel A.J.
    Biochemistry 47:1819-1826(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-284 IN COMPLEXES WITH CITRULLINE AND INHIBITOR L-257.
  13. "Developing dual and specific inhibitors of dimethylarginine dimethylaminohydrolase-1 and nitric oxide synthase: toward a targeted polypharmacology to control nitric oxide."
    Wang Y., Monzingo A.F., Hu S., Schaller T.H., Robertus J.D., Fast W.
    Biochemistry 48:8624-8635(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH N-1-IMINOPROPYL-L-ORNITHINE, CATALYTIC ACTIVITY, ZINC-BINDING, ENZYME REGULATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF LEU-30; GLU-78 AND LEU-271, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiDDAH1_HUMAN
AccessioniPrimary (citable) accession number: O94760
Secondary accession number(s): Q5HYC8, Q86XK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 142 of the entry and version 3 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.