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Protein

Arginase-1

Gene

ARG1

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

Functioni

Catalytic activityi

L-arginine + H2O = L-ornithine + urea.2 Publications

Cofactori

Mn2+4 PublicationsNote: Binds 2 manganese ions per subunit.4 Publications

Pathwayi: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and urea from L-arginine.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Arginase (ARG2), Arginase-2, mitochondrial (ARG2), Arginase-1 (ARG1)
This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine and urea from L-arginine, the pathway urea cycle and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi101Manganese 1Combined sources4 Publications1
Metal bindingi124Manganese 1Combined sources4 Publications1
Metal bindingi124Manganese 2Combined sources4 Publications1
Metal bindingi126Manganese 2Combined sources4 Publications1
Metal bindingi128Manganese 1Combined sources4 Publications1
Binding sitei183SubstrateCombined sources1
Metal bindingi232Manganese 1Combined sources4 Publications1
Metal bindingi232Manganese 2Combined sources4 Publications1
Metal bindingi234Manganese 2Combined sources4 Publications1
Binding sitei246SubstrateBy similarity1
Binding sitei277SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism, Urea cycle

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS04231-MONOMER.
ZFISH:HS04231-MONOMER.
BRENDAi3.5.3.1. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-70635. Urea cycle.
SABIO-RKP05089.
UniPathwayiUPA00158; UER00270.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginase-1 (EC:3.5.3.12 Publications)
Alternative name(s):
Liver-type arginase
Type I arginase
Gene namesi
Name:ARG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:663. ARG1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: Ensembl
  • mitochondrial outer membrane Source: Ensembl
  • neuronal cell body Source: Ensembl
  • neuron projection Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Argininemia (ARGIN)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia and progressive spastic quadriplegia.
See also OMIM:207800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01559411I → T in ARGIN; 12% of wild-type activity. 2 PublicationsCorresponds to variant rs28941474dbSNPEnsembl.1
Natural variantiVAR_07216427G → D in ARGIN; 5.2% of wild-type activity. 1 Publication1
Natural variantiVAR_07216574G → V in ARGIN; 9.3% of wild-type activity. 1 Publication1
Natural variantiVAR_072166125A → V in ARGIN; decreases erythrocyte arginase activity. 1 Publication1
Natural variantiVAR_072167134T → I in ARGIN; 9.3% of wild-type activity. 1 Publication1
Natural variantiVAR_015595138G → V in ARGIN. 1 PublicationCorresponds to variant rs104893943dbSNPEnsembl.1
Natural variantiVAR_072168180R → T in ARGIN; decreases erythrocyte arginase activity. 1 Publication1
Natural variantiVAR_000674235G → R in ARGIN; decreases erythrocyte arginase activity. 2 PublicationsCorresponds to variant rs104893948dbSNPEnsembl.1
Natural variantiVAR_072169308R → Q in ARGIN; 20.8% of wild-type activity. 1 PublicationCorresponds to variant rs377280518dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi383.
MalaCardsiARG1.
MIMi207800. phenotype.
OpenTargetsiENSG00000118520.
Orphaneti90. Argininemia.
PharmGKBiPA24947.

Chemistry databases

ChEMBLiCHEMBL1075097.
DrugBankiDB00129. L-Ornithine.
DB03904. Urea.
GuidetoPHARMACOLOGYi1244.

Polymorphism and mutation databases

BioMutaiARG1.
DMDMi12230985.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001736931 – 322Arginase-1Add BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17N6-succinyllysineBy similarity1
Modified residuei62PhosphoserineCombined sources1
Modified residuei72PhosphoserineBy similarity1
Modified residuei75N6-succinyllysineBy similarity1
Modified residuei163PhosphoserineCombined sources1
Modified residuei217PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP05089.
MaxQBiP05089.
PaxDbiP05089.
PeptideAtlasiP05089.
PRIDEiP05089.

PTM databases

iPTMnetiP05089.
PhosphoSitePlusiP05089.

Expressioni

Inductioni

By arginine or homoarginine.

Gene expression databases

BgeeiENSG00000118520.
CleanExiHS_ARG1.
GenevisibleiP05089. HS.

Organism-specific databases

HPAiCAB009434.
CAB056159.
HPA003595.
HPA024006.

Interactioni

Subunit structurei

Homotrimer.5 Publications

Protein-protein interaction databases

BioGridi106878. 26 interactors.
IntActiP05089. 14 interactors.
MINTiMINT-3974693.
STRINGi9606.ENSP00000357066.

Chemistry databases

BindingDBiP05089.

Structurei

Secondary structure

1322
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 13Combined sources7
Helixi22 – 26Combined sources5
Helixi27 – 33Combined sources7
Helixi36 – 42Combined sources7
Beta strandi46 – 52Combined sources7
Beta strandi67 – 69Combined sources3
Helixi70 – 89Combined sources20
Beta strandi93 – 99Combined sources7
Helixi101 – 103Combined sources3
Helixi104 – 114Combined sources11
Beta strandi119 – 126Combined sources8
Turni132 – 134Combined sources3
Helixi140 – 142Combined sources3
Helixi144 – 148Combined sources5
Helixi150 – 152Combined sources3
Turni153 – 155Combined sources3
Helixi171 – 173Combined sources3
Beta strandi174 – 179Combined sources6
Helixi184 – 193Combined sources10
Beta strandi196 – 199Combined sources4
Helixi200 – 206Combined sources7
Helixi208 – 220Combined sources13
Beta strandi221 – 223Combined sources3
Beta strandi227 – 232Combined sources6
Helixi233 – 235Combined sources3
Turni238 – 240Combined sources3
Beta strandi243 – 246Combined sources4
Helixi254 – 267Combined sources14
Beta strandi270 – 276Combined sources7
Helixi280 – 282Combined sources3
Helixi286 – 303Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WVAX-ray1.94A/B1-322[»]
1WVBX-ray2.30A/B1-322[»]
2AEBX-ray1.29A/B1-322[»]
2PHAX-ray1.90A/B1-322[»]
2PHOX-ray1.95A/B1-322[»]
2PLLX-ray1.90A/B1-322[»]
2ZAVX-ray1.70A/B1-322[»]
3DJ8X-ray1.51A/B1-322[»]
3E6KX-ray2.10A/B1-322[»]
3E6VX-ray1.72A/B1-322[»]
3F80X-ray1.60A/B1-322[»]
3GMZX-ray1.43A/B1-322[»]
3GN0X-ray1.70A/B1-322[»]
3KV2X-ray1.55A/B1-322[»]
3LP4X-ray1.90A/B1-322[»]
3LP7X-ray2.04A/B1-322[»]
3MFVX-ray1.90A/B1-322[»]
3MFWX-ray1.47A/B1-322[»]
3MJLX-ray1.90A/B1-322[»]
3SJTX-ray1.60A/B1-322[»]
3SKKX-ray1.70A/B1-322[»]
3TF3X-ray1.64A/B1-322[»]
3TH7X-ray2.10A/B1-322[»]
3THEX-ray1.97A/B1-322[»]
3THHX-ray1.85A/B1-322[»]
3THJX-ray1.50A/B1-322[»]
4FCIX-ray1.82A/B1-322[»]
4FCKX-ray1.90A/B1-322[»]
4GSMX-ray1.70A/B1-322[»]
4GSVX-ray1.48A/B1-322[»]
4GSZX-ray2.20A/B1-322[»]
4GWCX-ray1.90A/B1-322[»]
4GWDX-ray1.53A/B1-322[»]
4HWWX-ray1.30A/B5-318[»]
4HXQX-ray1.45A/B5-318[»]
4IE1X-ray2.00A/B5-318[»]
ProteinModelPortaliP05089.
SMRiP05089.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05089.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 130Substrate bindingCombined sources5
Regioni137 – 139Substrate bindingCombined sources3

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2965. Eukaryota.
COG0010. LUCA.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiP05089.
KOiK01476.
OMAiEQECDVK.
OrthoDBiEOG091G0A38.
PhylomeDBiP05089.
TreeFamiTF300034.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P05089-1) [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
MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY
60 70 80 90 100
GDLPFADIPN DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD
110 120 130 140 150
HSLAIGSISG HARVHPDLGV IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK
160 170 180 190 200
ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYIL KTLGIKYFSM
210 220 230 240 250
TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF TPATGTPVVG
260 270 280 290 300
GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT
310 320
LACFGLAREG NHKPIDYLNP PK
Length:322
Mass (Da):34,735
Last modified:January 11, 2001 - v2
Checksum:i8F3BE2652243F622
GO
Isoform 2 (identifier: P05089-2) [UniParc]FASTAAdd to basket
Also known as: Erythroid variant

The sequence of this isoform differs from the canonical sequence as follows:
     43-43: Q → QVTQNFLIL

Note: May be due to a competing acceptor splice site. No experimental confirmation available.
Show »
Length:330
Mass (Da):35,664
Checksum:i3547D8B6C254179B
GO
Isoform 3 (identifier: P05089-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     204-289: Missing.

Show »
Length:236
Mass (Da):25,356
Checksum:i79F02C69B700AB67
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti48K → E in AAL71547 (Ref. 3) Curated1
Sequence conflicti86E → Q in AAA51776 (PubMed:3540966).Curated1
Sequence conflicti202E → K in AAL71547 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01559411I → T in ARGIN; 12% of wild-type activity. 2 PublicationsCorresponds to variant rs28941474dbSNPEnsembl.1
Natural variantiVAR_07216427G → D in ARGIN; 5.2% of wild-type activity. 1 Publication1
Natural variantiVAR_07216574G → V in ARGIN; 9.3% of wild-type activity. 1 Publication1
Natural variantiVAR_072166125A → V in ARGIN; decreases erythrocyte arginase activity. 1 Publication1
Natural variantiVAR_072167134T → I in ARGIN; 9.3% of wild-type activity. 1 Publication1
Natural variantiVAR_015595138G → V in ARGIN. 1 PublicationCorresponds to variant rs104893943dbSNPEnsembl.1
Natural variantiVAR_072168180R → T in ARGIN; decreases erythrocyte arginase activity. 1 Publication1
Natural variantiVAR_000674235G → R in ARGIN; decreases erythrocyte arginase activity. 2 PublicationsCorresponds to variant rs104893948dbSNPEnsembl.1
Natural variantiVAR_000675290T → S.1 PublicationCorresponds to variant rs104893942dbSNPEnsembl.1
Natural variantiVAR_072169308R → Q in ARGIN; 20.8% of wild-type activity. 1 PublicationCorresponds to variant rs377280518dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00933043Q → QVTQNFLIL in isoform 2. 1 Publication1
Alternative sequenceiVSP_009331204 – 289Missing in isoform 3. 2 PublicationsAdd BLAST86

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14502 mRNA. Translation: AAA51776.1.
X12662
, X12663, X12664, X12665, X12666, X12667, X12668, X12669 Genomic DNA. Translation: CAA31188.1.
AY074488 mRNA. Translation: AAL71547.1.
BT006741 mRNA. Translation: AAP35387.1.
AL121575 Genomic DNA. Translation: CAB92071.1.
AL121575 Genomic DNA. Translation: CAI23317.1.
AL121575 Genomic DNA. Translation: CAI23318.1.
BC005321 mRNA. Translation: AAH05321.1.
BC020653 mRNA. Translation: AAH20653.1.
CCDSiCCDS5145.1. [P05089-1]
CCDS59038.1. [P05089-2]
PIRiS02132. A26370.
RefSeqiNP_000036.2. NM_000045.3. [P05089-1]
NP_001231367.1. NM_001244438.1. [P05089-2]
UniGeneiHs.440934.

Genome annotation databases

EnsembliENST00000356962; ENSP00000349446; ENSG00000118520. [P05089-2]
ENST00000368087; ENSP00000357066; ENSG00000118520. [P05089-1]
GeneIDi383.
KEGGihsa:383.
UCSCiuc003qcp.3. human. [P05089-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Arginase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14502 mRNA. Translation: AAA51776.1.
X12662
, X12663, X12664, X12665, X12666, X12667, X12668, X12669 Genomic DNA. Translation: CAA31188.1.
AY074488 mRNA. Translation: AAL71547.1.
BT006741 mRNA. Translation: AAP35387.1.
AL121575 Genomic DNA. Translation: CAB92071.1.
AL121575 Genomic DNA. Translation: CAI23317.1.
AL121575 Genomic DNA. Translation: CAI23318.1.
BC005321 mRNA. Translation: AAH05321.1.
BC020653 mRNA. Translation: AAH20653.1.
CCDSiCCDS5145.1. [P05089-1]
CCDS59038.1. [P05089-2]
PIRiS02132. A26370.
RefSeqiNP_000036.2. NM_000045.3. [P05089-1]
NP_001231367.1. NM_001244438.1. [P05089-2]
UniGeneiHs.440934.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WVAX-ray1.94A/B1-322[»]
1WVBX-ray2.30A/B1-322[»]
2AEBX-ray1.29A/B1-322[»]
2PHAX-ray1.90A/B1-322[»]
2PHOX-ray1.95A/B1-322[»]
2PLLX-ray1.90A/B1-322[»]
2ZAVX-ray1.70A/B1-322[»]
3DJ8X-ray1.51A/B1-322[»]
3E6KX-ray2.10A/B1-322[»]
3E6VX-ray1.72A/B1-322[»]
3F80X-ray1.60A/B1-322[»]
3GMZX-ray1.43A/B1-322[»]
3GN0X-ray1.70A/B1-322[»]
3KV2X-ray1.55A/B1-322[»]
3LP4X-ray1.90A/B1-322[»]
3LP7X-ray2.04A/B1-322[»]
3MFVX-ray1.90A/B1-322[»]
3MFWX-ray1.47A/B1-322[»]
3MJLX-ray1.90A/B1-322[»]
3SJTX-ray1.60A/B1-322[»]
3SKKX-ray1.70A/B1-322[»]
3TF3X-ray1.64A/B1-322[»]
3TH7X-ray2.10A/B1-322[»]
3THEX-ray1.97A/B1-322[»]
3THHX-ray1.85A/B1-322[»]
3THJX-ray1.50A/B1-322[»]
4FCIX-ray1.82A/B1-322[»]
4FCKX-ray1.90A/B1-322[»]
4GSMX-ray1.70A/B1-322[»]
4GSVX-ray1.48A/B1-322[»]
4GSZX-ray2.20A/B1-322[»]
4GWCX-ray1.90A/B1-322[»]
4GWDX-ray1.53A/B1-322[»]
4HWWX-ray1.30A/B5-318[»]
4HXQX-ray1.45A/B5-318[»]
4IE1X-ray2.00A/B5-318[»]
ProteinModelPortaliP05089.
SMRiP05089.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106878. 26 interactors.
IntActiP05089. 14 interactors.
MINTiMINT-3974693.
STRINGi9606.ENSP00000357066.

Chemistry databases

BindingDBiP05089.
ChEMBLiCHEMBL1075097.
DrugBankiDB00129. L-Ornithine.
DB03904. Urea.
GuidetoPHARMACOLOGYi1244.

PTM databases

iPTMnetiP05089.
PhosphoSitePlusiP05089.

Polymorphism and mutation databases

BioMutaiARG1.
DMDMi12230985.

Proteomic databases

EPDiP05089.
MaxQBiP05089.
PaxDbiP05089.
PeptideAtlasiP05089.
PRIDEiP05089.

Protocols and materials databases

DNASUi383.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356962; ENSP00000349446; ENSG00000118520. [P05089-2]
ENST00000368087; ENSP00000357066; ENSG00000118520. [P05089-1]
GeneIDi383.
KEGGihsa:383.
UCSCiuc003qcp.3. human. [P05089-1]

Organism-specific databases

CTDi383.
DisGeNETi383.
GeneCardsiARG1.
GeneReviewsiARG1.
HGNCiHGNC:663. ARG1.
HPAiCAB009434.
CAB056159.
HPA003595.
HPA024006.
MalaCardsiARG1.
MIMi207800. phenotype.
608313. gene.
neXtProtiNX_P05089.
OpenTargetsiENSG00000118520.
Orphaneti90. Argininemia.
PharmGKBiPA24947.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2965. Eukaryota.
COG0010. LUCA.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiP05089.
KOiK01476.
OMAiEQECDVK.
OrthoDBiEOG091G0A38.
PhylomeDBiP05089.
TreeFamiTF300034.

Enzyme and pathway databases

UniPathwayiUPA00158; UER00270.
BioCyciMetaCyc:HS04231-MONOMER.
ZFISH:HS04231-MONOMER.
BRENDAi3.5.3.1. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-70635. Urea cycle.
SABIO-RKP05089.

Miscellaneous databases

EvolutionaryTraceiP05089.
GenomeRNAii383.
PROiP05089.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000118520.
CleanExiHS_ARG1.
GenevisibleiP05089. HS.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARGI1_HUMAN
AccessioniPrimary (citable) accession number: P05089
Secondary accession number(s): A6NEA0
, Q5JWT5, Q5JWT6, Q8TE72, Q9BS50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 11, 2001
Last modified: November 30, 2016
This is version 200 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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 one 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.