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Protein

Histidine ammonia-lyase

Gene

hutH

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-histidine degradation into L-glutamate

This protein is involved in step 1 of the subpathway that synthesizes N-formimidoyl-L-glutamate from L-histidine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH_1), Histidine ammonia-lyase (BL240_15610), Histidine ammonia-lyase (DW66_2585), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (PU99_10260), Histidine ammonia-lyase (HB13667_15065), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (AYO28_15945), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (SAMN03097715_02348), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH_2), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH_3), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (HB4184_14930), Histidine ammonia-lyase (BGP84_10845), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (HA62_16700), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (BIW19_01715), Histidine ammonia-lyase (hutH)
  2. Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (BIW19_25300), Urocanate hydratase (hutU)
  3. Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI)
This subpathway is part of the pathway L-histidine degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-formimidoyl-L-glutamate from L-histidine, the pathway L-histidine degradation into L-glutamate and in Amino-acid degradation.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
Biological processHistidine metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-11608

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.3.1.3 5092

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00379;UER00549

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histidine ammonia-lyase (EC:4.3.1.3)
Short name:
Histidase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:hutH
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri303 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi113S → A: No loss of activity. 1
Mutagenesisi144S → A or T: Complete loss of activity. 3 Publications1
Mutagenesisi144S → C: No effect. 3 Publications1
Mutagenesisi394S → A: No loss of activity. 1
Mutagenesisi419S → A: No loss of activity. 1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001610172 – 510Histidine ammonia-lyaseAdd BLAST509

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki143 ↔ 1455-imidazolinone (Ala-Gly)
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1442,3-didehydroalanine (Ser)2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By histidine and urocanate.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1510
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P21310

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P21310

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P21310

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C84 Bacteria
COG2986 LUCA

KEGG Orthology (KO)

More...
KOi
K01745

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00332 PAL-HAL, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.275.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00229 His_ammonia_lyase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001106 Aromatic_Lyase
IPR024083 Fumarase/histidase_N
IPR005921 HutH
IPR008948 L-Aspartase-like
IPR022313 Phe/His_NH3-lyase_AS

The PANTHER Classification System

More...
PANTHERi
PTHR10362 PTHR10362, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00221 Lyase_aromatic, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48557 SSF48557, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01225 hutH, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00488 PAL_HISTIDASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P21310-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTELTLKPGT LTLAQLRAIH AAPVRLQLDA SAAPAIDASV ACVEQIIAED
60 70 80 90 100
RTAYGINTGF GLLASTRIAS HDLENLQRSL VLSHAAGIGA PLDDDLVRLI
110 120 130 140 150
MVLKINSLSR GFSGIRRKVI DALIALVNAE VYPHIPLKGS VGASGDLAPL
160 170 180 190 200
AHMSLVLLGE GKARYKGQWL SATEALAVAG LEPLTLAAKE GLALLNGTQA
210 220 230 240 250
STAYALRGLF YAEDLYAAAI ACGGLSVEAV LGSRSPFDAR IHEARGQRGQ
260 270 280 290 300
IDTAACFRDL LGDSSEVSLS HKNCDKVQDP YSLRCQPQVM GACLTQLRQA
310 320 330 340 350
AEVLGIEANA VSDNPLVFAA EGDVISGGNF HAEPVAMAAD NLALAIAEIG
360 370 380 390 400
SLSERRISLM MDKHMSQLPP FLVENGGVNS GFMIAQVTAA ALASENKALS
410 420 430 440 450
HPHSVDSLPT SANQEDHVSM APAAGKRLWE MAENTRGVLA IEWLGACQGL
460 470 480 490 500
DLRKGLKTSA KLEKARQALR SEVAHYDRDR FFAPDIEKAV ELLAKGSLTG
510
LLPAGVLPSL
Length:510
Mass (Da):53,761
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7D80C7E64B0C4F57
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti152H → T in AAA25840 (PubMed:2332400).Curated1
Sequence conflicti439L → P in AAA25840 (PubMed:2332400).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M35140 Genomic DNA Translation: AAA25840.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A35251

NCBI Reference Sequences

More...
RefSeqi
WP_016502005.1, NZ_UGUX01000003.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAA25840

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35140 Genomic DNA Translation: AAA25840.1
PIRiA35251
RefSeqiWP_016502005.1, NZ_UGUX01000003.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8FX-ray2.10A2-510[»]
1EB4X-ray2.00A2-510[»]
1GK2X-ray1.90A/B/C/D2-510[»]
1GK3X-ray2.25A2-510[»]
1GKJX-ray1.70A2-510[»]
1GKMX-ray1.00A2-510[»]
ProteinModelPortaliP21310
SMRiP21310
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA25840

Phylogenomic databases

eggNOGiENOG4105C84 Bacteria
COG2986 LUCA
KOiK01745

Enzyme and pathway databases

UniPathwayi
UPA00379;UER00549

BioCyciMetaCyc:MONOMER-11608
BRENDAi4.3.1.3 5092

Miscellaneous databases

EvolutionaryTraceiP21310

Family and domain databases

CDDicd00332 PAL-HAL, 1 hit
Gene3Di1.10.275.10, 1 hit
HAMAPiMF_00229 His_ammonia_lyase, 1 hit
InterProiView protein in InterPro
IPR001106 Aromatic_Lyase
IPR024083 Fumarase/histidase_N
IPR005921 HutH
IPR008948 L-Aspartase-like
IPR022313 Phe/His_NH3-lyase_AS
PANTHERiPTHR10362 PTHR10362, 1 hit
PfamiView protein in Pfam
PF00221 Lyase_aromatic, 1 hit
SUPFAMiSSF48557 SSF48557, 1 hit
TIGRFAMsiTIGR01225 hutH, 1 hit
PROSITEiView protein in PROSITE
PS00488 PAL_HISTIDASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHUTH_PSEPU
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P21310
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 127 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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