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Entry version 162 (02 Jun 2021)
Sequence version 4 (23 Jan 2007)
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Protein

Photosystem I P700 chlorophyll a apoprotein A2

Gene

psaB

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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

PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.

<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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Note: PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi556Iron-sulfur (4Fe-4S); shared with dimeric partner1
Metal bindingi565Iron-sulfur (4Fe-4S); shared with dimeric partner1
Metal bindingi651Magnesium (chlorophyll-a B1 axial ligand)By similarity1
Metal bindingi659Magnesium (chlorophyll-a B3 axial ligand)By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei667Chlorophyll-a B3By similarity1
Binding sitei668Phylloquinone BBy similarity1

<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 functionOxidoreductase
Biological processElectron transport, Photosynthesis, Transport
Ligand4Fe-4S, Chlorophyll, Chromophore, Iron, Iron-sulfur, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:PSAB-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.97.1.12, 6192

<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:
Photosystem I P700 chlorophyll a apoprotein A2 (EC:1.97.1.12)
Alternative name(s):
PsaB
<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:psaB
Ordered Locus Names:slr1835
<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>OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
<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 identifieri1111708 [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 lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystisunclassified Synechocystis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001425 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei46 – 69Helical; Name=ISequence analysisAdd BLAST24
Transmembranei135 – 158Helical; Name=IISequence analysisAdd BLAST24
Transmembranei175 – 199Helical; Name=IIISequence analysisAdd BLAST25
Transmembranei273 – 291Helical; Name=IVSequence analysisAdd BLAST19
Transmembranei328 – 351Helical; Name=VSequence analysisAdd BLAST24
Transmembranei367 – 393Helical; Name=VISequence analysisAdd BLAST27
Transmembranei415 – 437Helical; Name=VIISequence analysisAdd BLAST23
Transmembranei514 – 532Helical; Name=VIIISequence analysisAdd BLAST19
Transmembranei572 – 593Helical; Name=IXSequence analysisAdd BLAST22
Transmembranei640 – 662Helical; Name=XSequence analysisAdd BLAST23
Transmembranei704 – 724Helical; Name=XISequence analysisAdd BLAST21

Keywords - Cellular componenti

Membrane, Photosystem I, Thylakoid

<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>Mutagenesisi522L → P: No protein or PSI accumulate, unable to grow photoautotrophically. 1 Publication1
Mutagenesisi522L → V: No effect. 1 Publication1
Mutagenesisi536L → M: No effect. 1 Publication1
Mutagenesisi565C → D or H: Almost no protein accumulates. No PSI activity is present, unable to grow photoautotrophically. 1 Publication1
Mutagenesisi565C → S: Accumulates some protein and PSI, still does not grow photoautotrophically. 1 Publication1
Mutagenesisi595 – 596HL → CI: PSI less stably assembled than wild-type, possible decrease in ability to accept electrons from cytochrome c6. C-594 is exposed on complex surface. 1 Publication2
Mutagenesisi600 – 602SGN → RCI: No protein or PSI accumulate, unable to grow photoautotrophically. 1 Publication3
Mutagenesisi609 – 611NST → KCI: No protein or PSI accumulate, unable to grow photoautotrophically. 1 Publication3
Mutagenesisi614 – 616MGW → ICA: No protein or PSI accumulate, unable to grow photoautotrophically. 1 Publication3
Mutagenesisi622 – 623WA → CR: Decreases PSI levels, has slow autotrophic growth, unable to accept electrons in vitro from cytochrome c6. C-621 is exposed on complex surface. 1 Publication2
Mutagenesisi627 – 629QLI → HCS: Decreases PSI levels but no change in ability of complex to accept electrons from cytochrome c6. C-627 is exposed on complex surface. 1 Publication3
Mutagenesisi632 – 633YN → CI: Greatly decreases levels of PSI, cells do not grow photoautotrophically. Unable to accept electrons from cytochrome c6 in vitro. C-631 is exposed on complex surface. 1 Publication2
Mutagenesisi638 – 639NN → CS: PSI assembles less stably than in wild-type but no change in ability of complex to accept electrons from cytochrome c6. C-637 is exposed on complex surface. 1 Publication2

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000886572 – 731Photosystem I P700 chlorophyll a apoprotein A2Add BLAST730

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P29255

<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

The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The cyanobacterial PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes (By similarity).

By similarity

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P29255, 3 interactors

STRING: functional protein association networks

More...
STRINGi
1148.1652517

<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

1731
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P29255

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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 PsaA/PsaB family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2885, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P29255

Identification of Orthologs from Complete Genome Data

More...
OMAi
FEQWVAD

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P29255

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1130.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00482, PSI_PsaB, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001280, PSI_PsaA/B
IPR020586, PSI_PsaA/B_CS
IPR036408, PSI_PsaA/B_sf
IPR006244, PSI_PsaB

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00223, PsaA_PsaB, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF002905, PSI_A, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00257, PHOTSYSPSAAB

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81558, SSF81558, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01336, psaB, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00419, PHOTOSYSTEM_I_PSAAB, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P29255-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATKFPKFSQ DLAQDPTTRR IWYGIATAHD FETHDGMTEE NLYQKIFASH
60 70 80 90 100
FGHIAIIFLW TSGTLFHVAW QGNFEQWIKD PLNIRPIAHA IWDPHFGEGA
110 120 130 140 150
VNAFTQAGAS NPVNIAYSGV YHWFYTIGMT TNQELYSGAV FLLVLASLFL
160 170 180 190 200
FAGWLHLQPK FRPSLAWFKN AESRLNHHLA GLFGVSSLAW AGHLVHVAIP
210 220 230 240 250
EARGQHVGWD NFLSTPPHPA GLMPFFTGNW GVYAADPDTA GHIFGTSEGA
260 270 280 290 300
GTAILTFLGG FHPQTESLWL TDIAHHHLAI AVIFIIAGHM YRTNWGIGHS
310 320 330 340 350
IKEILNAHKG PLTGAGHTNL YDTINNSLHF QLGLALASLG VITSLVAQHM
360 370 380 390 400
YSLPSYAFIA QDHTTQAALY THHQYIAGFL MVGAFAHGAI FFVRDYDPVA
410 420 430 440 450
NKDNVLARML EHKEALISHL SWVSLFLGFH TLGLYVHNDV VVAFGTPEKQ
460 470 480 490 500
ILIEPVFAQW IQATSGKALY GFDVLLSNPD SIASTTGAAW LPGWLDAINS
510 520 530 540 550
GTNSLFLTIG PGDFLVHHAI ALGLHTTALI LIKGALDARG SKLMPDKKDF
560 570 580 590 600
GYSFPCDGPG RGGTCDISAW DAFYLAMFWM LNTLGWLTFY WHWKHLGVWS
610 620 630 640 650
GNVAQFNENS TYLMGWFRDY LWANSAQLIN GYNPYGVNNL SVWAWMFLFG
660 670 680 690 700
HLVWATGFMF LISWRGYWQE LIETIVWAHE RTPLANLVRW KDKPVALSIV
710 720 730
QARLVGLAHF TVGYVLTYAA FLIASTAGKF G
Length:731
Mass (Da):81,292
Last modified:January 23, 2007 - v4
<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:iBEED6B43CC5B3DD9
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 conflicti502T → I AA sequence (PubMed:9268309).Curated1
Sequence conflicti537 – 538DA → ES in CAA41630 (PubMed:1932686).Curated2

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
X58825 Genomic DNA Translation: CAA41630.1
BA000022 Genomic DNA Translation: BAA17438.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S18243

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAA17438; BAA17438; BAA17438

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
syn:slr1835

<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
X58825 Genomic DNA Translation: CAA41630.1
BA000022 Genomic DNA Translation: BAA17438.1
PIRiS18243

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
4KT0X-ray2.80B1-731[»]
4L6VX-ray3.802/B/b1-731[»]
6HQBX-ray4.00B1-731[»]
6NWAelectron microscopy3.48B/G/b1-731[»]
6UZVelectron microscopy3.102/B/b1-731[»]
SMRiP29255
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP29255, 3 interactors
STRINGi1148.1652517

Proteomic databases

PaxDbiP29255

Genome annotation databases

EnsemblBacteriaiBAA17438; BAA17438; BAA17438
KEGGisyn:slr1835

Phylogenomic databases

eggNOGiCOG2885, Bacteria
InParanoidiP29255
OMAiFEQWVAD
PhylomeDBiP29255

Enzyme and pathway databases

BioCyciMetaCyc:PSAB-MONOMER
BRENDAi1.97.1.12, 6192

Family and domain databases

Gene3Di1.20.1130.10, 1 hit
HAMAPiMF_00482, PSI_PsaB, 1 hit
InterProiView protein in InterPro
IPR001280, PSI_PsaA/B
IPR020586, PSI_PsaA/B_CS
IPR036408, PSI_PsaA/B_sf
IPR006244, PSI_PsaB
PfamiView protein in Pfam
PF00223, PsaA_PsaB, 1 hit
PIRSFiPIRSF002905, PSI_A, 1 hit
PRINTSiPR00257, PHOTSYSPSAAB
SUPFAMiSSF81558, SSF81558, 1 hit
TIGRFAMsiTIGR01336, psaB, 1 hit
PROSITEiView protein in PROSITE
PS00419, PHOTOSYSTEM_I_PSAAB, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiPSAB_SYNY3
<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: P29255
Secondary accession number(s): P73398
<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: December 1, 1992
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 162 of the entry and version 4 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, Reference proteome

Documents

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