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Entry version 32 (02 Jun 2021)
Sequence version 1 (13 Nov 2013)
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Protein

CRISPR-associated endonuclease Cas12a

Gene

cas12a

Organism
Acidaminococcus sp. (strain BV3L6)
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

CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Recognizes a short motif in the CRISPR repeat sequences (the 5' PAM or protospacer adjacent motif, TTTN in this organism) to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs (PubMed:26422227).

Has dsDNA endonuclease activity, results in staggered 4-base 5' overhangs 19 and 22 bases downstream of the PAM on the non-targeted and targeted strand respectively (PubMed:26422227).

Non-target strand cleavage by the RuvC domain is probably a prerequisite of target strand cleavage by the Nuc domain (PubMed:27114038).

In this CRISPR system correct processing of pre-crRNA requires only this protein and the CRISPR locus (By similarity).

By similarity2 Publications

Miscellaneous

Part of a type V-A CRISPR-Cas system.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei18Binds crRNA2 Publications1
Sitei167Binds PAM on target DNA2 Publications1
Sitei192Binds crRNA2 Publications1
Sitei382Binds crRNA-target DNA heteroduplex2 Publications1
Sitei548Binds PAM on target DNA2 Publications1
Sitei607Binds sequence-specific recognition of both target and non-target strand bases in PAM2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei800For pre-crRNA processingBy similarity1
Active sitei809For pre-crRNA processingBy similarity1
Active sitei860For pre-crRNA processingBy similarity1
Sitei872Binds crRNA2 Publications1
Active sitei908For DNase activity of RuvC domain1 Publication1
Active sitei993For DNase activity of RuvC domain1 Publication1
Sitei1014Binds target DNA1 Publication1
Active sitei1226For DNase activity of nuclease domain1 Publication1
Active sitei1263For DNase activity of RuvC domain1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi599 – 607PAM-binding on target DNA2 Publications9
DNA bindingi780 – 783Target DNA2 Publications4
DNA bindingi951 – 968Target DNA2 PublicationsAdd BLAST18
DNA bindingi1051 – 1053Target DNA2 Publications3

<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 functionDNA-binding, Endonuclease, Hydrolase, Lyase, Nuclease, RNA-binding
Biological processAntiviral defense
LigandMagnesium

<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%5Fand%5Ftaxonomy%5Fsection">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:
CRISPR-associated endonuclease Cas12a1 Publication (EC:3.1.21.1By similarity, EC:4.6.1.22By similarity)
Alternative name(s):
AsCpf11 Publication
CRISPR-associated endonuclease Cpf11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:cas12a1 Publication
Synonyms:cpf11 Publication
ORF Names:HMPREF1246_0236
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiAcidaminococcus sp. (strain BV3L6)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri1111120 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaFirmicutesNegativicutesAcidaminococcalesAcidaminococcaceaeAcidaminococcusunclassified Acidaminococcus

<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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

This class of CRISPR enzymes recognize a 5' T-rich protospacer adjacent motif (PAM, TTTN for this specific enzyme), unlike Cas9 enzymes which recognize 3' G-rich PAMs, thus this enzyme increases the possibilites for genome editing (PubMed:26422227). When appropriately expressed in a human cell line mediates human genome editing via indel formation; its T-rich PAM sequence may make it useful for engineering of AT-rich genomes or of regions such as scaffold-matrix attachment areas (PubMed:26422227, PubMed:27347757). It has also been engineered to recognize altered PAM sequences, which will enlarge its target scope (PubMed:28595896).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi167T → A: Wild-type to slightly improved guided indel formation. 1 Publication1
Mutagenesisi176R → A: Decreased guided indel formation. 1 Publication1
Mutagenesisi192R → A: Decreased guided indel formation. 1 Publication1
Mutagenesisi382W → A: Nearly complete loss of guided indel formation. 1 Publication1
Mutagenesisi548K → A: Decreased guided indel formation. 1 Publication1
Mutagenesisi604M → A: Decreased guided indel formation. 1 Publication1
Mutagenesisi607K → A: Nearly complete loss of guided indel formation, probable loss of PAM recognition. 1 Publication1
Mutagenesisi780K → A: Nearly complete loss of guided indel formation. 1 Publication1
Mutagenesisi783G → P: Complete loss of guided indel formation. 1 Publication1
Mutagenesisi908D → P: Complete loss of guided indel formation; neither DNA strand is cleaved in vitro. 1 Publication1
Mutagenesisi951R → A: Nearly complete loss of guided indel formation. 1 Publication1
Mutagenesisi955R → A: Partial loss of guided indel formation. 1 Publication1
Mutagenesisi958W → A: Partial loss of guided indel formation. 1 Publication1
Mutagenesisi993E → P: Complete loss of guided indel formation; neither DNA strand is cleaved in vitro. 1 Publication1
Mutagenesisi1226R → A: Nearly complete loss of guided indel formation; nickase cleaves only the non-target DNA strand in vitro. 1 Publication1
Mutagenesisi1228S → A: Wild-type to slightly improved guided indel formation. 1 Publication1
Mutagenesisi1235D → A: About half loss of guided indel formation. 1 Publication1
Mutagenesisi1263D → A: Nearly complete loss of guided indel formation; neither DNA strand is cleaved in vitro. 1 Publication1

<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 '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_00004349031 – 1307CRISPR-associated endonuclease Cas12aAdd BLAST1307

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:27114038).

2 Publications

<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

11307
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
U2UMQ6

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 35WED-I (OBD-I)2 PublicationsAdd BLAST35
Regioni36 – 320REC1 (helical-I)2 PublicationsAdd BLAST285
Regioni47 – 51crRNA-binding2 Publications5
Regioni175 – 176crRNA-binding2 Publications2
Regioni307 – 310crRNA-binding2 Publications4
Regioni321 – 526WED-II (helical-II)2 PublicationsAdd BLAST206
Regioni527 – 598WED-II (OBD-I)2 PublicationsAdd BLAST72
Regioni599 – 718PI (LHD)2 PublicationsAdd BLAST120
Regioni719 – 884WED-III (OBD-III)2 PublicationsAdd BLAST166
Regioni752 – 761crRNA-binding2 Publications10
Regioni806 – 808crRNA-binding1 Publication3
Regioni885 – 940RuvC-I2 PublicationsAdd BLAST56
Regioni941 – 957Bridge helix2 PublicationsAdd BLAST17
Regioni958 – 1066RuvC-II2 PublicationsAdd BLAST109
Regioni1067 – 1262Nuclease domain2 PublicationsAdd BLAST196
Regioni1263 – 1307RuvC-III2 PublicationsAdd BLAST45

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili74 – 106Sequence analysisAdd BLAST33

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Has a bilobed structure, with the REC lobe (residues 35-526) connected to the NUC lobe (residues 1-35 and 526-1307) by a discontinuous wedge domain (PubMed:27114038, PubMed:27444870). The crRNA-target DNA heteroduplex is bound in the channel between the 2 lobes (PubMed:27114038, PubMed:27444870). One nuclease site is found in the discontinuous RuvC domain which probably cuts target DNA strand in the crRNA-DNA heteroduplex (residues 884-940, 957-1066 and 1262-1307), the other in the NUC domain and probably cuts the non-target DNA strand outside the heteroduplex (residues 1067-1261) (PubMed:27114038). Target DNA binding induces domain movement (PubMed:27444870).2 Publications

<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 CRISPR-associated endonuclease Cas12a family.1 Publication

Keywords - Domaini

Coiled coil

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027620, Cas12a
IPR040882, Cas12a_NUC
IPR040787, Cas12a_REC1
IPR040852, RuvC_1

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18510, NUC, 1 hit
PF18501, REC1, 1 hit
PF18516, RuvC_1, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR04330, cas_Cpf1, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

U2UMQ6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTQFEGFTNL YQVSKTLRFE LIPQGKTLKH IQEQGFIEED KARNDHYKEL
60 70 80 90 100
KPIIDRIYKT YADQCLQLVQ LDWENLSAAI DSYRKEKTEE TRNALIEEQA
110 120 130 140 150
TYRNAIHDYF IGRTDNLTDA INKRHAEIYK GLFKAELFNG KVLKQLGTVT
160 170 180 190 200
TTEHENALLR SFDKFTTYFS GFYENRKNVF SAEDISTAIP HRIVQDNFPK
210 220 230 240 250
FKENCHIFTR LITAVPSLRE HFENVKKAIG IFVSTSIEEV FSFPFYNQLL
260 270 280 290 300
TQTQIDLYNQ LLGGISREAG TEKIKGLNEV LNLAIQKNDE TAHIIASLPH
310 320 330 340 350
RFIPLFKQIL SDRNTLSFIL EEFKSDEEVI QSFCKYKTLL RNENVLETAE
360 370 380 390 400
ALFNELNSID LTHIFISHKK LETISSALCD HWDTLRNALY ERRISELTGK
410 420 430 440 450
ITKSAKEKVQ RSLKHEDINL QEIISAAGKE LSEAFKQKTS EILSHAHAAL
460 470 480 490 500
DQPLPTTLKK QEEKEILKSQ LDSLLGLYHL LDWFAVDESN EVDPEFSARL
510 520 530 540 550
TGIKLEMEPS LSFYNKARNY ATKKPYSVEK FKLNFQMPTL ASGWDVNKEK
560 570 580 590 600
NNGAILFVKN GLYYLGIMPK QKGRYKALSF EPTEKTSEGF DKMYYDYFPD
610 620 630 640 650
AAKMIPKCST QLKAVTAHFQ THTTPILLSN NFIEPLEITK EIYDLNNPEK
660 670 680 690 700
EPKKFQTAYA KKTGDQKGYR EALCKWIDFT RDFLSKYTKT TSIDLSSLRP
710 720 730 740 750
SSQYKDLGEY YAELNPLLYH ISFQRIAEKE IMDAVETGKL YLFQIYNKDF
760 770 780 790 800
AKGHHGKPNL HTLYWTGLFS PENLAKTSIK LNGQAELFYR PKSRMKRMAH
810 820 830 840 850
RLGEKMLNKK LKDQKTPIPD TLYQELYDYV NHRLSHDLSD EARALLPNVI
860 870 880 890 900
TKEVSHEIIK DRRFTSDKFF FHVPITLNYQ AANSPSKFNQ RVNAYLKEHP
910 920 930 940 950
ETPIIGIDRG ERNLIYITVI DSTGKILEQR SLNTIQQFDY QKKLDNREKE
960 970 980 990 1000
RVAARQAWSV VGTIKDLKQG YLSQVIHEIV DLMIHYQAVV VLENLNFGFK
1010 1020 1030 1040 1050
SKRTGIAEKA VYQQFEKMLI DKLNCLVLKD YPAEKVGGVL NPYQLTDQFT
1060 1070 1080 1090 1100
SFAKMGTQSG FLFYVPAPYT SKIDPLTGFV DPFVWKTIKN HESRKHFLEG
1110 1120 1130 1140 1150
FDFLHYDVKT GDFILHFKMN RNLSFQRGLP GFMPAWDIVF EKNETQFDAK
1160 1170 1180 1190 1200
GTPFIAGKRI VPVIENHRFT GRYRDLYPAN ELIALLEEKG IVFRDGSNIL
1210 1220 1230 1240 1250
PKLLENDDSH AIDTMVALIR SVLQMRNSNA ATGEDYINSP VRDLNGVCFD
1260 1270 1280 1290 1300
SRFQNPEWPM DADANGAYHI ALKGQLLLNH LKESKDLKLQ NGISNQDWLA

YIQELRN
Length:1,307
Mass (Da):151,207
Last modified:November 13, 2013 - v1
<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:iCD5A76A624FEC1A8
GO

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
AWUR01000016 Genomic DNA Translation: ERL19323.1

NCBI Reference Sequences

More...
RefSeqi
WP_021736722.1, NZ_AWUR01000016.1

Genome annotation databases

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1111120.3.peg.776

<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
AWUR01000016 Genomic DNA Translation: ERL19323.1
RefSeqiWP_021736722.1, NZ_AWUR01000016.1

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
5B43X-ray2.80A1-1307[»]
5KK5X-ray3.29A1-1307[»]
5XH6X-ray2.00A1-1307[»]
5XH7X-ray2.00A1-1307[»]
SMRiU2UMQ6
ModBaseiSearch...
PDBe-KBiSearch...

Genome annotation databases

PATRICifig|1111120.3.peg.776

Family and domain databases

InterProiView protein in InterPro
IPR027620, Cas12a
IPR040882, Cas12a_NUC
IPR040787, Cas12a_REC1
IPR040852, RuvC_1
PfamiView protein in Pfam
PF18510, NUC, 1 hit
PF18501, REC1, 1 hit
PF18516, RuvC_1, 1 hit
TIGRFAMsiTIGR04330, cas_Cpf1, 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 nameiCS12A_ACISB
<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: U2UMQ6
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 9, 2015
Last sequence update: November 13, 2013
Last modified: June 2, 2021
This is version 32 of the entry and version 1 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

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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