Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adenosine deaminase CECR1

Gene

CECR1

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

Functioni

Adenosine deaminase that may contribute to the degradation of extracellular adenosine, a signaling molecule that controls a variety of cellular responses. Requires elevated adenosine levels for optimal enzyme activity. Binds to cell surfaces via proteoglycans and may play a role in the regulation of cell proliferation and differentiation, independently of its enzyme activity.2 Publications

Catalytic activityi

Adenosine + H2O = inosine + NH3.2 Publications

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Kineticsi

  1. KM=2.25 mM for adenosine1 Publication

    pH dependencei

    Optimum pH is 6.6.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi112Zinc; catalytic1
    Metal bindingi114Zinc; catalytic1
    Binding sitei115Substrate1
    Binding sitei293Substrate1
    Binding sitei326Substrate; via amide nitrogen1
    Metal bindingi356Zinc; catalytic1
    Active sitei359Proton donorCurated1
    Active sitei384Proton acceptorCurated1
    Metal bindingi441Zinc; catalytic1
    Binding sitei442Substrate1

    GO - Molecular functioni

    • adenosine deaminase activity Source: UniProtKB
    • adenosine receptor binding Source: UniProtKB
    • growth factor activity Source: UniProtKB
    • heparin binding Source: UniProtKB-KW
    • protein homodimerization activity Source: UniProtKB
    • proteoglycan binding Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • adenosine catabolic process Source: UniProtKB
    • cellular protein metabolic process Source: Reactome
    • hypoxanthine salvage Source: GO_Central
    • inosine biosynthetic process Source: GO_Central
    • multicellular organism development Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Heparin-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000093072-MONOMER.
    BRENDAi3.5.4.4. 2681.
    ReactomeiR-HSA-5683826. Surfactant metabolism.
    R-HSA-6798695. Neutrophil degranulation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenosine deaminase CECR1 (EC:3.5.4.4)
    Alternative name(s):
    Cat eye syndrome critical region protein 1
    Gene namesi
    Name:CECR1
    Synonyms:ADA2, ADGF, IDGFL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:1839. CECR1.

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: Reactome
    • extracellular space Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Polyarteritis nodosa (PAN)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA systemic necrotizing vasculitis that affects medium and small arteries. The ensuing tissue ischemia can affect any organ, including the skin, musculoskeletal system, kidneys, gastrointestinal tract, and the cardiovascular and nervous systems. Organ involvement and disease severity are highly variable. Clinical features include recurrent ischemic stroke affecting the small vessels of the brain and resulting in neurologic dysfunction, recurrent fever, myalgias, livedoid rash, gastrointestinal pain and hepatosplenomegaly.
    See also OMIM:615688
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07113747G → R in PAN; there is a decreased expression of the mutant protein compared to wild-type. 2 PublicationsCorresponds to variant rs202134424dbSNPEnsembl.1
    Natural variantiVAR_07113847G → V in PAN. 1 PublicationCorresponds to variant rs200930463dbSNPEnsembl.1
    Natural variantiVAR_071139109A → D in PAN. 1 PublicationCorresponds to variant rs587777240dbSNPEnsembl.1
    Natural variantiVAR_071140112H → Q in PAN. 1 PublicationCorresponds to variant rs587777241dbSNPEnsembl.1
    Natural variantiVAR_071141169R → Q in PAN. 2 PublicationsCorresponds to variant rs77563738dbSNPEnsembl.1
    Natural variantiVAR_071142251P → L in PAN. 1 PublicationCorresponds to variant rs148936893dbSNPEnsembl.1
    Natural variantiVAR_071143264W → S in PAN. 1 PublicationCorresponds to variant rs587777242dbSNPEnsembl.1
    Natural variantiVAR_071144453Y → C in PAN. 1 PublicationCorresponds to variant rs376785840dbSNPEnsembl.1
    Sneddon syndrome (SNDDS)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA systemic non-inflammatory thrombotic vasculopathy characterized by the association of livedo racemosa, and in some cases livedo reticularis, with cerebrovascular disease. Livedo racemosa is a persistent net-like violaceous-cyanotic, mottled discoloration of the skin affecting the legs, the arms, the buttocks and the trunk; livedo reticularis is limited to the extremities and is visible only in the cold. Cerebrovascular features include recurrent transient ischemic attacks, infarcts, and rarely spinal strokes or intracranial or subarachnoid hemorrhages. Headache and vertigo may precede the onset of livedo racemosa and cerebrovascular manifestations by several years. Rare neurologic symptoms include seizures, chorea, or myelopathies.
    See also OMIM:182410
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_072562119V → A in SNDDS. 1 Publication1
    Natural variantiVAR_072563142G → S in SNDDS. 1 Publication1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi137C → G: Abolishes secretion. 1 Publication1
    Mutagenesisi362W → G: Reduces dimerization and enzyme activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi51816.
    MalaCardsiCECR1.
    MIMi182410. phenotype.
    615688. phenotype.
    OpenTargetsiENSG00000093072.
    Orphaneti820. Sneddon syndrome.
    404553. Vasculitis due to ADA2 deficiency.
    PharmGKBiPA26382.

    Polymorphism and mutation databases

    DMDMi122065151.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 29Sequence analysisAdd BLAST29
    ChainiPRO_000000672530 – 511Adenosine deaminase CECR1Add BLAST482

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi127N-linked (GlcNAc...)1 Publication1
    Disulfide bondi137 ↔ 1591 Publication
    Glycosylationi174N-linked (GlcNAc...)1 Publication1
    Glycosylationi185N-linked (GlcNAc...)1 Publication1
    Glycosylationi378N-linked (GlcNAc...)2 Publications1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    EPDiQ9NZK5.
    MaxQBiQ9NZK5.
    PaxDbiQ9NZK5.
    PeptideAtlasiQ9NZK5.
    PRIDEiQ9NZK5.
    TopDownProteomicsiQ9NZK5-1. [Q9NZK5-1]

    PTM databases

    iPTMnetiQ9NZK5.
    PhosphoSitePlusiQ9NZK5.

    Expressioni

    Tissue specificityi

    Detected in blood plasma (at protein level). Widely expressed, with most abundant expression in human adult heart, lung, lymphoblasts, and placenta as well as fetal lung, liver, and kidney. In embryo, expressed in the outflow tract and atrium of the developing heart, the VII/VIII cranial nerve ganglion, and the notochord.1 Publication

    Gene expression databases

    BgeeiENSG00000093072.
    CleanExiHS_CECR1.
    ExpressionAtlasiQ9NZK5. baseline and differential.
    GenevisibleiQ9NZK5. HS.

    Organism-specific databases

    HPAiHPA007888.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with adenosine receptors. Binds heparin.2 Publications

    GO - Molecular functioni

    • adenosine receptor binding Source: UniProtKB
    • growth factor activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi119736. 1 interactor.
    STRINGi9606.ENSP00000262607.

    Structurei

    Secondary structure

    1511
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi30 – 44Combined sources15
    Turni46 – 49Combined sources4
    Helixi54 – 77Combined sources24
    Helixi81 – 83Combined sources3
    Helixi86 – 93Combined sources8
    Helixi97 – 104Combined sources8
    Beta strandi108 – 114Combined sources7
    Beta strandi117 – 119Combined sources3
    Helixi121 – 126Combined sources6
    Helixi128 – 130Combined sources3
    Beta strandi134 – 138Combined sources5
    Beta strandi144 – 148Combined sources5
    Helixi165 – 170Combined sources6
    Beta strandi171 – 173Combined sources3
    Helixi175 – 185Combined sources11
    Helixi193 – 196Combined sources4
    Helixi200 – 218Combined sources19
    Helixi221 – 237Combined sources17
    Beta strandi240 – 247Combined sources8
    Helixi262 – 279Combined sources18
    Beta strandi285 – 293Combined sources9
    Helixi298 – 314Combined sources17
    Turni316 – 318Combined sources3
    Beta strandi319 – 326Combined sources8
    Turni328 – 330Combined sources3
    Helixi335 – 337Combined sources3
    Helixi338 – 341Combined sources4
    Helixi343 – 346Combined sources4
    Turni366 – 369Combined sources4
    Helixi370 – 376Combined sources7
    Beta strandi380 – 384Combined sources5
    Helixi388 – 390Combined sources3
    Helixi392 – 400Combined sources9
    Beta strandi405 – 407Combined sources3
    Helixi409 – 414Combined sources6
    Helixi421 – 423Combined sources3
    Helixi426 – 431Combined sources6
    Beta strandi436 – 438Combined sources3
    Helixi443 – 446Combined sources4
    Helixi452 – 460Combined sources9
    Helixi469 – 481Combined sources13
    Beta strandi483 – 485Combined sources3
    Helixi487 – 509Combined sources23

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3LGDX-ray2.00A/B29-511[»]
    3LGGX-ray2.50A/B29-511[»]
    ProteinModelPortaliQ9NZK5.
    SMRiQ9NZK5.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NZK5.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni30 – 100DimerizationAdd BLAST71
    Regioni127 – 185PRB domainAdd BLAST59
    Regioni204 – 211Substrate binding8

    Domaini

    The PRB domain is involved in receptor binding, and may be responsible for the cytokine-like growth factor activity due to it's sharing of several structural properties with chemokines.1 Publication
    High-affinity binding to heparin/glycosaminoclycan (GAG) is mediated by a large, highly positively charged surface at the interface of dimer's subunits involving approximately residues 30-45, 389-396, and 422-428.1 Publication

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG1097. Eukaryota.
    COG1816. LUCA.
    GeneTreeiENSGT00390000012118.
    HOGENOMiHOG000044097.
    HOVERGENiHBG050883.
    InParanoidiQ9NZK5.
    KOiK19572.
    OMAiNTFMEIW.
    OrthoDBiEOG091G0CQY.
    PhylomeDBiQ9NZK5.
    TreeFamiTF324524.

    Family and domain databases

    InterProiIPR001365. A/AMP_deaminase_dom.
    IPR013659. A_deaminase_N.
    IPR006331. ADGF.
    IPR032466. Metal_Hydrolase.
    [Graphical view]
    PfamiPF00962. A_deaminase. 1 hit.
    PF08451. A_deaminase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51556. SSF51556. 1 hit.
    TIGRFAMsiTIGR01431. adm_rel. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

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

    Isoform 1 (identifier: Q9NZK5-1) [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
    MLVDGPSERP ALCFLLLAVA MSFFGSALSI DETRAHLLLK EKMMRLGGRL
    60 70 80 90 100
    VLNTKEELAN ERLMTLKIAE MKEAMRTLIF PPSMHFFQAK HLIERSQVFN
    110 120 130 140 150
    ILRMMPKGAA LHLHDIGIVT MDWLVRNVTY RPHCHICFTP RGIMQFRFAH
    160 170 180 190 200
    PTPRPSEKCS KWILLEDYRK RVQNVTEFDD SLLRNFTLVT QHPEVIYTNQ
    210 220 230 240 250
    NVVWSKFETI FFTISGLIHY APVFRDYVFR SMQEFYEDNV LYMEIRARLL
    260 270 280 290 300
    PVYELSGEHH DEEWSVKTYQ EVAQKFVETH PEFIGIKIIY SDHRSKDVAV
    310 320 330 340 350
    IAESIRMAMG LRIKFPTVVA GFDLVGHEDT GHSLHDYKEA LMIPAKDGVK
    360 370 380 390 400
    LPYFFHAGET DWQGTSIDRN ILDALMLNTT RIGHGFALSK HPAVRTYSWK
    410 420 430 440 450
    KDIPIEVCPI SNQVLKLVSD LRNHPVATLM ATGHPMVISS DDPAMFGAKG
    460 470 480 490 500
    LSYDFYEVFM GIGGMKADLR TLKQLAMNSI KYSTLLESEK NTFMEIWKKR
    510
    WDKFIADVAT K
    Length:511
    Mass (Da):58,934
    Last modified:January 9, 2007 - v2
    Checksum:iA4AB0A83E8A0611E
    GO
    Isoform 2 (identifier: Q9NZK5-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-241: Missing.
         242-251: YMEIRARLLP → MDSLEWNWAL

    Show »
    Length:270
    Mass (Da):30,668
    Checksum:iC526359224344500
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti359E → G in BAC11148 (PubMed:14702039).Curated1
    Sequence conflicti394V → L in AAH51755 (PubMed:15489334).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07113747G → R in PAN; there is a decreased expression of the mutant protein compared to wild-type. 2 PublicationsCorresponds to variant rs202134424dbSNPEnsembl.1
    Natural variantiVAR_07113847G → V in PAN. 1 PublicationCorresponds to variant rs200930463dbSNPEnsembl.1
    Natural variantiVAR_071139109A → D in PAN. 1 PublicationCorresponds to variant rs587777240dbSNPEnsembl.1
    Natural variantiVAR_071140112H → Q in PAN. 1 PublicationCorresponds to variant rs587777241dbSNPEnsembl.1
    Natural variantiVAR_072562119V → A in SNDDS. 1 Publication1
    Natural variantiVAR_072563142G → S in SNDDS. 1 Publication1
    Natural variantiVAR_071141169R → Q in PAN. 2 PublicationsCorresponds to variant rs77563738dbSNPEnsembl.1
    Natural variantiVAR_071142251P → L in PAN. 1 PublicationCorresponds to variant rs148936893dbSNPEnsembl.1
    Natural variantiVAR_071143264W → S in PAN. 1 PublicationCorresponds to variant rs587777242dbSNPEnsembl.1
    Natural variantiVAR_029802335H → R.2 PublicationsCorresponds to variant rs2231495dbSNPEnsembl.1
    Natural variantiVAR_071144453Y → C in PAN. 1 PublicationCorresponds to variant rs376785840dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0415091 – 241Missing in isoform 2. 1 PublicationAdd BLAST241
    Alternative sequenceiVSP_041510242 – 251YMEIRARLLP → MDSLEWNWAL in isoform 2. 1 Publication10

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF190746 mRNA. Translation: AAF65941.1.
    CR456417 mRNA. Translation: CAG30303.1.
    AK027682 mRNA. Translation: BAB55293.1.
    AK292689 mRNA. Translation: BAF85378.1.
    AK074702 mRNA. Translation: BAC11148.1.
    AC005300 Genomic DNA. No translation available.
    CH471193 Genomic DNA. Translation: EAW57750.1.
    BC051755 mRNA. Translation: AAH51755.1.
    CCDSiCCDS13742.1. [Q9NZK5-1]
    CCDS13743.1. [Q9NZK5-2]
    RefSeqiNP_001269154.1. NM_001282225.1. [Q9NZK5-1]
    NP_001269155.1. NM_001282226.1. [Q9NZK5-1]
    NP_001269156.1. NM_001282227.1.
    NP_001269157.1. NM_001282228.1.
    NP_001269158.1. NM_001282229.1.
    NP_803124.1. NM_177405.2. [Q9NZK5-2]
    XP_011544435.1. XM_011546133.1. [Q9NZK5-1]
    UniGeneiHs.170310.
    Hs.637274.

    Genome annotation databases

    EnsembliENST00000262607; ENSP00000262607; ENSG00000093072. [Q9NZK5-1]
    ENST00000330232; ENSP00000332871; ENSG00000093072. [Q9NZK5-2]
    ENST00000399837; ENSP00000382731; ENSG00000093072. [Q9NZK5-1]
    ENST00000399839; ENSP00000382733; ENSG00000093072. [Q9NZK5-1]
    GeneIDi51816.
    KEGGihsa:51816.
    UCSCiuc002zmj.3. human. [Q9NZK5-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF190746 mRNA. Translation: AAF65941.1.
    CR456417 mRNA. Translation: CAG30303.1.
    AK027682 mRNA. Translation: BAB55293.1.
    AK292689 mRNA. Translation: BAF85378.1.
    AK074702 mRNA. Translation: BAC11148.1.
    AC005300 Genomic DNA. No translation available.
    CH471193 Genomic DNA. Translation: EAW57750.1.
    BC051755 mRNA. Translation: AAH51755.1.
    CCDSiCCDS13742.1. [Q9NZK5-1]
    CCDS13743.1. [Q9NZK5-2]
    RefSeqiNP_001269154.1. NM_001282225.1. [Q9NZK5-1]
    NP_001269155.1. NM_001282226.1. [Q9NZK5-1]
    NP_001269156.1. NM_001282227.1.
    NP_001269157.1. NM_001282228.1.
    NP_001269158.1. NM_001282229.1.
    NP_803124.1. NM_177405.2. [Q9NZK5-2]
    XP_011544435.1. XM_011546133.1. [Q9NZK5-1]
    UniGeneiHs.170310.
    Hs.637274.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3LGDX-ray2.00A/B29-511[»]
    3LGGX-ray2.50A/B29-511[»]
    ProteinModelPortaliQ9NZK5.
    SMRiQ9NZK5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119736. 1 interactor.
    STRINGi9606.ENSP00000262607.

    PTM databases

    iPTMnetiQ9NZK5.
    PhosphoSitePlusiQ9NZK5.

    Polymorphism and mutation databases

    DMDMi122065151.

    Proteomic databases

    EPDiQ9NZK5.
    MaxQBiQ9NZK5.
    PaxDbiQ9NZK5.
    PeptideAtlasiQ9NZK5.
    PRIDEiQ9NZK5.
    TopDownProteomicsiQ9NZK5-1. [Q9NZK5-1]

    Protocols and materials databases

    DNASUi51816.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000262607; ENSP00000262607; ENSG00000093072. [Q9NZK5-1]
    ENST00000330232; ENSP00000332871; ENSG00000093072. [Q9NZK5-2]
    ENST00000399837; ENSP00000382731; ENSG00000093072. [Q9NZK5-1]
    ENST00000399839; ENSP00000382733; ENSG00000093072. [Q9NZK5-1]
    GeneIDi51816.
    KEGGihsa:51816.
    UCSCiuc002zmj.3. human. [Q9NZK5-1]

    Organism-specific databases

    CTDi51816.
    DisGeNETi51816.
    GeneCardsiCECR1.
    HGNCiHGNC:1839. CECR1.
    HPAiHPA007888.
    MalaCardsiCECR1.
    MIMi182410. phenotype.
    607575. gene.
    615688. phenotype.
    neXtProtiNX_Q9NZK5.
    OpenTargetsiENSG00000093072.
    Orphaneti820. Sneddon syndrome.
    404553. Vasculitis due to ADA2 deficiency.
    PharmGKBiPA26382.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1097. Eukaryota.
    COG1816. LUCA.
    GeneTreeiENSGT00390000012118.
    HOGENOMiHOG000044097.
    HOVERGENiHBG050883.
    InParanoidiQ9NZK5.
    KOiK19572.
    OMAiNTFMEIW.
    OrthoDBiEOG091G0CQY.
    PhylomeDBiQ9NZK5.
    TreeFamiTF324524.

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000093072-MONOMER.
    BRENDAi3.5.4.4. 2681.
    ReactomeiR-HSA-5683826. Surfactant metabolism.
    R-HSA-6798695. Neutrophil degranulation.

    Miscellaneous databases

    EvolutionaryTraceiQ9NZK5.
    GeneWikiiCECR1.
    GenomeRNAii51816.
    PROiQ9NZK5.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000093072.
    CleanExiHS_CECR1.
    ExpressionAtlasiQ9NZK5. baseline and differential.
    GenevisibleiQ9NZK5. HS.

    Family and domain databases

    InterProiIPR001365. A/AMP_deaminase_dom.
    IPR013659. A_deaminase_N.
    IPR006331. ADGF.
    IPR032466. Metal_Hydrolase.
    [Graphical view]
    PfamiPF00962. A_deaminase. 1 hit.
    PF08451. A_deaminase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51556. SSF51556. 1 hit.
    TIGRFAMsiTIGR01431. adm_rel. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCECR1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZK5
    Secondary accession number(s): A8K9H4
    , Q6ICF1, Q86UB6, Q8NCJ2, Q96K41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: January 9, 2007
    Last modified: November 30, 2016
    This is version 132 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

    Miscellaneous

    Candidate gene for the Cat Eye Syndrome (CES), a developmental disorder associated with the duplication of a 2 Mb region of 22q11.2. Duplication usually takes in the form of a surpernumerary bisatellited isodicentric chromosome, resulting in four copies of the region (represents an inv dup(22)(q11)). CES is characterized clinically by the combination of coloboma of the iris and anal atresia with fistula, downslanting palpebral fissures, preauricular tags and/or pits, frequent occurrence of heart and renal malformations, and normal or near-normal mental development.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. 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.