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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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi112 – 1121Zinc; catalytic
    Metal bindingi114 – 1141Zinc; catalytic
    Binding sitei115 – 1151Substrate
    Binding sitei293 – 2931Substrate
    Binding sitei326 – 3261Substrate; via amide nitrogen
    Metal bindingi356 – 3561Zinc; catalytic
    Active sitei359 – 3591Proton donorCurated
    Active sitei384 – 3841Proton acceptorCurated
    Metal bindingi441 – 4411Zinc; catalytic
    Binding sitei442 – 4421Substrate

    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

    BRENDAi3.5.4.4. 2681.
    ReactomeiR-HSA-5683826. Surfactant metabolism.

    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471G → R in PAN; there is a decreased expression of the mutant protein compared to wild-type. 2 Publications
    VAR_071137
    Natural varianti47 – 471G → V in PAN. 1 Publication
    VAR_071138
    Natural varianti109 – 1091A → D in PAN. 1 Publication
    VAR_071139
    Natural varianti112 – 1121H → Q in PAN. 1 Publication
    VAR_071140
    Natural varianti169 – 1691R → Q in PAN. 2 Publications
    VAR_071141
    Natural varianti251 – 2511P → L in PAN. 1 Publication
    VAR_071142
    Natural varianti264 – 2641W → S in PAN. 1 Publication
    VAR_071143
    Natural varianti453 – 4531Y → C in PAN. 1 Publication
    VAR_071144
    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti119 – 1191V → A in SNDDS. 1 Publication
    VAR_072562
    Natural varianti142 – 1421G → S in SNDDS. 1 Publication
    VAR_072563

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi137 – 1371C → G: Abolishes secretion. 1 Publication
    Mutagenesisi362 – 3621W → G: Reduces dimerization and enzyme activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

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

    Polymorphism and mutation databases

    DMDMi122065151.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence analysisAdd
    BLAST
    Chaini30 – 511482Adenosine deaminase CECR1PRO_0000006725Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi127 – 1271N-linked (GlcNAc...)1 Publication
    Disulfide bondi137 ↔ 1591 Publication
    Glycosylationi174 – 1741N-linked (GlcNAc...)1 Publication
    Glycosylationi185 – 1851N-linked (GlcNAc...)1 Publication
    Glycosylationi378 – 3781N-linked (GlcNAc...)2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

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

    PTM databases

    PhosphoSiteiQ9NZK5.

    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

    BgeeiQ9NZK5.
    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
    • proteoglycan binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi119736. 1 interaction.
    STRINGi9606.ENSP00000262607.

    Structurei

    Secondary structure

    1
    511
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 4415Combined sources
    Turni46 – 494Combined sources
    Helixi54 – 7724Combined sources
    Helixi81 – 833Combined sources
    Helixi86 – 938Combined sources
    Helixi97 – 1048Combined sources
    Beta strandi108 – 1147Combined sources
    Beta strandi117 – 1193Combined sources
    Helixi121 – 1266Combined sources
    Helixi128 – 1303Combined sources
    Beta strandi134 – 1385Combined sources
    Beta strandi144 – 1485Combined sources
    Helixi165 – 1706Combined sources
    Beta strandi171 – 1733Combined sources
    Helixi175 – 18511Combined sources
    Helixi193 – 1964Combined sources
    Helixi200 – 21819Combined sources
    Helixi221 – 23717Combined sources
    Beta strandi240 – 2478Combined sources
    Helixi262 – 27918Combined sources
    Beta strandi285 – 2939Combined sources
    Helixi298 – 31417Combined sources
    Turni316 – 3183Combined sources
    Beta strandi319 – 3268Combined sources
    Turni328 – 3303Combined sources
    Helixi335 – 3373Combined sources
    Helixi338 – 3414Combined sources
    Helixi343 – 3464Combined sources
    Turni366 – 3694Combined sources
    Helixi370 – 3767Combined sources
    Beta strandi380 – 3845Combined sources
    Helixi388 – 3903Combined sources
    Helixi392 – 4009Combined sources
    Beta strandi405 – 4073Combined sources
    Helixi409 – 4146Combined sources
    Helixi421 – 4233Combined sources
    Helixi426 – 4316Combined sources
    Beta strandi436 – 4383Combined sources
    Helixi443 – 4464Combined sources
    Helixi452 – 4609Combined sources
    Helixi469 – 48113Combined sources
    Beta strandi483 – 4853Combined sources
    Helixi487 – 50923Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LGDX-ray2.00A/B29-511[»]
    3LGGX-ray2.50A/B29-511[»]
    ProteinModelPortaliQ9NZK5.
    SMRiQ9NZK5. Positions 29-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NZK5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 10071DimerizationAdd
    BLAST
    Regioni127 – 18559PRB domainAdd
    BLAST
    Regioni204 – 2118Substrate binding

    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.
    OMAiNVLYMEI.
    OrthoDBiEOG77WWCN.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti359 – 3591E → G in BAC11148 (PubMed:14702039).Curated
    Sequence conflicti394 – 3941V → L in AAH51755 (PubMed:15489334).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471G → R in PAN; there is a decreased expression of the mutant protein compared to wild-type. 2 Publications
    VAR_071137
    Natural varianti47 – 471G → V in PAN. 1 Publication
    VAR_071138
    Natural varianti109 – 1091A → D in PAN. 1 Publication
    VAR_071139
    Natural varianti112 – 1121H → Q in PAN. 1 Publication
    VAR_071140
    Natural varianti119 – 1191V → A in SNDDS. 1 Publication
    VAR_072562
    Natural varianti142 – 1421G → S in SNDDS. 1 Publication
    VAR_072563
    Natural varianti169 – 1691R → Q in PAN. 2 Publications
    VAR_071141
    Natural varianti251 – 2511P → L in PAN. 1 Publication
    VAR_071142
    Natural varianti264 – 2641W → S in PAN. 1 Publication
    VAR_071143
    Natural varianti335 – 3351H → R.2 Publications
    Corresponds to variant rs2231495 [ dbSNP | Ensembl ].
    VAR_029802
    Natural varianti453 – 4531Y → C in PAN. 1 Publication
    VAR_071144

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 241241Missing in isoform 2. 1 PublicationVSP_041509Add
    BLAST
    Alternative sequencei242 – 25110YMEIRARLLP → MDSLEWNWAL in isoform 2. 1 PublicationVSP_041510

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LGDX-ray2.00A/B29-511[»]
    3LGGX-ray2.50A/B29-511[»]
    ProteinModelPortaliQ9NZK5.
    SMRiQ9NZK5. Positions 29-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119736. 1 interaction.
    STRINGi9606.ENSP00000262607.

    PTM databases

    PhosphoSiteiQ9NZK5.

    Polymorphism and mutation databases

    DMDMi122065151.

    Proteomic databases

    MaxQBiQ9NZK5.
    PaxDbiQ9NZK5.
    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.
    GeneCardsiCECR1.
    HGNCiHGNC:1839. CECR1.
    HPAiHPA007888.
    MalaCardsiCECR1.
    MIMi182410. phenotype.
    607575. gene.
    615688. phenotype.
    neXtProtiNX_Q9NZK5.
    Orphaneti820. Sneddon syndrome.
    404553. Vasculitis due to ADA2 deficiency.
    PharmGKBiPA26382.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1097. Eukaryota.
    COG1816. LUCA.
    GeneTreeiENSGT00390000012118.
    HOGENOMiHOG000044097.
    HOVERGENiHBG050883.
    InParanoidiQ9NZK5.
    KOiK19572.
    OMAiNVLYMEI.
    OrthoDBiEOG77WWCN.
    PhylomeDBiQ9NZK5.
    TreeFamiTF324524.

    Enzyme and pathway databases

    BRENDAi3.5.4.4. 2681.
    ReactomeiR-HSA-5683826. Surfactant metabolism.

    Miscellaneous databases

    EvolutionaryTraceiQ9NZK5.
    GeneWikiiCECR1.
    GenomeRNAii51816.
    NextBioi55944.
    PROiQ9NZK5.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NZK5.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "The human homolog of insect-derived growth factor, CECR1, is a candidate gene for features of cat eye syndrome."
      Riazi M.A., Brinkman-Mills P., Nguyen T., Pan H., Phan S., Ying F., Roe B.A., Tochigi J., Shimizu Y., Minoshima S., Shimizu N., Buchwald M., McDermid H.E.
      Genomics 64:277-285(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-335.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ARG-335.
      Tissue: Thymus.
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    7. "Human ADA2 belongs to a new family of growth factors with adenosine deaminase activity."
      Zavialov A.V., Engstroem A.
      Biochem. J. 391:51-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, HEPARIN-BINDING, SUBCELLULAR LOCATION.
    8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174 AND ASN-378.
      Tissue: Liver.
    9. "Human adenosine deaminase 2 induces differentiation of monocytes into macrophages and stimulates proliferation of T helper cells and macrophages."
      Zavialov A.V., Gracia E., Glaichenhaus N., Franco R., Zavialov A.V., Lauvau G.
      J. Leukoc. Biol. 88:279-290(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, HEPARIN-BINDING, SUBUNIT.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Structural basis for the growth factor activity of human adenosine deaminase ADA2."
      Zavialov A.V., Yu X., Spillmann D., Lauvau G., Zavialov A.V.
      J. Biol. Chem. 285:12367-12377(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-511 IN COMPLEX WITH ZINC IONS AND TRANSITION STATE ANALOG COFORMYCIN, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, SUBUNIT, DISULFIDE BOND, DOMAINS, GLYCOSAMINOCLYCAN BINDING, MUTAGENESIS OF CYS-137 AND TRP-362, GLYCOSYLATION AT ASN-127; ASN-185 AND ASN-378.
    12. "Early-onset stroke and vasculopathy associated with mutations in ADA2."
      Zhou Q., Yang D., Ombrello A.K., Zavialov A.V., Toro C., Zavialov A.V., Stone D.L., Chae J.J., Rosenzweig S.D., Bishop K., Barron K.S., Kuehn H.S., Hoffmann P., Negro A., Tsai W.L., Cowen E.W., Pei W., Milner J.D.
      , Silvin C., Heller T., Chin D.T., Patronas N.J., Barber J.S., Lee C.C., Wood G.M., Ling A., Kelly S.J., Kleiner D.E., Mullikin J.C., Ganson N.J., Kong H.H., Hambleton S., Candotti F., Quezado M.M., Calvo K.R., Alao H., Barham B.K., Jones A., Meschia J.F., Worrall B.B., Kasner S.E., Rich S.S., Goldbach-Mansky R., Abinun M., Chalom E., Gotte A.C., Punaro M., Pascual V., Verbsky J.W., Torgerson T.R., Singer N.G., Gershon T.R., Ozen S., Karadag O., Fleisher T.A., Remmers E.F., Burgess S.M., Moir S.L., Gadina M., Sood R., Hershfield M.S., Boehm M., Kastner D.L., Aksentijevich I.
      N. Engl. J. Med. 370:911-920(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PAN, VARIANTS PAN ARG-47; ASP-109; GLN-112; GLN-169 AND CYS-453.
    13. Cited for: VARIANTS PAN VAL-47; ARG-47; GLN-169; LEU-251 AND SER-264.
    14. Cited for: INVOLVEMENT IN SNDDS, VARIANTS SNDDS ALA-119 AND SER-142.

    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: May 11, 2016
    This is version 127 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.