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Protein

Isoaspartyl peptidase/L-asparaginase

Gene

ASRGL1

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

Functioni

Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.1 Publication

Catalytic activityi

L-asparagine + H2O = L-aspartate + NH3.
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.

Enzyme regulationi

Glycine accelerates autocleavage into an alpha and beta chain.1 Publication

Kineticsi

  1. KM=3.4 mM for L-asparagine (L-Asn)1 Publication
  2. KM=0.4 mM for L-aspartic acid beta-methyl ester1 Publication
  3. KM=0.4 mM for L-Asp-L-Phe1 Publication
  4. KM=1.0 mM for L-Asp-L-Ala1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei168 – 1681Nucleophile2 Publications

    GO - Molecular functioni

    • asparaginase activity Source: UniProtKB
    • beta-aspartyl-peptidase activity Source: UniProtKB

    GO - Biological processi

    • asparagine catabolic process via L-aspartate Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease

    Enzyme and pathway databases

    BRENDAi3.4.19.5. 2681.

    Protein family/group databases

    MEROPSiT02.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoaspartyl peptidase/L-asparaginase (EC:3.4.19.5, EC:3.5.1.1)
    Alternative name(s):
    Asparaginase-like protein 1
    Beta-aspartyl-peptidase
    Isoaspartyl dipeptidase
    L-asparagine amidohydrolase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:ASRGL1
    Synonyms:ALP, CRASH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:16448. ASRGL1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi168 – 1681T → A or C: Abolishes activation by autocleavage. Abolishes enzyme activity. 2 Publications
    Mutagenesisi168 – 1681T → S: Strongly reduced enzyme activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA25059.

    Chemistry

    DrugBankiDB00174. L-Asparagine.
    DB00128. L-Aspartic Acid.

    Polymorphism and mutation databases

    BioMutaiASRGL1.
    DMDMi158706477.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 167167Isoaspartyl peptidase/L-asparaginase alpha chainPRO_0000305204Add
    BLAST
    Chaini168 – 308141Isoaspartyl peptidase/L-asparaginase beta chainPRO_0000420556Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Post-translational modificationi

    Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.

    Keywords - PTMi

    Acetylation, Autocatalytic cleavage

    Proteomic databases

    MaxQBiQ7L266.
    PaxDbiQ7L266.
    PRIDEiQ7L266.

    2D gel databases

    UCD-2DPAGEQ7L266.

    PTM databases

    PhosphoSiteiQ7L266.

    Expressioni

    Tissue specificityi

    Expressed in brain, kidney, testis and tissues of the gastrointestinal tract. Present in sperm (at protein level). Over-expressed in uterine, mammary, prostatic and ovarian carcinoma.2 Publications

    Inductioni

    By 5-alpha-di-hydrotestosterone and progesterone.1 Publication

    Gene expression databases

    BgeeiQ7L266.
    CleanExiHS_ASRGL1.
    ExpressionAtlasiQ7L266. baseline and differential.
    GenevisibleiQ7L266. HS.

    Organism-specific databases

    HPAiHPA029725.
    HPA055572.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi123142. 5 interactions.
    IntActiQ7L266. 4 interactions.
    STRINGi9606.ENSP00000301776.

    Structurei

    Secondary structure

    1
    308
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85Combined sources
    Helixi17 – 3822Combined sources
    Turni39 – 413Combined sources
    Helixi44 – 5714Combined sources
    Beta strandi61 – 644Combined sources
    Beta strandi71 – 733Combined sources
    Beta strandi77 – 837Combined sources
    Turni84 – 863Combined sources
    Beta strandi89 – 957Combined sources
    Helixi101 – 11111Combined sources
    Beta strandi115 – 1184Combined sources
    Helixi119 – 12810Combined sources
    Helixi136 – 1383Combined sources
    Helixi142 – 15211Combined sources
    Beta strandi169 – 1746Combined sources
    Beta strandi180 – 1867Combined sources
    Turni203 – 2053Combined sources
    Beta strandi206 – 2105Combined sources
    Turni211 – 2133Combined sources
    Beta strandi214 – 2207Combined sources
    Helixi222 – 2287Combined sources
    Helixi230 – 23910Combined sources
    Helixi244 – 25916Combined sources
    Beta strandi263 – 2697Combined sources
    Beta strandi274 – 2829Combined sources
    Beta strandi285 – 2895Combined sources
    Beta strandi292 – 2987Combined sources
    Beta strandi303 – 3064Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3TKJX-ray2.30A/B2-308[»]
    4ET0X-ray3.30A/B2-308[»]
    4O0CX-ray1.50A/B1-308[»]
    4O0DX-ray1.95A/B1-308[»]
    4O0EX-ray1.71A/B1-308[»]
    4O0FX-ray1.92A/B1-308[»]
    4O0GX-ray2.10A/B1-308[»]
    4O0HX-ray1.97A/B1-308[»]
    4OSXX-ray1.95A/B1-308[»]
    4OSYX-ray1.91A/B1-308[»]
    4PVPX-ray1.85A/B1-308[»]
    4PVQX-ray2.13A/B1-308[»]
    4PVRX-ray1.75A/B1-308[»]
    4PVSX-ray1.84A/B1-308[»]
    ProteinModelPortaliQ7L266.
    SMRiQ7L266. Positions 1-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni196 – 1994Substrate binding
    Regioni219 – 2224Substrate binding

    Sequence similaritiesi

    Belongs to the Ntn-hydrolase family.Curated

    Phylogenomic databases

    eggNOGiCOG1446.
    GeneTreeiENSGT00530000063034.
    HOGENOMiHOG000174613.
    HOVERGENiHBG101662.
    InParanoidiQ7L266.
    KOiK13051.
    OMAiPCVGAGG.
    OrthoDBiEOG7TBC2N.
    PhylomeDBiQ7L266.
    TreeFamiTF323960.

    Family and domain databases

    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000246. Peptidase_T2.
    [Graphical view]
    PANTHERiPTHR10188. PTHR10188. 1 hit.
    PfamiPF01112. Asparaginase_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 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: Q7L266-1) [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
    MNPIVVVHGG GAGPISKDRK ERVHQGMVRA ATVGYGILRE GGSAVDAVEG
    60 70 80 90 100
    AVVALEDDPE FNAGCGSVLN TNGEVEMDAS IMDGKDLSAG AVSAVQCIAN
    110 120 130 140 150
    PIKLARLVME KTPHCFLTDQ GAAQFAAAMG VPEIPGEKLV TERNKKRLEK
    160 170 180 190 200
    EKHEKGAQKT DCQKNLGTVG AVALDCKGNV AYATSTGGIV NKMVGRVGDS
    210 220 230 240 250
    PCLGAGGYAD NDIGAVSTTG HGESILKVNL ARLTLFHIEQ GKTVEEAADL
    260 270 280 290 300
    SLGYMKSRVK GLGGLIVVSK TGDWVAKWTS TSMPWAAAKD GKLHFGIDPD

    DTTITDLP
    Length:308
    Mass (Da):32,055
    Last modified:April 3, 2007 - v2
    Checksum:i84E3D6C2D1555B32
    GO
    Isoform 2 (identifier: Q7L266-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-128: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:180
    Mass (Da):18,981
    Checksum:iE21C4620A2261D0C
    GO

    Sequence cautioni

    The sequence BAB15302.1 differs from that shown.Contaminating sequence.Curated
    The sequence BAB15302.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811A → T in AAM28434 (PubMed:11984834).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 128128Missing in isoform 2. 1 PublicationVSP_028287Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF411076 mRNA. Translation: AAM28434.1.
    AK025969 mRNA. Translation: BAB15302.1. Different initiation.
    AK091894 mRNA. Translation: BAG52437.1.
    AK313069 mRNA. Translation: BAG35897.1.
    CH471076 Genomic DNA. Translation: EAW74012.1.
    BC021295 mRNA. Translation: AAH21295.3.
    BC064963 mRNA. Translation: AAH64963.1.
    BC093070 mRNA. Translation: AAH93070.1.
    CCDSiCCDS8019.1. [Q7L266-1]
    RefSeqiNP_001077395.1. NM_001083926.1. [Q7L266-1]
    NP_079356.3. NM_025080.3. [Q7L266-1]
    XP_005274362.1. XM_005274305.2. [Q7L266-2]
    XP_005274363.1. XM_005274306.2. [Q7L266-2]
    UniGeneiHs.535326.

    Genome annotation databases

    EnsembliENST00000301776; ENSP00000301776; ENSG00000162174.
    ENST00000415229; ENSP00000400057; ENSG00000162174.
    GeneIDi80150.
    KEGGihsa:80150.
    UCSCiuc001nte.4. human. [Q7L266-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF411076 mRNA. Translation: AAM28434.1.
    AK025969 mRNA. Translation: BAB15302.1. Different initiation.
    AK091894 mRNA. Translation: BAG52437.1.
    AK313069 mRNA. Translation: BAG35897.1.
    CH471076 Genomic DNA. Translation: EAW74012.1.
    BC021295 mRNA. Translation: AAH21295.3.
    BC064963 mRNA. Translation: AAH64963.1.
    BC093070 mRNA. Translation: AAH93070.1.
    CCDSiCCDS8019.1. [Q7L266-1]
    RefSeqiNP_001077395.1. NM_001083926.1. [Q7L266-1]
    NP_079356.3. NM_025080.3. [Q7L266-1]
    XP_005274362.1. XM_005274305.2. [Q7L266-2]
    XP_005274363.1. XM_005274306.2. [Q7L266-2]
    UniGeneiHs.535326.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3TKJX-ray2.30A/B2-308[»]
    4ET0X-ray3.30A/B2-308[»]
    4O0CX-ray1.50A/B1-308[»]
    4O0DX-ray1.95A/B1-308[»]
    4O0EX-ray1.71A/B1-308[»]
    4O0FX-ray1.92A/B1-308[»]
    4O0GX-ray2.10A/B1-308[»]
    4O0HX-ray1.97A/B1-308[»]
    4OSXX-ray1.95A/B1-308[»]
    4OSYX-ray1.91A/B1-308[»]
    4PVPX-ray1.85A/B1-308[»]
    4PVQX-ray2.13A/B1-308[»]
    4PVRX-ray1.75A/B1-308[»]
    4PVSX-ray1.84A/B1-308[»]
    ProteinModelPortaliQ7L266.
    SMRiQ7L266. Positions 1-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi123142. 5 interactions.
    IntActiQ7L266. 4 interactions.
    STRINGi9606.ENSP00000301776.

    Chemistry

    DrugBankiDB00174. L-Asparagine.
    DB00128. L-Aspartic Acid.

    Protein family/group databases

    MEROPSiT02.002.

    PTM databases

    PhosphoSiteiQ7L266.

    Polymorphism and mutation databases

    BioMutaiASRGL1.
    DMDMi158706477.

    2D gel databases

    UCD-2DPAGEQ7L266.

    Proteomic databases

    MaxQBiQ7L266.
    PaxDbiQ7L266.
    PRIDEiQ7L266.

    Protocols and materials databases

    DNASUi80150.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000301776; ENSP00000301776; ENSG00000162174.
    ENST00000415229; ENSP00000400057; ENSG00000162174.
    GeneIDi80150.
    KEGGihsa:80150.
    UCSCiuc001nte.4. human. [Q7L266-1]

    Organism-specific databases

    CTDi80150.
    GeneCardsiGC11P062104.
    HGNCiHGNC:16448. ASRGL1.
    HPAiHPA029725.
    HPA055572.
    MIMi609212. gene.
    neXtProtiNX_Q7L266.
    PharmGKBiPA25059.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1446.
    GeneTreeiENSGT00530000063034.
    HOGENOMiHOG000174613.
    HOVERGENiHBG101662.
    InParanoidiQ7L266.
    KOiK13051.
    OMAiPCVGAGG.
    OrthoDBiEOG7TBC2N.
    PhylomeDBiQ7L266.
    TreeFamiTF323960.

    Enzyme and pathway databases

    BRENDAi3.4.19.5. 2681.

    Miscellaneous databases

    ChiTaRSiASRGL1. human.
    GeneWikiiASRGL1.
    GenomeRNAii80150.
    NextBioi70434.
    PROiQ7L266.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ7L266.
    CleanExiHS_ASRGL1.
    ExpressionAtlasiQ7L266. baseline and differential.
    GenevisibleiQ7L266. HS.

    Family and domain databases

    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000246. Peptidase_T2.
    [Graphical view]
    PANTHERiPTHR10188. PTHR10188. 1 hit.
    PfamiPF01112. Asparaginase_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A novel asparaginase-like protein is a sperm autoantigen in rats."
      Bush L.A., Herr J.C., Wolkowicz M., Sherman N.E., Shore A., Flickinger C.J.
      Mol. Reprod. Dev. 62:233-247(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Testis.
    2. "Identification of CRASH, a gene deregulated in gynecological tumors."
      Evtimova V., Zeillinger R., Kaul S., Weidle U.H.
      Int. J. Oncol. 24:33-41(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION.
    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] (ISOFORM 1).
      Tissue: Corpus callosum.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 2).
      Tissue: Eye, Lung and Skin.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity."
      Cantor J.R., Stone E.M., Chantranupong L., Georgiou G.
      Biochemistry 48:11026-11031(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF THR-168, IDENTIFICATION BY MASS SPECTROMETRY, AUTOCATALYTIC CLEAVAGE.
    8. "Structures of apo and product-bound human L-asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis."
      Nomme J., Su Y., Konrad M., Lavie A.
      Biochemistry 51:6816-6826(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEXES WITH ASPARTATE, ACTIVE SITE, SUBUNIT, ENZYME REGULATION, AUTOCATALYTIC CLEAVAGE.
    9. "Uncoupling intramolecular processing and substrate hydrolysis in the N-terminal nucleophile hydrolase hASRGL1 by circular permutation."
      Li W., Cantor J.R., Yogesha S.D., Yang S., Chantranupong L., Liu J.Q., Agnello G., Georgiou G., Stone E.M., Zhang Y.
      ACS Chem. Biol. 7:1840-1847(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS OF THR-168, SUBUNIT.

    Entry informationi

    Entry nameiASGL1_HUMAN
    AccessioniPrimary (citable) accession number: Q7L266
    Secondary accession number(s): B2R7Q0
    , Q567Q4, Q6P1P0, Q8NI34, Q9H6F7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: April 3, 2007
    Last modified: July 22, 2015
    This is version 106 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.