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Q7L266

- ASGL1_HUMAN

UniProt

Q7L266 - ASGL1_HUMAN

Protein

Isoaspartyl peptidase/L-asparaginase

Gene

ASRGL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    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

    1. asparaginase activity Source: UniProtKB
    2. beta-aspartyl-peptidase activity Source: UniProtKB

    GO - Biological processi

    1. asparagine catabolic process via L-aspartate Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease

    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: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:16448. ASRGL1.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Midpiece of sperm tail.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProt

    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.

    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

    ArrayExpressiQ7L266.
    BgeeiQ7L266.
    CleanExiHS_ASRGL1.
    GenevestigatoriQ7L266.

    Organism-specific databases

    HPAiHPA029725.

    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 – 85
    Helixi17 – 3822
    Turni39 – 413
    Helixi44 – 5714
    Beta strandi61 – 644
    Beta strandi71 – 733
    Beta strandi77 – 837
    Turni84 – 863
    Beta strandi89 – 957
    Helixi101 – 11111
    Beta strandi115 – 1184
    Helixi119 – 12810
    Helixi136 – 1383
    Helixi142 – 15211
    Beta strandi169 – 1746
    Beta strandi180 – 1867
    Turni203 – 2053
    Beta strandi206 – 2105
    Turni211 – 2133
    Beta strandi214 – 2207
    Helixi222 – 2287
    Helixi230 – 23910
    Helixi244 – 25916
    Beta strandi263 – 2697
    Beta strandi274 – 2829
    Beta strandi285 – 2895
    Beta strandi292 – 2987
    Beta strandi303 – 3064

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000174613.
    HOVERGENiHBG101662.
    InParanoidiQ7L266.
    KOiK13051.
    OMAiLITERSK.
    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. Align

    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

    MNPIVVVHGG GAGPISKDRK ERVHQGMVRA ATVGYGILRE GGSAVDAVEG    50
    AVVALEDDPE FNAGCGSVLN TNGEVEMDAS IMDGKDLSAG AVSAVQCIAN 100
    PIKLARLVME KTPHCFLTDQ GAAQFAAAMG VPEIPGEKLV TERNKKRLEK 150
    EKHEKGAQKT DCQKNLGTVG AVALDCKGNV AYATSTGGIV NKMVGRVGDS 200
    PCLGAGGYAD NDIGAVSTTG HGESILKVNL ARLTLFHIEQ GKTVEEAADL 250
    SLGYMKSRVK GLGGLIVVSK TGDWVAKWTS TSMPWAAAKD GKLHFGIDPD 300
    DTTITDLP 308
    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. Reason: Contaminating sequence.
    The sequence BAB15302.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    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:
    EMBL
    GenBank
    DDBJ
    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_005274305.1. [Q7L266-2]
    XP_005274363.1. XM_005274306.1. [Q7L266-2]
    UniGeneiHs.535326.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi158706477.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS8019.1. [Q7L266-1 ]
    RefSeqi NP_001077395.1. NM_001083926.1. [Q7L266-1 ]
    NP_079356.3. NM_025080.3. [Q7L266-1 ]
    XP_005274362.1. XM_005274305.1. [Q7L266-2 ]
    XP_005274363.1. XM_005274306.1. [Q7L266-2 ]
    UniGenei Hs.535326.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3TKJ X-ray 2.30 A/B 2-308 [» ]
    4ET0 X-ray 3.30 A/B 2-308 [» ]
    4O0C X-ray 1.50 A/B 1-308 [» ]
    4O0D X-ray 1.95 A/B 1-308 [» ]
    4O0E X-ray 1.71 A/B 1-308 [» ]
    4O0F X-ray 1.92 A/B 1-308 [» ]
    4O0G X-ray 2.10 A/B 1-308 [» ]
    4O0H X-ray 1.97 A/B 1-308 [» ]
    4OSX X-ray 1.95 A/B 1-308 [» ]
    4OSY X-ray 1.91 A/B 1-308 [» ]
    4PVP X-ray 1.85 A/B 1-308 [» ]
    4PVQ X-ray 2.13 A/B 1-308 [» ]
    4PVR X-ray 1.75 A/B 1-308 [» ]
    4PVS X-ray 1.84 A/B 1-308 [» ]
    ProteinModelPortali Q7L266.
    SMRi Q7L266. Positions 1-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123142. 5 interactions.
    IntActi Q7L266. 4 interactions.
    STRINGi 9606.ENSP00000301776.

    Chemistry

    DrugBanki DB00174. L-Asparagine.
    DB00128. L-Aspartic Acid.

    Protein family/group databases

    MEROPSi T02.002.

    PTM databases

    PhosphoSitei Q7L266.

    Polymorphism databases

    DMDMi 158706477.

    2D gel databases

    UCD-2DPAGE Q7L266.

    Proteomic databases

    MaxQBi Q7L266.
    PaxDbi Q7L266.
    PRIDEi Q7L266.

    Protocols and materials databases

    DNASUi 80150.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301776 ; ENSP00000301776 ; ENSG00000162174 . [Q7L266-1 ]
    ENST00000415229 ; ENSP00000400057 ; ENSG00000162174 . [Q7L266-1 ]
    GeneIDi 80150.
    KEGGi hsa:80150.
    UCSCi uc001nte.4. human. [Q7L266-1 ]

    Organism-specific databases

    CTDi 80150.
    GeneCardsi GC11P062104.
    HGNCi HGNC:16448. ASRGL1.
    HPAi HPA029725.
    MIMi 609212. gene.
    neXtProti NX_Q7L266.
    PharmGKBi PA25059.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1446.
    HOGENOMi HOG000174613.
    HOVERGENi HBG101662.
    InParanoidi Q7L266.
    KOi K13051.
    OMAi LITERSK.
    OrthoDBi EOG7TBC2N.
    PhylomeDBi Q7L266.
    TreeFami TF323960.

    Miscellaneous databases

    ChiTaRSi ASRGL1. human.
    GeneWikii ASRGL1.
    GenomeRNAii 80150.
    NextBioi 70434.
    PROi Q7L266.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7L266.
    Bgeei Q7L266.
    CleanExi HS_ASRGL1.
    Genevestigatori Q7L266.

    Family and domain databases

    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000246. Peptidase_T2.
    [Graphical view ]
    PANTHERi PTHR10188. PTHR10188. 1 hit.
    Pfami PF01112. Asparaginase_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 98 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