Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6UY14

- ATL4_HUMAN

UniProt

Q6UY14 - ATL4_HUMAN

Protein

ADAMTS-like protein 4

Gene

ADAMTSL4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (31 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Positive regulation of apoptosis. May facilitate FBN1 microfibril biogenesis.2 Publications

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. protease binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. extracellular matrix organization Source: Ensembl
    3. positive regulation of apoptotic process Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    ReactomeiREACT_200626. O-glycosylation of TSR domain-containing proteins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ADAMTS-like protein 4
    Short name:
    ADAMTSL-4
    Alternative name(s):
    Thrombospondin repeat-containing protein 1
    Gene namesi
    Name:ADAMTSL4
    Synonyms:TSRC1Imported
    ORF Names:PP1396, UNQ2803/PRO34012
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19706. ADAMTSL4.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix 1 Publication
    Note: Colocalizes with FMN1 microfibrils in the eye ECM.

    GO - Cellular componenti

    1. extracellular matrix Source: InterPro
    2. interstitial matrix Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ectopia lentis 2, isolated, autosomal recessive (ECTOL2) [MIM:225200]: An ocular abnormality characterized by partial or complete displacement of the lens from its space resulting from defective zonule formation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Ectopia lentis et pupillae (ECTOLP) [MIM:225200]: An ocular abnormality characterized by displacement of the lenses and the pupils, associated with other ocular anomalies, but without systemic manifestations. The condition is usually bilateral, with the lenses and pupils displaced in opposite directions. Additional signs include enlarged corneal diameter, increased corneal astigmatism, increased anterior chamber depth, thinning and flattening of the iris with loss of crypts, angle malformation caused by enlarged iris processes, persistent pupillary membrane, loss of zonular fibers, tilted disk, and increased axial length. Secondary manifestations include refractive errors, glaucoma, early cataract development, and retinal detachment. Membrane formation on the posterior aspect of the iris has been observed both in histologic sections and on ultrasound biomicroscopy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi225200. phenotype.
    Orphaneti1885. Isolated ectopia lentis.
    PharmGKBiPA134879921.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 10741050ADAMTS-like protein 4Sequence AnalysisPRO_0000257966Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi3 – 31N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi490 – 4901N-linked (GlcNAc...) (complex)3 Publications
    Glycosylationi773 – 7731N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs. N- and C-glycosylations can also facilitate secretion By similarity.By similarity

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ6UY14.
    PRIDEiQ6UY14.

    PTM databases

    PhosphoSiteiQ6UY14.

    Expressioni

    Tissue specificityi

    Expressed in colon, heart, leukocyte, liver, lung, skeletal muscle, spleen, testis and placenta. Weaker expression in bone marrow, brain tissue, kidney and pancreas. Expression studies in fetal tissues reveal strong expression in heart, kidney, liver, lung and skeletal muscle, but weaker expression in fetal brain and skin.1 Publication

    Gene expression databases

    ArrayExpressiQ6UY14.
    BgeeiQ6UY14.
    CleanExiHS_ADAMTSL4.
    GenevestigatoriQ6UY14.

    Organism-specific databases

    HPAiHPA006279.

    Interactioni

    Subunit structurei

    Interacts with CTSB. Interacts with FBN1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTSBP078583EBI-742002,EBI-715062
    Hoxa1P090223EBI-742002,EBI-3957603From a different organism.
    STK16O757163EBI-742002,EBI-749295

    Protein-protein interaction databases

    BioGridi120002. 19 interactions.
    IntActiQ6UY14. 22 interactions.
    MINTiMINT-1445070.
    STRINGi9606.ENSP00000271643.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6UY14.
    SMRiQ6UY14. Positions 364-548.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini48 – 9346TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini723 – 78260TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini783 – 84260TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini845 – 90965TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini910 – 96960TSP type-1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini970 – 102657TSP type-1 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1029 – 106638PLACPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi602 – 66463Pro-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PLAC domain.PROSITE-ProRule annotation
    Contains 6 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG242665.
    HOGENOMiHOG000034174.
    HOVERGENiHBG080879.
    InParanoidiQ6UY14.
    OrthoDBiEOG73FQKT.
    PhylomeDBiQ6UY14.
    TreeFamiTF316874.

    Family and domain databases

    InterProiIPR010294. ADAM_spacer1.
    IPR010909. PLAC.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF08686. PLAC. 1 hit.
    PF00090. TSP_1. 5 hits.
    [Graphical view]
    SMARTiSM00209. TSP1. 6 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 6 hits.
    PROSITEiPS50900. PLAC. 1 hit.
    PS50092. TSP1. 6 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q6UY14-1) [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

    MENWTGRPWL YLLLLLSLPQ LCLDQEVLSG HSLQTPTEEG QGPEGVWGPW     50
    VQWASCSQPC GVGVQRRSRT CQLPTVQLHP SLPLPPRPPR HPEALLPRGQ 100
    GPRPQTSPET LPLYRTQSRG RGGPLRGPAS HLGREETQEI RAARRSRLRD 150
    PIKPGMFGYG RVPFALPLHR NRRHPRSPPR SELSLISSRG EEAIPSPTPR 200
    AEPFSANGSP QTELPPTELS VHTPSPQAEP LSPETAQTEV APRTRPAPLR 250
    HHPRAQASGT EPPSPTHSLG EGGFFRASPQ PRRPSSQGWA SPQVAGRRPD 300
    PFPSVPRGRG QQGQGPWGTG GTPHGPRLEP DPQHPGAWLP LLSNGPHASS 350
    LWSLFAPSSP IPRCSGESEQ LRACSQAPCP PEQPDPRALQ CAAFNSQEFM 400
    GQLYQWEPFT EVQGSQRCEL NCRPRGFRFY VRHTEKVQDG TLCQPGAPDI 450
    CVAGRCLSPG CDGILGSGRR PDGCGVCGGD DSTCRLVSGN LTDRGGPLGY 500
    QKILWIPAGA LRLQIAQLRP SSNYLALRGP GGRSIINGNW AVDPPGSYRA 550
    GGTVFRYNRP PREEGKGESL SAEGPTTQPV DVYMIFQEEN PGVFYQYVIS 600
    SPPPILENPT PEPPVPQLQP EILRVEPPLA PAPRPARTPG TLQRQVRIPQ 650
    MPAPPHPRTP LGSPAAYWKR VGHSACSASC GKGVWRPIFL CISRESGEEL 700
    DERSCAAGAR PPASPEPCHG TPCPPYWEAG EWTSCSRSCG PGTQHRQLQC 750
    RQEFGGGGSS VPPERCGHLP RPNITQSCQL RLCGHWEVGS PWSQCSVRCG 800
    RGQRSRQVRC VGNNGDEVSE QECASGPPQP PSREACDMGP CTTAWFHSDW 850
    SSKCSAECGT GIQRRSVVCL GSGAALGPGQ GEAGAGTGQS CPTGSRPPDM 900
    RACSLGPCER TWRWYTGPWG ECSSECGSGT QRRDIICVSK LGTEFNVTSP 950
    SNCSHLPRPP ALQPCQGQAC QDRWFSTPWS PCSRSCQGGT QTREVQCLST 1000
    NQTLSTRCPP QLRPSRKRPC NSQPCSQRPD DQCKDSSPHC PLVVQARLCV 1050
    YPYYTATCCR SCAHVLERSP QDPS 1074

    Note: Gene prediction confirmed by EST data.Curated

    Length:1,074
    Mass (Da):116,545
    Last modified:October 31, 2006 - v2
    Checksum:i79AE0E5DF5488CA1
    GO
    Isoform 21 Publication (identifier: Q6UY14-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         854-877: CSAECGTGIQRRSVVCLGSGAALG → VSPEPPAISCILGNHAQDTSAFPA
         878-1074: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:877
    Mass (Da):95,132
    Checksum:iB778D79DB24E4EA9
    GO
    Isoform 3 (identifier: Q6UY14-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         411-411: E → EAPLLPLRHAFFLLPGAGSGDSTG

    Note: No experimental confirmation available.

    Show »
    Length:1,097
    Mass (Da):118,822
    Checksum:iF7C5EB712A3EA448
    GO

    Sequence cautioni

    The sequence AAG17217.1 differs from that shown. Reason: Frameshift at position 719.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti193 – 1931A → P.1 Publication
    Corresponds to variant rs41317515 [ dbSNP | Ensembl ].
    VAR_061918
    Natural varianti1028 – 10281R → H.
    Corresponds to variant rs56411234 [ dbSNP | Ensembl ].
    VAR_061919

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei411 – 4111E → EAPLLPLRHAFFLLPGAGSG DSTG in isoform 3. CuratedVSP_055759
    Alternative sequencei854 – 87724CSAEC…GAALG → VSPEPPAISCILGNHAQDTS AFPA in isoform 2. 2 PublicationsVSP_052183Add
    BLAST
    Alternative sequencei878 – 1074197Missing in isoform 2. 2 PublicationsVSP_052184Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY358122 mRNA. Translation: AAQ88489.1.
    AL356356 Genomic DNA. Translation: CAI15499.1.
    AL356356 Genomic DNA. Translation: CAI15500.2.
    BC027478 mRNA. Translation: AAH27478.2.
    BC071852 mRNA. Translation: AAH71852.1.
    BC094811 mRNA. Translation: AAH94811.1.
    BC140800 mRNA. Translation: AAI40801.1.
    AF217974 mRNA. Translation: AAG17217.1. Frameshift.
    CCDSiCCDS30852.1. [Q6UY14-2]
    CCDS955.1. [Q6UY14-1]
    RefSeqiNP_001275536.1. NM_001288607.1.
    NP_001275537.1. NM_001288608.1.
    NP_061905.2. NM_019032.5. [Q6UY14-1]
    NP_079284.2. NM_025008.4. [Q6UY14-2]
    UniGeneiHs.516243.

    Genome annotation databases

    EnsembliENST00000271643; ENSP00000271643; ENSG00000143382. [Q6UY14-1]
    ENST00000369038; ENSP00000358034; ENSG00000143382. [Q6UY14-1]
    ENST00000369039; ENSP00000358035; ENSG00000143382. [Q6UY14-3]
    ENST00000369041; ENSP00000358037; ENSG00000143382. [Q6UY14-2]
    GeneIDi54507.
    KEGGihsa:54507.
    UCSCiuc001euw.3. human. [Q6UY14-2]
    uc001eux.3. human. [Q6UY14-1]

    Polymorphism databases

    DMDMi118573317.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY358122 mRNA. Translation: AAQ88489.1 .
    AL356356 Genomic DNA. Translation: CAI15499.1 .
    AL356356 Genomic DNA. Translation: CAI15500.2 .
    BC027478 mRNA. Translation: AAH27478.2 .
    BC071852 mRNA. Translation: AAH71852.1 .
    BC094811 mRNA. Translation: AAH94811.1 .
    BC140800 mRNA. Translation: AAI40801.1 .
    AF217974 mRNA. Translation: AAG17217.1 . Frameshift.
    CCDSi CCDS30852.1. [Q6UY14-2 ]
    CCDS955.1. [Q6UY14-1 ]
    RefSeqi NP_001275536.1. NM_001288607.1.
    NP_001275537.1. NM_001288608.1.
    NP_061905.2. NM_019032.5. [Q6UY14-1 ]
    NP_079284.2. NM_025008.4. [Q6UY14-2 ]
    UniGenei Hs.516243.

    3D structure databases

    ProteinModelPortali Q6UY14.
    SMRi Q6UY14. Positions 364-548.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120002. 19 interactions.
    IntActi Q6UY14. 22 interactions.
    MINTi MINT-1445070.
    STRINGi 9606.ENSP00000271643.

    PTM databases

    PhosphoSitei Q6UY14.

    Polymorphism databases

    DMDMi 118573317.

    Proteomic databases

    PaxDbi Q6UY14.
    PRIDEi Q6UY14.

    Protocols and materials databases

    DNASUi 54507.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000271643 ; ENSP00000271643 ; ENSG00000143382 . [Q6UY14-1 ]
    ENST00000369038 ; ENSP00000358034 ; ENSG00000143382 . [Q6UY14-1 ]
    ENST00000369039 ; ENSP00000358035 ; ENSG00000143382 . [Q6UY14-3 ]
    ENST00000369041 ; ENSP00000358037 ; ENSG00000143382 . [Q6UY14-2 ]
    GeneIDi 54507.
    KEGGi hsa:54507.
    UCSCi uc001euw.3. human. [Q6UY14-2 ]
    uc001eux.3. human. [Q6UY14-1 ]

    Organism-specific databases

    CTDi 54507.
    GeneCardsi GC01P150522.
    GeneReviewsi ADAMTSL4.
    HGNCi HGNC:19706. ADAMTSL4.
    HPAi HPA006279.
    MIMi 225200. phenotype.
    610113. gene.
    neXtProti NX_Q6UY14.
    Orphaneti 1885. Isolated ectopia lentis.
    PharmGKBi PA134879921.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242665.
    HOGENOMi HOG000034174.
    HOVERGENi HBG080879.
    InParanoidi Q6UY14.
    OrthoDBi EOG73FQKT.
    PhylomeDBi Q6UY14.
    TreeFami TF316874.

    Enzyme and pathway databases

    Reactomei REACT_200626. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    ChiTaRSi ADAMTSL4. human.
    GeneWikii ADAMTSL4.
    GenomeRNAii 54507.
    NextBioi 56873.
    PROi Q6UY14.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6UY14.
    Bgeei Q6UY14.
    CleanExi HS_ADAMTSL4.
    Genevestigatori Q6UY14.

    Family and domain databases

    InterProi IPR010294. ADAM_spacer1.
    IPR010909. PLAC.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF05986. ADAM_spacer1. 1 hit.
    PF08686. PLAC. 1 hit.
    PF00090. TSP_1. 5 hits.
    [Graphical view ]
    SMARTi SM00209. TSP1. 6 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 6 hits.
    PROSITEi PS50900. PLAC. 1 hit.
    PS50092. TSP1. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-1074 (ISOFORM 1), VARIANT PRO-193.
      Tissue: LungImported and Placenta.
    4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 638-1074.
    5. "TSRC1, a widely expressed gene containing seven thrombospondin type I repeats."
      Buchner D.A., Meisler M.H.
      Gene 307:23-30(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION (ISOFORM 1).
    6. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-490.
      Tissue: Plasma.
    7. "Cathepsin B and its interacting proteins, bikunin and TSRC1, correlate with TNF-induced apoptosis of ovarian cancer cells OV-90."
      Liu J., Guo Q., Chen B., Yu Y., Lu H., Li Y.-Y.
      FEBS Lett. 580:245-250(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTSB.
    8. "A homozygous mutation in ADAMTSL4 causes autosomal-recessive isolated ectopia lentis."
      Ahram D., Sato T.S., Kohilan A., Tayeh M., Chen S., Leal S., Al-Salem M., El-Shanti H.
      Am. J. Hum. Genet. 84:274-278(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INVOLVEMENT IN ECTOL2.
    9. Cited for: GLYCOSYLATION AT ASN-490.
    10. "A novel ADAMTSL4 mutation in autosomal recessive ectopia lentis et pupillae."
      Christensen A.E., Fiskerstrand T., Knappskog P.M., Boman H., Roedahl E.
      Invest. Ophthalmol. Vis. Sci. 51:6369-6373(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN ECTOLP.
    11. "ADAMTSL4, a secreted glycoprotein widely distributed in the eye, binds Fibrillin-1 microfibrils and accelerates microfibril biogenesis."
      Gabriel L.A., Wang L.W., Bader H., Ho J.C., Majors A.K., Hollyfield J.G., Traboulsi E.I., Apte S.S.
      Invest. Ophthalmol. Vis. Sci. 53:461-469(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FBN1, GLYCOSYLATION.

    Entry informationi

    Entry nameiATL4_HUMAN
    AccessioniPrimary (citable) accession number: Q6UY14
    Secondary accession number(s): B2RTT0
    , F8WAD0, Q5T5F7, Q6IPM6, Q8N643, Q9HBS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: October 31, 2006
    Last modified: October 1, 2014
    This is version 100 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3