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Q9Y3M8

- STA13_HUMAN

UniProt

Q9Y3M8 - STA13_HUMAN

Protein

StAR-related lipid transfer protein 13

Gene

STARD13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    GTPase-activating protein for RhoA, and perhaps for Cdc42. May be involved in regulation of cytoskeletal reorganization, cell proliferation and cell motility. Acts a tumor suppressor in hepatocellular carcinoma cells.2 Publications

    GO - Molecular functioni

    1. GTPase activator activity Source: UniProtKB-KW
    2. lipid binding Source: InterPro
    3. protein binding Source: IntAct

    GO - Biological processi

    1. regulation of small GTPase mediated signal transduction Source: Reactome
    2. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    StAR-related lipid transfer protein 13
    Alternative name(s):
    46H23.2
    Deleted in liver cancer 2 protein
    Short name:
    DLC-2
    Rho GTPase-activating protein
    START domain-containing protein 13
    Short name:
    StARD13
    Gene namesi
    Name:STARD13
    Synonyms:DLC2, GT650
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:19164. STARD13.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. lipid particle Source: UniProtKB-SubCell
    3. mitochondrial membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Lipid droplet, Membrane, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi699 – 6991R → A: Loss of RhoGAP activity. 1 Publication
    Mutagenesisi736 – 7361K → E: Loss of RhoGAP activity. 1 Publication
    Mutagenesisi740 – 7401R → E: Loss of RhoGAP activity. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA38806.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11131113StAR-related lipid transfer protein 13PRO_0000220679Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei133 – 1331PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y3M8.
    PaxDbiQ9Y3M8.
    PRIDEiQ9Y3M8.

    PTM databases

    PhosphoSiteiQ9Y3M8.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Underexpressed in hepatocellular carcinoma cells and some breast cancer cell lines.2 Publications

    Gene expression databases

    ArrayExpressiQ9Y3M8.
    BgeeiQ9Y3M8.
    GenevestigatoriQ9Y3M8.

    Organism-specific databases

    HPAiHPA039535.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with TAX1BP1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TAX1BP1Q86VP12EBI-465487,EBI-529518

    Protein-protein interaction databases

    BioGridi124744. 12 interactions.
    IntActiQ9Y3M8. 10 interactions.
    MINTiMINT-1194865.

    Structurei

    Secondary structure

    1
    1113
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi56 – 6914
    Helixi73 – 775
    Turni78 – 825
    Helixi88 – 925
    Helixi100 – 1023
    Helixi103 – 11715
    Helixi913 – 92412
    Beta strandi929 – 9313
    Beta strandi934 – 9363
    Beta strandi938 – 9425
    Beta strandi952 – 96110
    Helixi963 – 97210
    Helixi974 – 9763
    Beta strandi985 – 9917
    Beta strandi994 – 10018
    Beta strandi1004 – 10063
    Beta strandi1010 – 102011
    Helixi1023 – 10253
    Beta strandi1027 – 10337
    Beta strandi1043 – 10464
    Beta strandi1049 – 105810
    Beta strandi1064 – 10729
    Beta strandi1075 – 10773
    Turni1079 – 10846
    Helixi1085 – 109915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H80NMR-A56-120[»]
    2JW2NMR-A56-120[»]
    2PSOX-ray2.80A/B/C903-1113[»]
    ProteinModelPortaliQ9Y3M8.
    SMRiQ9Y3M8. Positions 50-120, 655-863, 907-1104.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y3M8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 12268SAMAdd
    BLAST
    Domaini663 – 868206Rho-GAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini899 – 1107209STARTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
    Contains 1 START domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG236923.
    HOVERGENiHBG055955.
    InParanoidiQ9Y3M8.
    OMAiFVQWKVV.
    OrthoDBiEOG7CG6Z8.
    PhylomeDBiQ9Y3M8.
    TreeFamiTF314044.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    3.30.530.20. 1 hit.
    InterProiIPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR023393. START-like_dom.
    IPR002913. START_lipid-bd_dom.
    [Graphical view]
    PfamiPF00620. RhoGAP. 1 hit.
    PF07647. SAM_2. 1 hit.
    PF01852. START. 1 hit.
    [Graphical view]
    SMARTiSM00324. RhoGAP. 1 hit.
    SM00234. START. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF48350. SSF48350. 1 hit.
    PROSITEiPS50238. RHOGAP. 1 hit.
    PS50848. START. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y3M8-1) [UniParc]FASTAAdd to Basket

    Also known as: DLC2alpha

    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

    MFSQVPRTPA SGCYYLNSMT PEGQEMYLRF DQTTRRSPYR MSRILARHQL     50
    VTKIQQEIEA KEACDWLRAA GFPQYAQLYE DSQFPINIVA VKNDHDFLEK 100
    DLVEPLCRRL NTLNKCASMK LDVNFQRKKG DDSDEEDLCI SNKWTFQRTS 150
    RRWSRVDDLY TLLPRGDRNG SPGGTGMRNT TSSESVLTDL SEPEVCSIHS 200
    ESSGGSDSRS QPGQCCTDNP VMLDAPLVSS SLPQPPRDVL NHPFHPKNEK 250
    PTRARAKSFL KRMETLRGKG AHGRHKGSGR TGGLVISGPM LQQEPESFKA 300
    MQCIQIPNGD LQNSPPPACR KGLPCSGKSS GESSPSEHSS SGVSTPCLKE 350
    RKCHEANKRG GMYLEDLDVL AGTALPDAGD QSRMHEFHSQ ENLVVHIPKD 400
    HKPGTFPKAL SIESLSPTDS SNGVNWRTGS ISLGREQVPG AREPRLMASC 450
    HRASRVSIYD NVPGSHLYAS TGDLLDLEKD DLFPHLDDIL QHVNGLQEVV 500
    DDWSKDVLPE LQTHDTLVGE PGLSTFPSPN QITLDFEGNS VSEGRTTPSD 550
    VERDVTSLNE SEPPGVRDRR DSGVGASLTR PNRRLRWNSF QLSHQPRPAP 600
    ASPHISSQTA SQLSLLQRFS LLRLTAIMEK HSMSNKHGWT WSVPKFMKRM 650
    KVPDYKDKAV FGVPLIVHVQ RTGQPLPQSI QQALRYLRSN CLDQVGLFRK 700
    SGVKSRIHAL RQMNENFPEN VNYEDQSAYD VADMVKQFFR DLPEPLFTNK 750
    LSETFLHIYQ YVSKEQRLQA VQAAILLLAD ENREVLQTLL CFLNDVVNLV 800
    EENQMTPMNL AVCLAPSLFH LNLLKKESSP RVIQKKYATG KPDQKDLNEN 850
    LAAAQGLAHM IMECDRLFEV PHELVAQSRN SYVEAEIHVP TLEELGTQLE 900
    ESGATFHTYL NHLIQGLQKE AKEKFKGWVT CSSTDNTDLA FKKVGDGNPL 950
    KLWKASVEVE APPSVVLNRV LRERHLWDED FVQWKVVETL DRQTEIYQYV 1000
    LNSMAPHPSR DFVVLRTWKT DLPKGMCTLV SLSVEHEEAQ LLGGVRAVVM 1050
    DSQYLIEPCG SGKSRLTHIC RIDLKGHSPE WYSKGFGHLC AAEVARIRNS 1100
    FQPLIAEGPE TKI 1113
    Length:1,113
    Mass (Da):124,967
    Last modified:March 7, 2006 - v2
    Checksum:i314F809C23E6E1E4
    GO
    Isoform 2 (identifier: Q9Y3M8-2) [UniParc]FASTAAdd to Basket

    Also known as: DLC2beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: MFSQVPRTPA...RHQLVTKIQQ → MLEPSSVLHA...SRVNHTFQRR

    Show »
    Length:1,105
    Mass (Da):123,893
    Checksum:iC447ADE6F7AAF9D8
    GO
    Isoform 3 (identifier: Q9Y3M8-3) [UniParc]FASTAAdd to Basket

    Also known as: DLC2gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         1-118: Missing.

    Show »
    Length:995
    Mass (Da):111,192
    Checksum:i3F608FA94A4EF8BF
    GO
    Isoform 4 (identifier: Q9Y3M8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: MFSQVPRTPA...RHQLVTKIQQ → MSTGTQPKTKVLSDKRPKERV

    Show »
    Length:1,078
    Mass (Da):120,684
    Checksum:i1B108966B3EDC44D
    GO
    Isoform 5 (identifier: Q9Y3M8-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: MFSQVPRTPA...RHQLVTKIQQ → MLEPSSVLHA...SRVNHTFQRR
         695-695: V → E
         696-1113: Missing.

    Show »
    Length:687
    Mass (Da):76,367
    Checksum:i4E1B65EA0FDCB836
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 1431K → R in AAQ72791. (PubMed:14697242)Curated
    Sequence conflicti397 – 3971I → V in AAQ72791. (PubMed:14697242)Curated
    Sequence conflicti1097 – 10971I → T in AAQ72791. (PubMed:14697242)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti175 – 1751T → M.
    Corresponds to variant rs9568878 [ dbSNP | Ensembl ].
    VAR_037494
    Natural varianti250 – 2501K → R.
    Corresponds to variant rs3742321 [ dbSNP | Ensembl ].
    VAR_022098
    Natural varianti383 – 3831R → P.
    Corresponds to variant rs34425674 [ dbSNP | Ensembl ].
    VAR_037495
    Natural varianti798 – 7981N → S.
    Corresponds to variant rs35144435 [ dbSNP | Ensembl ].
    VAR_037496

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 118118Missing in isoform 3. 2 PublicationsVSP_017353Add
    BLAST
    Alternative sequencei1 – 5656MFSQV…TKIQQ → MLEPSSVLHANVNQAPLWCL VLRWCRECKDTVCGGKQKSR VNHTFQRR in isoform 2 and isoform 5. 2 PublicationsVSP_017354Add
    BLAST
    Alternative sequencei1 – 5656MFSQV…TKIQQ → MSTGTQPKTKVLSDKRPKER V in isoform 4. 1 PublicationVSP_017355Add
    BLAST
    Alternative sequencei695 – 6951V → E in isoform 5. 1 PublicationVSP_017356
    Alternative sequencei696 – 1113418Missing in isoform 5. 1 PublicationVSP_017357Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY082589 mRNA. Translation: AAL91648.1.
    AY366448 mRNA. Translation: AAQ72791.1.
    AY082590 mRNA. Translation: AAL91649.1.
    AY082591 mRNA. Translation: AAL91650.1.
    AL049801 mRNA. Translation: CAB42562.1.
    BX647695 mRNA. Translation: CAI46026.1.
    Z84483 Genomic DNA. Translation: CAC94774.1.
    AL627232, AL139187 Genomic DNA. Translation: CAM17900.1.
    AL139187, AL627232 Genomic DNA. Translation: CAM23625.1.
    AL139187 Genomic DNA. Translation: CAM23626.1.
    BC046563 mRNA. Translation: AAH46563.1.
    CCDSiCCDS9348.1. [Q9Y3M8-1]
    CCDS9349.1. [Q9Y3M8-2]
    CCDS9350.1. [Q9Y3M8-3]
    PIRiH59432.
    RefSeqiNP_001230395.1. NM_001243466.1. [Q9Y3M8-5]
    NP_001230403.1. NM_001243474.1.
    NP_001230405.1. NM_001243476.2.
    NP_443083.1. NM_052851.2. [Q9Y3M8-3]
    NP_821074.1. NM_178006.3. [Q9Y3M8-1]
    NP_821075.1. NM_178007.2. [Q9Y3M8-2]
    XP_006719951.1. XM_006719888.1. [Q9Y3M8-3]
    XP_006719952.1. XM_006719889.1. [Q9Y3M8-3]
    UniGeneiHs.507704.
    Hs.721224.

    Genome annotation databases

    EnsembliENST00000255486; ENSP00000255486; ENSG00000133121. [Q9Y3M8-2]
    ENST00000336934; ENSP00000338785; ENSG00000133121. [Q9Y3M8-1]
    ENST00000399365; ENSP00000382300; ENSG00000133121. [Q9Y3M8-3]
    GeneIDi90627.
    KEGGihsa:90627.
    UCSCiuc001uuu.3. human. [Q9Y3M8-2]
    uc001uuv.3. human. [Q9Y3M8-1]
    uc021rhz.1. human. [Q9Y3M8-5]

    Polymorphism databases

    DMDMi90185285.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY082589 mRNA. Translation: AAL91648.1 .
    AY366448 mRNA. Translation: AAQ72791.1 .
    AY082590 mRNA. Translation: AAL91649.1 .
    AY082591 mRNA. Translation: AAL91650.1 .
    AL049801 mRNA. Translation: CAB42562.1 .
    BX647695 mRNA. Translation: CAI46026.1 .
    Z84483 Genomic DNA. Translation: CAC94774.1 .
    AL627232 , AL139187 Genomic DNA. Translation: CAM17900.1 .
    AL139187 , AL627232 Genomic DNA. Translation: CAM23625.1 .
    AL139187 Genomic DNA. Translation: CAM23626.1 .
    BC046563 mRNA. Translation: AAH46563.1 .
    CCDSi CCDS9348.1. [Q9Y3M8-1 ]
    CCDS9349.1. [Q9Y3M8-2 ]
    CCDS9350.1. [Q9Y3M8-3 ]
    PIRi H59432.
    RefSeqi NP_001230395.1. NM_001243466.1. [Q9Y3M8-5 ]
    NP_001230403.1. NM_001243474.1.
    NP_001230405.1. NM_001243476.2.
    NP_443083.1. NM_052851.2. [Q9Y3M8-3 ]
    NP_821074.1. NM_178006.3. [Q9Y3M8-1 ]
    NP_821075.1. NM_178007.2. [Q9Y3M8-2 ]
    XP_006719951.1. XM_006719888.1. [Q9Y3M8-3 ]
    XP_006719952.1. XM_006719889.1. [Q9Y3M8-3 ]
    UniGenei Hs.507704.
    Hs.721224.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H80 NMR - A 56-120 [» ]
    2JW2 NMR - A 56-120 [» ]
    2PSO X-ray 2.80 A/B/C 903-1113 [» ]
    ProteinModelPortali Q9Y3M8.
    SMRi Q9Y3M8. Positions 50-120, 655-863, 907-1104.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124744. 12 interactions.
    IntActi Q9Y3M8. 10 interactions.
    MINTi MINT-1194865.

    PTM databases

    PhosphoSitei Q9Y3M8.

    Polymorphism databases

    DMDMi 90185285.

    Proteomic databases

    MaxQBi Q9Y3M8.
    PaxDbi Q9Y3M8.
    PRIDEi Q9Y3M8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255486 ; ENSP00000255486 ; ENSG00000133121 . [Q9Y3M8-2 ]
    ENST00000336934 ; ENSP00000338785 ; ENSG00000133121 . [Q9Y3M8-1 ]
    ENST00000399365 ; ENSP00000382300 ; ENSG00000133121 . [Q9Y3M8-3 ]
    GeneIDi 90627.
    KEGGi hsa:90627.
    UCSCi uc001uuu.3. human. [Q9Y3M8-2 ]
    uc001uuv.3. human. [Q9Y3M8-1 ]
    uc021rhz.1. human. [Q9Y3M8-5 ]

    Organism-specific databases

    CTDi 90627.
    GeneCardsi GC13M033677.
    H-InvDB HIX0171887.
    HGNCi HGNC:19164. STARD13.
    HPAi HPA039535.
    MIMi 609866. gene.
    neXtProti NX_Q9Y3M8.
    PharmGKBi PA38806.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236923.
    HOVERGENi HBG055955.
    InParanoidi Q9Y3M8.
    OMAi FVQWKVV.
    OrthoDBi EOG7CG6Z8.
    PhylomeDBi Q9Y3M8.
    TreeFami TF314044.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.

    Miscellaneous databases

    ChiTaRSi STARD13. human.
    EvolutionaryTracei Q9Y3M8.
    GeneWikii STARD13.
    GenomeRNAii 90627.
    NextBioi 76872.
    PROi Q9Y3M8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y3M8.
    Bgeei Q9Y3M8.
    Genevestigatori Q9Y3M8.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    3.30.530.20. 1 hit.
    InterProi IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR023393. START-like_dom.
    IPR002913. START_lipid-bd_dom.
    [Graphical view ]
    Pfami PF00620. RhoGAP. 1 hit.
    PF07647. SAM_2. 1 hit.
    PF01852. START. 1 hit.
    [Graphical view ]
    SMARTi SM00324. RhoGAP. 1 hit.
    SM00234. START. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF48350. SSF48350. 1 hit.
    PROSITEi PS50238. RHOGAP. 1 hit.
    PS50848. START. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Deleted in liver cancer (DLC) 2 encodes a RhoGAP protein with growth suppressor function and is underexpressed in hepatocellular carcinoma."
      Ching Y.-P., Wong C.-M., Chan S.-F., Leung T.H.-Y., Ng D.-C., Jin D.-Y., Ng I.O.
      J. Biol. Chem. 278:10824-10830(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF ARG-699.
    2. "Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins."
      Nagaraja G.M., Kandpal R.P.
      Biochem. Biophys. Res. Commun. 313:654-665(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TAX1BP1.
    3. "Deleted in liver cancer 2 (DLC2) suppresses cell transformation by means of inhibition of RhoA activity."
      Leung T.H.-Y., Ching Y.-P., Yam J.W.P., Wong C.-M., Yau T.-O., Jin D.-Y., Ng I.O.
      Proc. Natl. Acad. Sci. U.S.A. 102:15207-15212(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-736 AND ARG-740.
    4. Rhodes S.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Uterus.
    6. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 5).
      Tissue: Skin.
    8. "Mitochondrial targeting of growth suppressor protein DLC2 through the START domain."
      Ng D.C.-H., Chan S.-F., Kok K.H., Yam J.W.P., Ching Y.-P., Ng I.O., Jin D.-Y.
      FEBS Lett. 580:191-198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Solution structures, dynamics, and lipid-binding of the sterile alpha-motif domain of the deleted in liver cancer 2."
      Li H., Fung K.-L., Jin D.-Y., Chung S.S.M., Ching Y.-P., Ng I.O., Sze K.-H., Ko B.C.B., Sun H.
      Proteins 67:1154-1166(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 56-120, SUBUNIT, INTERACTION WITH MEMBRANE PHOSPHOLIPIDS.
    11. "The crystal structure of human STARD13 (DLC2) lipid transfer and protein localization domain."
      Structural genomics consortium (SGC)
      Submitted (MAY-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 900-1113.

    Entry informationi

    Entry nameiSTA13_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3M8
    Secondary accession number(s): A2A309
    , A2A310, Q5HYH1, Q5TAE3, Q6UN61, Q86TP6, Q86WQ3, Q86XT1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 122 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 13
      Human chromosome 13: 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

    External Data

    Dasty 3