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Q14393

- GAS6_HUMAN

UniProt

Q14393 - GAS6_HUMAN

Protein

Growth arrest-specific protein 6

Gene

GAS6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi372 – 3721Calcium
    Metal bindingi374 – 3741Calcium; via carbonyl oxygen
    Metal bindingi483 – 4831Calcium; via carbonyl oxygen
    Metal bindingi699 – 6991Calcium

    GO - Molecular functioni

    1. binding, bridging Source: UniProtKB
    2. calcium ion binding Source: InterPro
    3. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
    4. phosphatidylserine binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein tyrosine kinase activator activity Source: UniProtKB
    7. receptor agonist activity Source: MGI
    8. receptor binding Source: UniProtKB
    9. receptor tyrosine kinase binding Source: UniProtKB
    10. voltage-gated calcium channel activity Source: UniProtKB

    GO - Biological processi

    1. activation of protein kinase B activity Source: UniProtKB
    2. apoptotic cell clearance Source: UniProtKB
    3. B cell chemotaxis Source: UniProtKB
    4. blood coagulation Source: Reactome
    5. calcium ion transmembrane transport Source: UniProtKB
    6. cell adhesion Source: UniProtKB
    7. cell cycle arrest Source: UniProtKB
    8. cell migration Source: UniProtKB
    9. cell proliferation Source: UniProtKB
    10. cell-substrate adhesion Source: Ensembl
    11. cellular protein metabolic process Source: Reactome
    12. cellular response to drug Source: UniProtKB
    13. cellular response to glucose stimulus Source: UniProtKB
    14. cellular response to growth factor stimulus Source: Ensembl
    15. cellular response to interferon-alpha Source: UniProtKB
    16. cellular response to starvation Source: Ensembl
    17. cellular response to vitamin K Source: UniProtKB
    18. dendritic cell differentiation Source: UniProtKB
    19. enzyme linked receptor protein signaling pathway Source: Ensembl
    20. extracellular matrix assembly Source: UniProtKB
    21. fusion of virus membrane with host plasma membrane Source: UniProtKB
    22. hematopoietic stem cell migration to bone marrow Source: UniProtKB
    23. leukocyte migration Source: Reactome
    24. macrophage cytokine production Source: Ensembl
    25. negative regulation of apoptotic process Source: UniProtKB
    26. negative regulation of biomineral tissue development Source: UniProtKB
    27. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    28. negative regulation of dendritic cell apoptotic process Source: UniProtKB
    29. negative regulation of endothelial cell apoptotic process Source: UniProtKB
    30. negative regulation of fibroblast apoptotic process Source: UniProtKB
    31. negative regulation of interferon-gamma production Source: UniProtKB
    32. negative regulation of interleukin-1 secretion Source: UniProtKB
    33. negative regulation of interleukin-6 production Source: UniProtKB
    34. negative regulation of interleukin-6 secretion Source: UniProtKB
    35. negative regulation of oligodendrocyte apoptotic process Source: UniProtKB
    36. negative regulation of protein import into nucleus, translocation Source: UniProtKB
    37. negative regulation of renal albumin absorption Source: UniProtKB
    38. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    39. negative regulation of transcription, DNA-templated Source: UniProtKB
    40. negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
    41. negative regulation of tumor necrosis factor production Source: UniProtKB
    42. neuron migration Source: Ensembl
    43. organ regeneration Source: Ensembl
    44. peptidyl-glutamic acid carboxylation Source: Reactome
    45. peptidyl-serine phosphorylation Source: UniProtKB
    46. phagocytosis Source: UniProtKB
    47. platelet activation Source: UniProtKB
    48. platelet aggregation Source: UniProtKB
    49. platelet degranulation Source: Reactome
    50. positive regulation of cytokine-mediated signaling pathway Source: UniProtKB
    51. positive regulation of dendritic cell chemotaxis Source: UniProtKB
    52. positive regulation of ERK1 and ERK2 cascade Source: MGI
    53. positive regulation of fibroblast proliferation Source: UniProtKB
    54. positive regulation of gene expression Source: UniProtKB
    55. positive regulation of glomerular filtration Source: UniProtKB
    56. positive regulation of natural killer cell differentiation Source: UniProtKB
    57. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
    58. positive regulation of phagocytosis Source: UniProtKB
    59. positive regulation of protein export from nucleus Source: UniProtKB
    60. positive regulation of protein kinase activity Source: UniProtKB
    61. positive regulation of protein kinase B signaling Source: UniProtKB
    62. positive regulation of protein phosphorylation Source: UniProtKB
    63. positive regulation of protein tyrosine kinase activity Source: UniProtKB
    64. positive regulation of TOR signaling Source: UniProtKB
    65. post-translational protein modification Source: Reactome
    66. protein kinase B signaling Source: UniProtKB
    67. protein phosphorylation Source: UniProtKB
    68. protein targeting to plasma membrane Source: UniProtKB
    69. proteolysis Source: Reactome
    70. receptor-mediated virion attachment to host cell Source: UniProtKB
    71. regulation of growth Source: UniProtKB-KW
    72. signal transduction Source: UniProtKB
    73. viral entry into host cell Source: UniProtKB
    74. viral genome replication Source: UniProtKB

    Keywords - Biological processi

    Growth regulation

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_1050. Gamma-carboxylation of protein precursors.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
    REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
    SignaLinkiQ14393.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Growth arrest-specific protein 6
    Short name:
    GAS-6
    Alternative name(s):
    AXL receptor tyrosine kinase ligand
    Gene namesi
    Name:GAS6
    Synonyms:AXLLG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:4168. GAS6.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular region Source: Reactome
    4. extracellular space Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi lumen Source: Reactome
    7. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi353 – 3531R → E: Strongly reduced affinity for AXL. Abolishes phosphorylation of AXL. 1 Publication
    Mutagenesisi355 – 3551K → E: Strongly reduced affinity for AXL. Abolishes phosphorylation of AXL. 1 Publication
    Mutagenesisi530 – 5301F → A: Decreases activation of AXL. 1 Publication
    Mutagenesisi663 – 6631L → A: Reduces affinity for AXL 15-fold and decreases activation of AXL. 1 Publication
    Mutagenesisi703 – 7031Y → A: Reduces affinity for AXL 3-fold. 1 Publication

    Organism-specific databases

    PharmGKBiPA28582.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 721691Growth arrest-specific protein 6PRO_0000007589Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi65 ↔ 70By similarity
    Disulfide bondi120 ↔ 133By similarity
    Disulfide bondi125 ↔ 142By similarity
    Disulfide bondi144 ↔ 153By similarity
    Disulfide bondi160 ↔ 171By similarity
    Disulfide bondi167 ↔ 180By similarity
    Disulfide bondi182 ↔ 195By similarity
    Disulfide bondi201 ↔ 212By similarity
    Disulfide bondi207 ↔ 221By similarity
    Disulfide bondi223 ↔ 236By similarity
    Disulfide bondi242 ↔ 251By similarity
    Disulfide bondi247 ↔ 260By similarity
    Disulfide bondi262 ↔ 277
    Disulfide bondi326 ↔ 613
    Glycosylationi463 – 4631N-linked (GlcNAc...)1 Publication
    Disulfide bondi487 ↔ 513
    Modified residuei664 – 6641PhosphothreonineBy similarity
    Modified residuei680 – 6801PhosphothreonineBy similarity
    Modified residuei683 – 6831PhosphotyrosineBy similarity
    Disulfide bondi686 ↔ 713

    Post-translational modificationi

    Isoform 1 is proteolytically processed after secretion to yield a N-terminal 36 kDa protein and a C-terminal 50 kDa protein including the laminin G-like domains which activates AXL.1 Publication
    Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ14393.
    PaxDbiQ14393.
    PRIDEiQ14393.

    PTM databases

    PhosphoSiteiQ14393.

    Expressioni

    Tissue specificityi

    Plasma. Isoform 1 and isoform 2 are widely expressed. Isoform 1 is the predominant form in spleen.2 Publications

    Gene expression databases

    ArrayExpressiQ14393.
    BgeeiQ14393.
    CleanExiHS_GAS6.
    GenevestigatoriQ14393.

    Organism-specific databases

    HPAiHPA008275.
    HPA056080.

    Interactioni

    Subunit structurei

    Heterodimer and heterotetramer with AXL.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AXLP305308EBI-2802811,EBI-2850927

    Protein-protein interaction databases

    BioGridi108891. 4 interactions.
    IntActiQ14393. 3 interactions.
    MINTiMINT-2735698.
    STRINGi9606.ENSP00000331831.

    Structurei

    Secondary structure

    1
    721
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi264 – 2663
    Beta strandi268 – 2714
    Turni272 – 2754
    Beta strandi276 – 2783
    Beta strandi337 – 3393
    Beta strandi350 – 3534
    Beta strandi356 – 3583
    Beta strandi363 – 3708
    Beta strandi373 – 38210
    Beta strandi386 – 3949
    Beta strandi397 – 4048
    Beta strandi407 – 41610
    Beta strandi419 – 4213
    Beta strandi423 – 4297
    Beta strandi431 – 4388
    Beta strandi441 – 4477
    Beta strandi452 – 4565
    Beta strandi459 – 4613
    Beta strandi463 – 4686
    Helixi473 – 4753
    Beta strandi476 – 4783
    Beta strandi486 – 4938
    Helixi501 – 5077
    Helixi509 – 5113
    Beta strandi512 – 5165
    Beta strandi518 – 5236
    Beta strandi529 – 5313
    Beta strandi550 – 56112
    Beta strandi563 – 5708
    Helixi571 – 5733
    Beta strandi575 – 58410
    Beta strandi595 – 6006
    Beta strandi603 – 6097
    Beta strandi618 – 6258
    Beta strandi628 – 6336
    Beta strandi639 – 6424
    Helixi644 – 65815
    Beta strandi663 – 6675
    Beta strandi676 – 6783
    Beta strandi685 – 6917
    Helixi698 – 7003
    Beta strandi701 – 7044

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H30X-ray2.20A261-721[»]
    2C5DX-ray3.30A/B261-721[»]
    ProteinModelPortaliQ14393.
    SMRiQ14393. Positions 53-721.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14393.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 9442GlaPROSITE-ProRule annotationAdd
    BLAST
    Domaini116 – 15439EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini156 – 19641EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini197 – 23741EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini238 – 27841EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini341 – 513173Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini520 – 713194Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 4 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
    Contains 2 laminin G-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG149502.
    HOGENOMiHOG000065758.
    HOVERGENiHBG051702.
    InParanoidiQ14393.
    KOiK05464.
    OrthoDBiEOG7F5119.
    PhylomeDBiQ14393.
    TreeFamiTF352157.

    Family and domain databases

    Gene3Di2.60.120.200. 2 hits.
    4.10.740.10. 1 hit.
    InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR000294. GLA_domain.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR001791. Laminin_G.
    [Graphical view]
    PfamiPF07645. EGF_CA. 2 hits.
    PF00594. Gla. 1 hit.
    PF00054. Laminin_G_1. 1 hit.
    PF02210. Laminin_G_2. 1 hit.
    [Graphical view]
    PRINTSiPR00001. GLABLOOD.
    SMARTiSM00181. EGF. 1 hit.
    SM00179. EGF_CA. 3 hits.
    SM00069. GLA. 1 hit.
    SM00282. LamG. 2 hits.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 3 hits.
    SSF57184. SSF57184. 1 hit.
    SSF57630. SSF57630. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 3 hits.
    PS50026. EGF_3. 4 hits.
    PS01187. EGF_CA. 3 hits.
    PS00011. GLA_1. 1 hit.
    PS50998. GLA_2. 1 hit.
    PS50025. LAM_G_DOMAIN. 2 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14393-1) [UniParc]FASTAAdd to Basket

    Also known as: gas6SV

    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

    MAPSLSPGPA ALRRAPQLLL LLLAAECALA ALLPAREATQ FLRPRQRRAF    50
    QVFEEAKQGH LERECVEELC SREEAREVFE NDPETDYFYP RYLDCINKYG 100
    SPYTKNSGFA TCVQNLPDQC TPNPCDRKGT QACQDLMGNF FCLCKAGWGG 150
    RLCDKDVNEC SQENGGCLQI CHNKPGSFHC SCHSGFELSS DGRTCQDIDE 200
    CADSEACGEA RCKNLPGSYS CLCDEGFAYS SQEKACRDVD ECLQGRCEQV 250
    CVNSPGSYTC HCDGRGGLKL SQDMDTCELE AGWPCPRHRR DGSPAARPGR 300
    GAQGSRSEGH IPDRRGPRPW QDILPCVPFS VAKSVKSLYL GRMFSGTPVI 350
    RLRFKRLQPT RLVAEFDFRT FDPEGILLFA GGHQDSTWIV LALRAGRLEL 400
    QLRYNGVGRV TSSGPVINHG MWQTISVEEL ARNLVIKVNR DAVMKIAVAG 450
    DLFQPERGLY HLNLTVGGIP FHEKDLVQPI NPRLDGCMRS WNWLNGEDTT 500
    IQETVKVNTR MQCFSVTERG SFYPGSGFAF YSLDYMRTPL DVGTESTWEV 550
    EVVAHIRPAA DTGVLFALWA PDLRAVPLSV ALVDYHSTKK LKKQLVVLAV 600
    EHTALALMEI KVCDGQEHVV TVSLRDGEAT LEVDGTRGQS EVSAAQLQER 650
    LAVLERHLRS PVLTFAGGLP DVPVTSAPVT AFYRGCMTLE VNRRLLDLDE 700
    AAYKHSDITA HSCPPVEPAA A 721
    Length:721
    Mass (Da):79,677
    Last modified:June 7, 2004 - v2
    Checksum:iE7B22B0E010930F9
    GO
    Isoform 2 (identifier: Q14393-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         279-321: Missing.

    Show »
    Length:678
    Mass (Da):74,925
    Checksum:iBB6D8AB0F6C48EA9
    GO
    Isoform 3 (identifier: Q14393-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: Missing.
         55-94: EAKQGHLERE...TDYFYPRYLD → MCMCQASPPP...AFSKAEWLSN
         279-321: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:624
    Mass (Da):68,256
    Checksum:i6CCEBDDE139C9F53
    GO
    Isoform 4 (identifier: Q14393-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-273: Missing.
         279-321: Missing.

    Show »
    Length:405
    Mass (Da):44,841
    Checksum:iECF30C620FA69B60
    GO
    Isoform 5 (identifier: Q14393-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-342: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:379
    Mass (Da):41,986
    Checksum:iA0EE62BA476927C6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti399 – 3991E → K in BAG52469. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411F → L.1 Publication
    VAR_038823
    Natural varianti231 – 2311S → Y.1 Publication
    Corresponds to variant rs146159446 [ dbSNP | Ensembl ].
    VAR_038824
    Natural varianti390 – 3901V → M.1 Publication
    VAR_038825
    Natural varianti543 – 5431G → R.1 Publication
    VAR_038826
    Natural varianti623 – 6231S → L.1 Publication
    VAR_038827
    Natural varianti655 – 6551E → K.1 Publication
    VAR_038828
    Natural varianti659 – 6591R → Q.1 Publication
    VAR_038829

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 342342Missing in isoform 5. 1 PublicationVSP_045685Add
    BLAST
    Alternative sequencei1 – 273273Missing in isoform 4. 1 PublicationVSP_043832Add
    BLAST
    Alternative sequencei1 – 5454Missing in isoform 3. 1 PublicationVSP_010492Add
    BLAST
    Alternative sequencei55 – 9440EAKQG…PRYLD → MCMCQASPPPAALAGCLLSS CVQPAREHGGAFSKAEWLSN in isoform 3. 1 PublicationVSP_010493Add
    BLAST
    Alternative sequencei279 – 32143Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_010494Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13720 mRNA. Translation: AAA58494.1.
    AY256843
    , AY256830, AY256831, AY256832, AY256833, AY256834, AY256835, AY256836, AY256837, AY256838, AY256839, AY256840, AY256841, AY256842 Genomic DNA. Translation: AAO84057.1.
    AK092028 mRNA. Translation: BAG52469.1.
    AK122969 mRNA. Translation: BAG53826.1.
    AK126533 mRNA. Translation: BAC86580.1.
    AK290803 mRNA. Translation: BAF83492.1.
    EF631974 Genomic DNA. Translation: ABR09277.1.
    BX072579 Genomic DNA. Translation: CAH71174.1.
    BC038984 mRNA. Translation: AAH38984.1.
    AY170372 Genomic DNA. Translation: AAO41859.1.
    BK001240 Genomic DNA. Translation: DAA01155.1.
    CCDSiCCDS45072.1. [Q14393-2]
    CCDS45073.1. [Q14393-4]
    CCDS45074.1. [Q14393-5]
    PIRiB48089.
    RefSeqiNP_000811.1. NM_000820.2. [Q14393-2]
    NP_001137417.1. NM_001143945.1. [Q14393-4]
    NP_001137418.1. NM_001143946.1. [Q14393-5]
    UniGeneiHs.646346.

    Genome annotation databases

    EnsembliENST00000327773; ENSP00000331831; ENSG00000183087. [Q14393-2]
    GeneIDi2621.
    KEGGihsa:2621.
    UCSCiuc001vud.3. human. [Q14393-2]
    uc001vuf.3. human. [Q14393-4]
    uc001vug.3. human. [Q14393-1]

    Polymorphism databases

    DMDMi48427995.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13720 mRNA. Translation: AAA58494.1 .
    AY256843
    , AY256830 , AY256831 , AY256832 , AY256833 , AY256834 , AY256835 , AY256836 , AY256837 , AY256838 , AY256839 , AY256840 , AY256841 , AY256842 Genomic DNA. Translation: AAO84057.1 .
    AK092028 mRNA. Translation: BAG52469.1 .
    AK122969 mRNA. Translation: BAG53826.1 .
    AK126533 mRNA. Translation: BAC86580.1 .
    AK290803 mRNA. Translation: BAF83492.1 .
    EF631974 Genomic DNA. Translation: ABR09277.1 .
    BX072579 Genomic DNA. Translation: CAH71174.1 .
    BC038984 mRNA. Translation: AAH38984.1 .
    AY170372 Genomic DNA. Translation: AAO41859.1 .
    BK001240 Genomic DNA. Translation: DAA01155.1 .
    CCDSi CCDS45072.1. [Q14393-2 ]
    CCDS45073.1. [Q14393-4 ]
    CCDS45074.1. [Q14393-5 ]
    PIRi B48089.
    RefSeqi NP_000811.1. NM_000820.2. [Q14393-2 ]
    NP_001137417.1. NM_001143945.1. [Q14393-4 ]
    NP_001137418.1. NM_001143946.1. [Q14393-5 ]
    UniGenei Hs.646346.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H30 X-ray 2.20 A 261-721 [» ]
    2C5D X-ray 3.30 A/B 261-721 [» ]
    ProteinModelPortali Q14393.
    SMRi Q14393. Positions 53-721.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108891. 4 interactions.
    IntActi Q14393. 3 interactions.
    MINTi MINT-2735698.
    STRINGi 9606.ENSP00000331831.

    PTM databases

    PhosphoSitei Q14393.

    Polymorphism databases

    DMDMi 48427995.

    Proteomic databases

    MaxQBi Q14393.
    PaxDbi Q14393.
    PRIDEi Q14393.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327773 ; ENSP00000331831 ; ENSG00000183087 . [Q14393-2 ]
    GeneIDi 2621.
    KEGGi hsa:2621.
    UCSCi uc001vud.3. human. [Q14393-2 ]
    uc001vuf.3. human. [Q14393-4 ]
    uc001vug.3. human. [Q14393-1 ]

    Organism-specific databases

    CTDi 2621.
    GeneCardsi GC13M114523.
    HGNCi HGNC:4168. GAS6.
    HPAi HPA008275.
    HPA056080.
    MIMi 600441. gene.
    neXtProti NX_Q14393.
    PharmGKBi PA28582.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149502.
    HOGENOMi HOG000065758.
    HOVERGENi HBG051702.
    InParanoidi Q14393.
    KOi K05464.
    OrthoDBi EOG7F5119.
    PhylomeDBi Q14393.
    TreeFami TF352157.

    Enzyme and pathway databases

    Reactomei REACT_1050. Gamma-carboxylation of protein precursors.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
    REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
    SignaLinki Q14393.

    Miscellaneous databases

    ChiTaRSi GAS6. human.
    EvolutionaryTracei Q14393.
    GeneWikii GAS6.
    GenomeRNAii 2621.
    NextBioi 10323.
    PROi Q14393.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14393.
    Bgeei Q14393.
    CleanExi HS_GAS6.
    Genevestigatori Q14393.

    Family and domain databases

    Gene3Di 2.60.120.200. 2 hits.
    4.10.740.10. 1 hit.
    InterProi IPR017857. Coagulation_fac_subgr_Gla_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR000294. GLA_domain.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR001791. Laminin_G.
    [Graphical view ]
    Pfami PF07645. EGF_CA. 2 hits.
    PF00594. Gla. 1 hit.
    PF00054. Laminin_G_1. 1 hit.
    PF02210. Laminin_G_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00001. GLABLOOD.
    SMARTi SM00181. EGF. 1 hit.
    SM00179. EGF_CA. 3 hits.
    SM00069. GLA. 1 hit.
    SM00282. LamG. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 3 hits.
    SSF57184. SSF57184. 1 hit.
    SSF57630. SSF57630. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 4 hits.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 3 hits.
    PS50026. EGF_3. 4 hits.
    PS01187. EGF_CA. 3 hits.
    PS00011. GLA_1. 1 hit.
    PS50998. GLA_2. 1 hit.
    PS50025. LAM_G_DOMAIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The protein encoded by a growth arrest-specific gene (gas6) is a new member of the vitamin K-dependent proteins related to protein S, a negative coregulator in the blood coagulation cascade."
      Manfioletti G., Brancolini C., Avanzi G., Schneider C.
      Mol. Cell. Biol. 13:4976-4985(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    2. "Human vitamin K-dependent GAS6: gene structure, allelic variation, and association with stroke."
      Munoz X., Sumoy L., Ramirez-Lorca R., Villar J., de Frutos P.G., Sala N.
      Hum. Mutat. 23:506-512(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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 2; 3; 4 AND 5).
      Tissue: Kidney and Uterus.
    4. SeattleSNPs variation discovery resource
      Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-41; TYR-231; MET-390; ARG-543; LEU-623; LYS-655 AND GLN-659.
    5. "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].
    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 2).
      Tissue: Fetal lung and Fetal spleen.
    7. Maree A.O., Hillmann A., McRedmond J.P., Fitzgerald D.J.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85.
    8. "Axl receptor tyrosine kinase stimulated by the vitamin K-dependent protein encoded by growth-arrest-specific gene 6."
      Varnum B.C., Young C., Elliott G., Garcia A., Bartley T.D., Fridell Y.W., Hunt R.W., Trail G., Clogston C., Toso R.J., Yanagihara D., Bennett L., Silber M., Merewether L.A., Tseng A., Escobar E., Liu E.T., Yamane H.K.
      Nature 373:623-626(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECEPTOR INTERACTION.
    9. "The anticoagulation factor protein S and its relative, Gas6, are ligands for the Tyro 3/Axl family of receptor tyrosine kinases."
      Stitt T.N., Conn G., Gore M., Lai C., Bruno J., Radziejewski C., Mattsson K., Fisher J., Gies D.R., Jones P.F., Masiakowski P., Ryan T.E., Tobkes N.J., Chen D.H., DiStefano P.S., Long G.L., Basilico C., Goldfarb M.P.
      , Lemke G., Glass D.J., Yancopoulos G.D.
      Cell 80:661-670(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECEPTOR INTERACTION.
    10. "Identification and tissue expression of a splice variant for the growth arrest-specific gene gas6."
      Marcandalli P., Gostissa M., Varnum B., Goruppi S., Schneider C.
      FEBS Lett. 415:56-58(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 1), TISSUE SPECIFICITY.
    11. "Identification of the product of growth arrest-specific gene 6 as a common ligand for Axl, Sky, and Mer receptor tyrosine kinases."
      Nagata K., Ohashi K., Nakano T., Arita H., Zong C., Hanafusa H., Mizuno K.
      J. Biol. Chem. 271:30022-30027(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECEPTOR INTERACTION.
    12. "The product of a gas6 splice variant allows the release of the domain responsible for Axl tyrosine kinase receptor activation."
      Goruppi S., Yamane H., Marcandalli P., Garcia A., Clogston C., Gostissa M., Varnum B., Schneider C.
      FEBS Lett. 415:59-63(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECEPTOR INTERACTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
    13. "Acidification prevents endothelial cell apoptosis by Axl activation."
      D'Arcangelo D., Gaetano C., Capogrossi M.C.
      Circ. Res. 91:E4-12(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE GAS6/AXL SIGNALING PATHWAY.
    14. "The Axl/Gas6 pathway is required for optimal cytokine signaling during human natural killer cell development."
      Park I.K., Giovenzana C., Hughes T.L., Yu J., Trotta R., Caligiuri M.A.
      Blood 113:2470-2477(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE GAS6/AXL SIGNALING PATHWAY.
    15. "Characterization of Gas6, a member of the superfamily of G domain-containing proteins, as a ligand for Rse and Axl."
      Mark M.R., Chen J., Hammonds R.G., Sadick M., Godowski P.J.
      J. Biol. Chem. 271:9785-9789(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 261-721 (ISOFORM 2), MUTAGENESIS OF PHE-530; LEU-663 AND TYR-703, INTERACTION WITH AXL.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 322-721 IN COMPLEX WITH AXL, SUBUNIT, GLYCOSYLATION AT ASN-463, MUTAGENESIS OF ARG-353 AND LYS-355.

    Entry informationi

    Entry nameiGAS6_HUMAN
    AccessioniPrimary (citable) accession number: Q14393
    Secondary accession number(s): B3KRQ7
    , B3KVL4, E9PBL7, Q6IMN1, Q7Z7N3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 151 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