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Q14393

- GAS6_HUMAN

UniProt

Q14393 - GAS6_HUMAN

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Protein
Growth arrest-specific protein 6
Gene
GAS6, AXLLG
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

  1. B cell chemotaxis Source: UniProtKB
  2. activation of protein kinase B activity Source: UniProtKB
  3. apoptotic cell clearance 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 production Source: UniProtKB
  41. negative regulation of tumor necrosis factor-mediated signaling pathway 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 ERK1 and ERK2 cascade Source: MGI
  51. positive regulation of TOR signaling Source: UniProtKB
  52. positive regulation of cytokine-mediated signaling pathway Source: UniProtKB
  53. positive regulation of dendritic cell chemotaxis Source: UniProtKB
  54. positive regulation of fibroblast proliferation Source: UniProtKB
  55. positive regulation of gene expression Source: UniProtKB
  56. positive regulation of glomerular filtration Source: UniProtKB
  57. positive regulation of natural killer cell differentiation Source: UniProtKB
  58. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  59. positive regulation of phagocytosis Source: UniProtKB
  60. positive regulation of protein export from nucleus Source: UniProtKB
  61. positive regulation of protein kinase B signaling Source: UniProtKB
  62. positive regulation of protein kinase activity Source: UniProtKB
  63. positive regulation of protein phosphorylation Source: UniProtKB
  64. positive regulation of protein tyrosine kinase activity 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
Complete GO annotation...

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

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 – 3030 Reviewed prediction
Add
BLAST
Chaini31 – 721691Growth arrest-specific protein 6
PRO_0000007589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi65 ↔ 70 By similarity
Disulfide bondi120 ↔ 133 By similarity
Disulfide bondi125 ↔ 142 By similarity
Disulfide bondi144 ↔ 153 By similarity
Disulfide bondi160 ↔ 171 By similarity
Disulfide bondi167 ↔ 180 By similarity
Disulfide bondi182 ↔ 195 By similarity
Disulfide bondi201 ↔ 212 By similarity
Disulfide bondi207 ↔ 221 By similarity
Disulfide bondi223 ↔ 236 By similarity
Disulfide bondi242 ↔ 251 By similarity
Disulfide bondi247 ↔ 260 By similarity
Disulfide bondi262 ↔ 277
Disulfide bondi326 ↔ 613
Glycosylationi463 – 4631N-linked (GlcNAc...)1 Publication
Disulfide bondi487 ↔ 513
Modified residuei664 – 6641Phosphothreonine By similarity
Modified residuei680 – 6801Phosphothreonine By similarity
Modified residuei683 – 6831Phosphotyrosine By 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.
Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium By similarity.

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

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.

Miscellaneous databases

EvolutionaryTraceiQ14393.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 9442Gla
Add
BLAST
Domaini116 – 15439EGF-like 1; calcium-binding Reviewed prediction
Add
BLAST
Domaini156 – 19641EGF-like 2; calcium-binding Reviewed prediction
Add
BLAST
Domaini197 – 23741EGF-like 3; calcium-binding Reviewed prediction
Add
BLAST
Domaini238 – 27841EGF-like 4; calcium-binding Reviewed prediction
Add
BLAST
Domaini341 – 513173Laminin G-like 1
Add
BLAST
Domaini520 – 713194Laminin G-like 2
Add
BLAST

Sequence similaritiesi

Contains 4 EGF-like domains.

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

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.
VSP_045685Add
BLAST
Alternative sequencei1 – 273273Missing in isoform 4.
VSP_043832Add
BLAST
Alternative sequencei1 – 5454Missing in isoform 3.
VSP_010492Add
BLAST
Alternative sequencei55 – 9440EAKQG…PRYLD → MCMCQASPPPAALAGCLLSS CVQPAREHGGAFSKAEWLSN in isoform 3.
VSP_010493Add
BLAST
Alternative sequencei279 – 32143Missing in isoform 2, isoform 3 and isoform 4.
VSP_010494Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti399 – 3991E → K in BAG52469. 1 Publication

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]
ENST00000355761; ENSP00000348003; ENSG00000183087. [Q14393-3]
ENST00000418959; ENSP00000400117; ENSG00000183087. [Q14393-5]
ENST00000450766; ENSP00000416498; ENSG00000183087. [Q14393-4]
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...

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 ]
ENST00000355761 ; ENSP00000348003 ; ENSG00000183087 . [Q14393-3 ]
ENST00000418959 ; ENSP00000400117 ; ENSG00000183087 . [Q14393-5 ]
ENST00000450766 ; ENSP00000416498 ; ENSG00000183087 . [Q14393-4 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 150 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

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