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Q14393 (GAS6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Growth arrest-specific protein 6

Short name=GAS-6
Alternative name(s):
AXL receptor tyrosine kinase ligand
Gene names
Name:GAS6
Synonyms:AXLLG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13 Ref.14

Subunit structure

Heterodimer and heterotetramer with AXL. Ref.16

Subcellular location

Secreted Ref.12.

Tissue specificity

Plasma. Isoform 1 and isoform 2 are widely expressed. Isoform 1 is the predominant form in spleen. Ref.1 Ref.10

Post-translational modification

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.

Sequence similarities

Contains 4 EGF-like domains.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Contains 2 laminin G-like domains.

Ontologies

Keywords
   Biological processGrowth regulation
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Gamma-carboxyglutamic acid
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell chemotaxis

Inferred from direct assay PubMed 19922767. Source: UniProtKB

activation of protein kinase B activity

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic cell clearance

Inferred from direct assay PubMed 21501828. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

calcium ion transmembrane transport

Inferred from direct assay PubMed 18395422. Source: UniProtKB

cell adhesion

Traceable author statement PubMed 16564713. Source: UniProtKB

cell cycle arrest

Traceable author statement PubMed 16564713. Source: UniProtKB

cell migration

Traceable author statement PubMed 16564713. Source: UniProtKB

cell proliferation

Traceable author statement PubMed 16564713. Source: UniProtKB

cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to drug

Inferred from direct assay PubMed 16359517. Source: UniProtKB

cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to interferon-alpha

Inferred from direct assay PubMed 19657094. Source: UniProtKB

cellular response to starvation

Inferred from electronic annotation. Source: Ensembl

cellular response to vitamin K

Inferred from direct assay PubMed 16359517. Source: UniProtKB

dendritic cell differentiation

Inferred from expression pattern PubMed 19657094. Source: UniProtKB

enzyme linked receptor protein signaling pathway

Inferred from electronic annotation. Source: Ensembl

extracellular matrix assembly

Inferred from sequence or structural similarity. Source: UniProtKB

fusion of virus membrane with host plasma membrane

Inferred from direct assay PubMed 21501828. Source: UniProtKB

hematopoietic stem cell migration to bone marrow

Inferred from direct assay PubMed 19922767. Source: UniProtKB

leukocyte migration

Traceable author statement. Source: Reactome

macrophage cytokine production

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay PubMed 19922767. Source: UniProtKB

negative regulation of biomineral tissue development

Inferred from direct assay PubMed 20048160. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 16723520. Source: UniProtKB

negative regulation of dendritic cell apoptotic process

Inferred from direct assay PubMed 19657094. Source: UniProtKB

negative regulation of endothelial cell apoptotic process

Inferred from direct assay PubMed 16359517PubMed 18680538PubMed 18760998. Source: UniProtKB

negative regulation of fibroblast apoptotic process

Inferred from direct assay PubMed 16359517. Source: UniProtKB

negative regulation of interferon-gamma production

Inferred from direct assay Ref.14. Source: UniProtKB

negative regulation of interleukin-1 secretion

Inferred from direct assay PubMed 20103767. Source: UniProtKB

negative regulation of interleukin-6 production

Inferred from direct assay PubMed 19657094. Source: UniProtKB

negative regulation of interleukin-6 secretion

Inferred from direct assay PubMed 20103767. Source: UniProtKB

negative regulation of oligodendrocyte apoptotic process

Inferred from direct assay PubMed 16723520. Source: UniProtKB

negative regulation of protein import into nucleus, translocation

Inferred from direct assay PubMed 20103767. Source: UniProtKB

negative regulation of renal albumin absorption

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 18680538. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18680538. Source: UniProtKB

negative regulation of tumor necrosis factor production

Inferred from direct assay PubMed 19657094PubMed 20103767. Source: UniProtKB

negative regulation of tumor necrosis factor-mediated signaling pathway

Inferred from direct assay PubMed 19657094. Source: UniProtKB

neuron migration

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

peptidyl-glutamic acid carboxylation

Traceable author statement. Source: Reactome

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 18680538PubMed 20103767. Source: UniProtKB

phagocytosis

Inferred from direct assay PubMed 21501828. Source: UniProtKB

platelet activation

Traceable author statement PubMed 16564713. Source: UniProtKB

platelet aggregation

Traceable author statement PubMed 16564713. Source: UniProtKB

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 15184064. Source: MGI

positive regulation of TOR signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine-mediated signaling pathway

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of dendritic cell chemotaxis

Inferred from direct assay PubMed 19657094. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of gene expression

Inferred from direct assay PubMed 19657094. Source: UniProtKB

positive regulation of glomerular filtration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of natural killer cell differentiation

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 16723520. Source: UniProtKB

positive regulation of phagocytosis

Inferred from direct assay PubMed 18395422. Source: UniProtKB

positive regulation of protein export from nucleus

Inferred from direct assay PubMed 18680538. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from direct assay PubMed 16359517PubMed 16723520PubMed 18680538. Source: UniProtKB

positive regulation of protein kinase activity

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 16723520PubMed 20103767Ref.8. Source: UniProtKB

positive regulation of protein tyrosine kinase activity

Inferred from direct assay PubMed 20103767. Source: UniProtKB

post-translational protein modification

Traceable author statement. Source: Reactome

protein kinase B signaling

Inferred from direct assay PubMed 16723520PubMed 20103767. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 16359517. Source: UniProtKB

protein targeting to plasma membrane

Inferred from direct assay PubMed 16359517. Source: UniProtKB

proteolysis

Traceable author statement. Source: Reactome

receptor-mediated virion attachment to host cell

Inferred from direct assay PubMed 21501828. Source: UniProtKB

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Inferred from direct assay PubMed 18680538Ref.8. Source: UniProtKB

viral entry into host cell

Inferred from direct assay PubMed 21501828. Source: UniProtKB

viral genome replication

Inferred from direct assay PubMed 21501828. Source: UniProtKB

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

cytoplasm

Inferred from direct assay PubMed 18395422. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 18395422PubMed 19922767PubMed 20088931. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionbinding, bridging

Inferred from direct assay PubMed 21501828. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from direct assay PubMed 16723520. Source: UniProtKB

phosphatidylserine binding

Inferred from direct assay PubMed 21501828. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18760998PubMed 20088931PubMed 20103767. Source: UniProtKB

protein tyrosine kinase activator activity

Inferred from direct assay PubMed 20103767. Source: UniProtKB

receptor agonist activity

Inferred from direct assay PubMed 15184064. Source: MGI

receptor binding

Inferred from direct assay PubMed 16359517. Source: UniProtKB

receptor tyrosine kinase binding

Inferred from physical interaction PubMed 7634325. Source: UniProtKB

voltage-gated calcium channel activity

Inferred from direct assay PubMed 18395422. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AXLP305308EBI-2802811,EBI-2850927

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14393-1)

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.
Isoform 2 (identifier: Q14393-2)

The sequence of this isoform differs from the canonical sequence as follows:
     279-321: Missing.
Isoform 3 (identifier: Q14393-3)

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.
Isoform 4 (identifier: Q14393-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-273: Missing.
     279-321: Missing.
Isoform 5 (identifier: Q14393-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-342: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 721691Growth arrest-specific protein 6
PRO_0000007589

Regions

Domain53 – 9442Gla
Domain116 – 15439EGF-like 1; calcium-binding Potential
Domain156 – 19641EGF-like 2; calcium-binding Potential
Domain197 – 23741EGF-like 3; calcium-binding Potential
Domain238 – 27841EGF-like 4; calcium-binding Potential
Domain341 – 513173Laminin G-like 1
Domain520 – 713194Laminin G-like 2

Sites

Metal binding3721Calcium
Metal binding3741Calcium; via carbonyl oxygen
Metal binding4831Calcium; via carbonyl oxygen
Metal binding6991Calcium

Amino acid modifications

Modified residue6641Phosphothreonine By similarity
Modified residue6801Phosphothreonine By similarity
Modified residue6831Phosphotyrosine By similarity
Glycosylation4631N-linked (GlcNAc...) Ref.16
Disulfide bond65 ↔ 70 By similarity
Disulfide bond120 ↔ 133 By similarity
Disulfide bond125 ↔ 142 By similarity
Disulfide bond144 ↔ 153 By similarity
Disulfide bond160 ↔ 171 By similarity
Disulfide bond167 ↔ 180 By similarity
Disulfide bond182 ↔ 195 By similarity
Disulfide bond201 ↔ 212 By similarity
Disulfide bond207 ↔ 221 By similarity
Disulfide bond223 ↔ 236 By similarity
Disulfide bond242 ↔ 251 By similarity
Disulfide bond247 ↔ 260 By similarity
Disulfide bond262 ↔ 277
Disulfide bond326 ↔ 613
Disulfide bond487 ↔ 513
Disulfide bond686 ↔ 713

Natural variations

Alternative sequence1 – 342342Missing in isoform 5.
VSP_045685
Alternative sequence1 – 273273Missing in isoform 4.
VSP_043832
Alternative sequence1 – 5454Missing in isoform 3.
VSP_010492
Alternative sequence55 – 9440EAKQG…PRYLD → MCMCQASPPPAALAGCLLSS CVQPAREHGGAFSKAEWLSN in isoform 3.
VSP_010493
Alternative sequence279 – 32143Missing in isoform 2, isoform 3 and isoform 4.
VSP_010494
Natural variant411F → L. Ref.4
VAR_038823
Natural variant2311S → Y. Ref.4
Corresponds to variant rs146159446 [ dbSNP | Ensembl ].
VAR_038824
Natural variant3901V → M. Ref.4
VAR_038825
Natural variant5431G → R. Ref.4
VAR_038826
Natural variant6231S → L. Ref.4
VAR_038827
Natural variant6551E → K. Ref.4
VAR_038828
Natural variant6591R → Q. Ref.4
VAR_038829

Experimental info

Mutagenesis3531R → E: Strongly reduced affinity for AXL. Abolishes phosphorylation of AXL. Ref.16
Mutagenesis3551K → E: Strongly reduced affinity for AXL. Abolishes phosphorylation of AXL. Ref.16
Mutagenesis5301F → A: Decreases activation of AXL. Ref.15
Mutagenesis6631L → A: Reduces affinity for AXL 15-fold and decreases activation of AXL. Ref.15
Mutagenesis7031Y → A: Reduces affinity for AXL 3-fold. Ref.15
Sequence conflict3991E → K in BAG52469. Ref.3

Secondary structure

............................................................................... 721
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (gas6SV) [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: E7B22B0E010930F9

FASTA72179,677
        10         20         30         40         50         60 
MAPSLSPGPA ALRRAPQLLL LLLAAECALA ALLPAREATQ FLRPRQRRAF QVFEEAKQGH 

        70         80         90        100        110        120 
LERECVEELC SREEAREVFE NDPETDYFYP RYLDCINKYG SPYTKNSGFA TCVQNLPDQC 

       130        140        150        160        170        180 
TPNPCDRKGT QACQDLMGNF FCLCKAGWGG RLCDKDVNEC SQENGGCLQI CHNKPGSFHC 

       190        200        210        220        230        240 
SCHSGFELSS DGRTCQDIDE CADSEACGEA RCKNLPGSYS CLCDEGFAYS SQEKACRDVD 

       250        260        270        280        290        300 
ECLQGRCEQV CVNSPGSYTC HCDGRGGLKL SQDMDTCELE AGWPCPRHRR DGSPAARPGR 

       310        320        330        340        350        360 
GAQGSRSEGH IPDRRGPRPW QDILPCVPFS VAKSVKSLYL GRMFSGTPVI RLRFKRLQPT 

       370        380        390        400        410        420 
RLVAEFDFRT FDPEGILLFA GGHQDSTWIV LALRAGRLEL QLRYNGVGRV TSSGPVINHG 

       430        440        450        460        470        480 
MWQTISVEEL ARNLVIKVNR DAVMKIAVAG DLFQPERGLY HLNLTVGGIP FHEKDLVQPI 

       490        500        510        520        530        540 
NPRLDGCMRS WNWLNGEDTT IQETVKVNTR MQCFSVTERG SFYPGSGFAF YSLDYMRTPL 

       550        560        570        580        590        600 
DVGTESTWEV EVVAHIRPAA DTGVLFALWA PDLRAVPLSV ALVDYHSTKK LKKQLVVLAV 

       610        620        630        640        650        660 
EHTALALMEI KVCDGQEHVV TVSLRDGEAT LEVDGTRGQS EVSAAQLQER LAVLERHLRS 

       670        680        690        700        710        720 
PVLTFAGGLP DVPVTSAPVT AFYRGCMTLE VNRRLLDLDE AAYKHSDITA HSCPPVEPAA 


A 

« Hide

Isoform 2 [UniParc].

Checksum: BB6D8AB0F6C48EA9
Show »

FASTA67874,925
Isoform 3 [UniParc].

Checksum: 6CCEBDDE139C9F53
Show »

FASTA62468,256
Isoform 4 [UniParc].

Checksum: ECF30C620FA69B60
Show »

FASTA40544,841
Isoform 5 [UniParc].

Checksum: A0EE62BA476927C6
Show »

FASTA37941,986

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Structural basis for Gas6-Axl signalling."
Sasaki T., Knyazev P.G., Clout N.J., Cheburkin Y., Goehring W., Ullrich A., Timpl R., Hohenester E.
EMBO J. 25:80-87(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13720 mRNA. Translation: AAA58494.1.
AY256843 expand/collapse EMBL AC list , 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.
CCDSCCDS45072.1. [Q14393-2]
CCDS45073.1. [Q14393-4]
CCDS45074.1. [Q14393-5]
PIRB48089.
RefSeqNP_000811.1. NM_000820.2. [Q14393-2]
NP_001137417.1. NM_001143945.1. [Q14393-4]
NP_001137418.1. NM_001143946.1. [Q14393-5]
UniGeneHs.646346.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H30X-ray2.20A261-721[»]
2C5DX-ray3.30A/B261-721[»]
ProteinModelPortalQ14393.
SMRQ14393. Positions 53-721.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108891. 4 interactions.
IntActQ14393. 3 interactions.
MINTMINT-2735698.
STRING9606.ENSP00000331831.

PTM databases

PhosphoSiteQ14393.

Polymorphism databases

DMDM48427995.

Proteomic databases

MaxQBQ14393.
PaxDbQ14393.
PRIDEQ14393.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327773; ENSP00000331831; ENSG00000183087. [Q14393-2]
ENST00000355761; ENSP00000348003; ENSG00000183087. [Q14393-3]
ENST00000418959; ENSP00000400117; ENSG00000183087. [Q14393-5]
ENST00000450766; ENSP00000416498; ENSG00000183087. [Q14393-4]
GeneID2621.
KEGGhsa:2621.
UCSCuc001vud.3. human. [Q14393-2]
uc001vuf.3. human. [Q14393-4]
uc001vug.3. human. [Q14393-1]

Organism-specific databases

CTD2621.
GeneCardsGC13M114523.
HGNCHGNC:4168. GAS6.
HPAHPA008275.
HPA056080.
MIM600441. gene.
neXtProtNX_Q14393.
PharmGKBPA28582.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149502.
HOGENOMHOG000065758.
HOVERGENHBG051702.
InParanoidQ14393.
KOK05464.
OrthoDBEOG7F5119.
PhylomeDBQ14393.
TreeFamTF352157.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
SignaLinkQ14393.

Gene expression databases

ArrayExpressQ14393.
BgeeQ14393.
CleanExHS_GAS6.
GenevestigatorQ14393.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
4.10.740.10. 1 hit.
InterProIPR017857. 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]
PfamPF07645. EGF_CA. 2 hits.
PF00594. Gla. 1 hit.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSPR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 3 hits.
SM00069. GLA. 1 hit.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 3 hits.
SSF57184. SSF57184. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

ChiTaRSGAS6. human.
EvolutionaryTraceQ14393.
GeneWikiGAS6.
GenomeRNAi2621.
NextBio10323.
PROQ14393.
SOURCESearch...

Entry information

Entry nameGAS6_HUMAN
AccessionPrimary (citable) accession number: Q14393
Secondary accession number(s): B3KRQ7 expand/collapse secondary AC list , B3KVL4, E9PBL7, Q6IMN1, Q7Z7N3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM