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Protein

Growth arrest-specific protein 6

Gene

GAS6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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
(Microbial infection) Can bridges virus envelope phosphatidylserine to the TAM receptor tyrosine kinase Axl to mediate viral entry by apoptotic mimicry (PubMed:21501828). Plays a role in Dengue cell entry by apoptotic mimicry (PubMed:23084921). Plays a role in Vaccinia virus cell entry by apoptotic mimicry (PubMed:21501828). Plays a role in ebolavirus and marburgvirus cell entry by apoptotic mimicry (PubMed:17005688).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi372Calcium1
Metal bindingi374Calcium; via carbonyl oxygen1
Metal bindingi483Calcium; via carbonyl oxygen1
Metal bindingi699Calcium1

GO - Molecular functioni

  • binding, bridging Source: UniProtKB
  • calcium ion binding Source: InterPro
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  • phosphatidylserine binding Source: UniProtKB
  • protein tyrosine kinase activator activity Source: UniProtKB
  • receptor agonist activity Source: MGI
  • receptor binding Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB
  • voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  • activation of protein kinase B activity Source: UniProtKB
  • animal organ regeneration Source: Ensembl
  • apoptotic cell clearance Source: UniProtKB
  • B cell chemotaxis Source: UniProtKB
  • calcium ion transmembrane transport Source: UniProtKB
  • cell adhesion Source: UniProtKB
  • cell cycle arrest Source: UniProtKB
  • cell migration Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • cell-substrate adhesion Source: Ensembl
  • cellular response to drug Source: UniProtKB
  • cellular response to glucose stimulus Source: UniProtKB
  • cellular response to growth factor stimulus Source: Ensembl
  • cellular response to interferon-alpha Source: UniProtKB
  • cellular response to starvation Source: Ensembl
  • cellular response to vitamin K Source: UniProtKB
  • dendritic cell differentiation Source: UniProtKB
  • enzyme linked receptor protein signaling pathway Source: Ensembl
  • ER to Golgi vesicle-mediated transport Source: Reactome
  • extracellular matrix assembly Source: UniProtKB
  • fusion of virus membrane with host plasma membrane Source: UniProtKB
  • hematopoietic stem cell migration to bone marrow Source: UniProtKB
  • leukocyte migration Source: Reactome
  • macrophage cytokine production Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of biomineral tissue development Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of dendritic cell apoptotic process Source: UniProtKB
  • negative regulation of endothelial cell apoptotic process Source: UniProtKB
  • negative regulation of fibroblast apoptotic process Source: UniProtKB
  • negative regulation of interferon-gamma production Source: UniProtKB
  • negative regulation of interleukin-1 secretion Source: UniProtKB
  • negative regulation of interleukin-6 production Source: UniProtKB
  • negative regulation of interleukin-6 secretion Source: UniProtKB
  • negative regulation of oligodendrocyte apoptotic process Source: UniProtKB
  • negative regulation of protein import into nucleus, translocation Source: UniProtKB
  • negative regulation of renal albumin absorption Source: UniProtKB
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
  • negative regulation of tumor necrosis factor production Source: UniProtKB
  • neuron migration Source: Ensembl
  • peptidyl-serine phosphorylation Source: UniProtKB
  • phagocytosis Source: UniProtKB
  • platelet activation Source: UniProtKB
  • platelet aggregation Source: UniProtKB
  • platelet degranulation Source: Reactome
  • positive regulation of cytokine-mediated signaling pathway Source: UniProtKB
  • positive regulation of dendritic cell chemotaxis Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: MGI
  • positive regulation of fibroblast proliferation Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of glomerular filtration Source: UniProtKB
  • positive regulation of natural killer cell differentiation Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  • positive regulation of phagocytosis Source: UniProtKB
  • positive regulation of protein export from nucleus Source: UniProtKB
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of protein tyrosine kinase activity Source: UniProtKB
  • positive regulation of TOR signaling Source: UniProtKB
  • protein kinase B signaling Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • protein targeting to plasma membrane Source: UniProtKB
  • receptor-mediated virion attachment to host cell Source: UniProtKB
  • regulation of growth Source: UniProtKB-KW
  • signal peptide processing Source: Reactome
  • signal transduction Source: UniProtKB
  • viral entry into host cell Source: UniProtKB
  • viral genome replication Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Growth regulation, Host-virus interaction

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:G66-32537-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-159740. Gamma-carboxylation of protein precursors.
R-HSA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
R-HSA-202733. Cell surface interactions at the vascular wall.
SignaLinkiQ14393.
SIGNORiQ14393.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:4168. GAS6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • Golgi lumen Source: Reactome
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi353R → E: Strongly reduced affinity for AXL. Abolishes phosphorylation of AXL. 1 Publication1
Mutagenesisi355K → E: Strongly reduced affinity for AXL. Abolishes phosphorylation of AXL. 1 Publication1
Mutagenesisi530F → A: Decreases activation of AXL. 1 Publication1
Mutagenesisi663L → A: Reduces affinity for AXL 15-fold and decreases activation of AXL. 1 Publication1
Mutagenesisi703Y → A: Reduces affinity for AXL 3-fold. 1 Publication1

Organism-specific databases

DisGeNETi2621.
OpenTargetsiENSG00000183087.
PharmGKBiPA28582.

Polymorphism and mutation databases

BioMutaiGAS6.
DMDMi48427995.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000000758931 – 721Growth arrest-specific protein 6Add BLAST691

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi65 ↔ 70By similarity
Modified residuei71Phosphoserine; by FAM20C1 Publication1
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
Glycosylationi463N-linked (GlcNAc...)1 Publication1
Disulfide bondi487 ↔ 513
Modified residuei664PhosphothreonineBy similarity1
Modified residuei680PhosphothreonineBy similarity1
Modified residuei683PhosphotyrosineBy similarity1
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

EPDiQ14393.
MaxQBiQ14393.
PeptideAtlasiQ14393.
PRIDEiQ14393.

PTM databases

iPTMnetiQ14393.
PhosphoSitePlusiQ14393.

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

BgeeiENSG00000183087.
CleanExiHS_GAS6.
GenevisibleiQ14393. HS.

Organism-specific databases

HPAiHPA008275.
HPA056080.

Interactioni

Subunit structurei

Heterodimer and heterotetramer with AXL.1 Publication

Binary interactionsi

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

GO - Molecular functioni

  • receptor agonist activity Source: MGI
  • receptor binding Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108891. 24 interactors.
IntActiQ14393. 13 interactors.
MINTiMINT-2735698.

Structurei

Secondary structure

1721
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi264 – 266Combined sources3
Beta strandi268 – 271Combined sources4
Turni272 – 275Combined sources4
Beta strandi276 – 278Combined sources3
Beta strandi337 – 339Combined sources3
Beta strandi350 – 353Combined sources4
Beta strandi356 – 358Combined sources3
Beta strandi363 – 370Combined sources8
Beta strandi373 – 382Combined sources10
Beta strandi386 – 394Combined sources9
Beta strandi397 – 404Combined sources8
Beta strandi407 – 416Combined sources10
Beta strandi419 – 421Combined sources3
Beta strandi423 – 429Combined sources7
Beta strandi431 – 438Combined sources8
Beta strandi441 – 447Combined sources7
Beta strandi452 – 456Combined sources5
Beta strandi459 – 461Combined sources3
Beta strandi463 – 468Combined sources6
Helixi473 – 475Combined sources3
Beta strandi476 – 478Combined sources3
Beta strandi486 – 493Combined sources8
Helixi501 – 507Combined sources7
Helixi509 – 511Combined sources3
Beta strandi512 – 516Combined sources5
Beta strandi518 – 523Combined sources6
Beta strandi529 – 531Combined sources3
Beta strandi550 – 561Combined sources12
Beta strandi563 – 570Combined sources8
Helixi571 – 573Combined sources3
Beta strandi575 – 584Combined sources10
Beta strandi588 – 590Combined sources3
Beta strandi595 – 600Combined sources6
Beta strandi603 – 609Combined sources7
Beta strandi618 – 625Combined sources8
Beta strandi628 – 633Combined sources6
Beta strandi639 – 642Combined sources4
Helixi644 – 658Combined sources15
Beta strandi663 – 667Combined sources5
Beta strandi676 – 678Combined sources3
Beta strandi685 – 691Combined sources7
Helixi698 – 700Combined sources3
Beta strandi701 – 704Combined sources4
Beta strandi708 – 711Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H30X-ray2.20A261-721[»]
2C5DX-ray3.30A/B261-721[»]
4RA0X-ray3.07A/B322-721[»]
ProteinModelPortaliQ14393.
SMRiQ14393.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14393.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 94GlaPROSITE-ProRule annotationAdd BLAST42
Domaini116 – 154EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini156 – 196EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini197 – 237EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini238 – 278EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini341 – 513Laminin G-like 1PROSITE-ProRule annotationAdd BLAST173
Domaini520 – 713Laminin G-like 2PROSITE-ProRule annotationAdd BLAST194

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

GeneTreeiENSGT00530000063339.
HOGENOMiHOG000065758.
HOVERGENiHBG051702.
InParanoidiQ14393.
KOiK05464.
OMAiPVIRLRF.
OrthoDBiEOG091G034Z.
PhylomeDBiQ14393.
TreeFamiTF352157.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
4.10.740.10. 1 hit.
InterProiIPR026823. cEGF.
IPR017857. Coagulation_fac_subgr_Gla_dom.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR009030. Growth_fac_rcpt_.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00594. Gla. 1 hit.
PF12661. hEGF. 2 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSiPR00001. GLABLOOD.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 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. AlignAdd to basket

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

        10         20         30         40         50
MAPSLSPGPA ALRRAPQLLL LLLAAECALA ALLPAREATQ FLRPRQRRAF
60 70 80 90 100
QVFEEAKQGH LERECVEELC SREEAREVFE NDPETDYFYP RYLDCINKYG
110 120 130 140 150
SPYTKNSGFA TCVQNLPDQC TPNPCDRKGT QACQDLMGNF FCLCKAGWGG
160 170 180 190 200
RLCDKDVNEC SQENGGCLQI CHNKPGSFHC SCHSGFELSS DGRTCQDIDE
210 220 230 240 250
CADSEACGEA RCKNLPGSYS CLCDEGFAYS SQEKACRDVD ECLQGRCEQV
260 270 280 290 300
CVNSPGSYTC HCDGRGGLKL SQDMDTCELE AGWPCPRHRR DGSPAARPGR
310 320 330 340 350
GAQGSRSEGH IPDRRGPRPW QDILPCVPFS VAKSVKSLYL GRMFSGTPVI
360 370 380 390 400
RLRFKRLQPT RLVAEFDFRT FDPEGILLFA GGHQDSTWIV LALRAGRLEL
410 420 430 440 450
QLRYNGVGRV TSSGPVINHG MWQTISVEEL ARNLVIKVNR DAVMKIAVAG
460 470 480 490 500
DLFQPERGLY HLNLTVGGIP FHEKDLVQPI NPRLDGCMRS WNWLNGEDTT
510 520 530 540 550
IQETVKVNTR MQCFSVTERG SFYPGSGFAF YSLDYMRTPL DVGTESTWEV
560 570 580 590 600
EVVAHIRPAA DTGVLFALWA PDLRAVPLSV ALVDYHSTKK LKKQLVVLAV
610 620 630 640 650
EHTALALMEI KVCDGQEHVV TVSLRDGEAT LEVDGTRGQS EVSAAQLQER
660 670 680 690 700
LAVLERHLRS PVLTFAGGLP DVPVTSAPVT AFYRGCMTLE VNRRLLDLDE
710 720
AAYKHSDITA HSCPPVEPAA A
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)DescriptionActionsGraphical viewLength
Sequence conflicti399E → K in BAG52469 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03882341F → L.1 Publication1
Natural variantiVAR_038824231S → Y.1 PublicationCorresponds to variant rs146159446dbSNPEnsembl.1
Natural variantiVAR_038825390V → M.1 Publication1
Natural variantiVAR_038826543G → R.1 Publication1
Natural variantiVAR_038827623S → L.1 Publication1
Natural variantiVAR_038828655E → K.1 Publication1
Natural variantiVAR_038829659R → Q.1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0456851 – 342Missing in isoform 5. 1 PublicationAdd BLAST342
Alternative sequenceiVSP_0438321 – 273Missing in isoform 4. 1 PublicationAdd BLAST273
Alternative sequenceiVSP_0104921 – 54Missing in isoform 3. 1 PublicationAdd BLAST54
Alternative sequenceiVSP_01049355 – 94EAKQG…PRYLD → MCMCQASPPPAALAGCLLSS CVQPAREHGGAFSKAEWLSN in isoform 3. 1 PublicationAdd BLAST40
Alternative sequenceiVSP_010494279 – 321Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsAdd BLAST43

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
PIRiB48089.
RefSeqiNP_000811.1. NM_000820.3. [Q14393-2]
UniGeneiHs.646346.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
PIRiB48089.
RefSeqiNP_000811.1. NM_000820.3. [Q14393-2]
UniGeneiHs.646346.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H30X-ray2.20A261-721[»]
2C5DX-ray3.30A/B261-721[»]
4RA0X-ray3.07A/B322-721[»]
ProteinModelPortaliQ14393.
SMRiQ14393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108891. 24 interactors.
IntActiQ14393. 13 interactors.
MINTiMINT-2735698.

PTM databases

iPTMnetiQ14393.
PhosphoSitePlusiQ14393.

Polymorphism and mutation databases

BioMutaiGAS6.
DMDMi48427995.

Proteomic databases

EPDiQ14393.
MaxQBiQ14393.
PeptideAtlasiQ14393.
PRIDEiQ14393.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2621.
DisGeNETi2621.
GeneCardsiGAS6.
HGNCiHGNC:4168. GAS6.
HPAiHPA008275.
HPA056080.
MIMi600441. gene.
neXtProtiNX_Q14393.
OpenTargetsiENSG00000183087.
PharmGKBiPA28582.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000063339.
HOGENOMiHOG000065758.
HOVERGENiHBG051702.
InParanoidiQ14393.
KOiK05464.
OMAiPVIRLRF.
OrthoDBiEOG091G034Z.
PhylomeDBiQ14393.
TreeFamiTF352157.

Enzyme and pathway databases

BioCyciZFISH:G66-32537-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-159740. Gamma-carboxylation of protein precursors.
R-HSA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
R-HSA-202733. Cell surface interactions at the vascular wall.
SignaLinkiQ14393.
SIGNORiQ14393.

Miscellaneous databases

ChiTaRSiGAS6. human.
EvolutionaryTraceiQ14393.
GeneWikiiGAS6.
GenomeRNAii2621.
PROiQ14393.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000183087.
CleanExiHS_GAS6.
GenevisibleiQ14393. HS.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
4.10.740.10. 1 hit.
InterProiIPR026823. cEGF.
IPR017857. Coagulation_fac_subgr_Gla_dom.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR009030. Growth_fac_rcpt_.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00594. Gla. 1 hit.
PF12661. hEGF. 2 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSiPR00001. GLABLOOD.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 172 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.