SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q12866

- MERTK_HUMAN

UniProt

Q12866 - MERTK_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tyrosine-protein kinase Mer

Gene
MERTK, MER
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei615 – 6151ATP By similarity
Active sitei723 – 7231Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi593 – 6019ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. transmembrane receptor protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

  1. apoptotic cell clearance Source: Ensembl
  2. blood coagulation Source: Reactome
  3. cell-cell signaling Source: ProtInc
  4. cell surface receptor signaling pathway Source: ProtInc
  5. leukocyte migration Source: Reactome
  6. natural killer cell differentiation Source: Ensembl
  7. negative regulation of lymphocyte activation Source: Ensembl
  8. peptidyl-tyrosine phosphorylation Source: GOC
  9. phagocytosis Source: BHF-UCL
  10. platelet activation Source: Ensembl
  11. positive regulation of phagocytosis Source: UniProtKB
  12. protein kinase B signaling Source: Ensembl
  13. protein phosphorylation Source: ProtInc
  14. retina development in camera-type eye Source: Ensembl
  15. secretion by cell Source: Ensembl
  16. spermatogenesis Source: Ensembl
  17. substrate adhesion-dependent cell spreading Source: Ensembl
  18. vagina development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
SignaLinkiQ12866.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Mer (EC:2.7.10.1)
Alternative name(s):
Proto-oncogene c-Mer
Receptor tyrosine kinase MerTK
Gene namesi
Name:MERTK
Synonyms:MER
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:7027. MERTK.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 505485Extracellular Reviewed predictionAdd
BLAST
Transmembranei506 – 52621Helical; Reviewed predictionAdd
BLAST
Topological domaini527 – 999473Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular space Source: UniProtKB
  3. integral component of plasma membrane Source: ProtInc
  4. photoreceptor outer segment Source: Ensembl
  5. plasma membrane Source: Reactome
  6. rhabdomere Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 38 (RP38) [MIM:613862]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti540 – 5401E → K in RP38. 1 Publication
Corresponds to variant rs113485015 [ dbSNP | Ensembl ].
VAR_021046
Natural varianti661 – 6611S → C in RP38. 1 Publication
VAR_021047
Natural varianti871 – 8711I → T in RP38. 1 Publication
VAR_021048

Keywords - Diseasei

Disease mutation, Proto-oncogene, Retinitis pigmentosa

Organism-specific databases

MIMi613862. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA30759.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed predictionAdd
BLAST
Chaini21 – 999979Tyrosine-protein kinase MerPRO_0000024443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi114 – 1141N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi115 ↔ 175 By similarity
Glycosylationi170 – 1701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi207 – 2071N-linked (GlcNAc...) Reviewed prediction
Glycosylationi215 – 2151N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi218 ↔ 262 By similarity
Glycosylationi234 – 2341N-linked (GlcNAc...) Reviewed prediction
Glycosylationi294 – 2941N-linked (GlcNAc...) Reviewed prediction
Glycosylationi316 – 3161N-linked (GlcNAc...) Reviewed prediction
Glycosylationi329 – 3291N-linked (GlcNAc...) Reviewed prediction
Glycosylationi336 – 3361N-linked (GlcNAc...) Reviewed prediction
Glycosylationi354 – 3541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi389 – 3891N-linked (GlcNAc...) Reviewed prediction
Glycosylationi395 – 3951N-linked (GlcNAc...) Reviewed prediction
Glycosylationi442 – 4421N-linked (GlcNAc...)1 Publication
Glycosylationi454 – 4541N-linked (GlcNAc...) Reviewed prediction
Modified residuei543 – 5431Phosphoserine1 Publication
Modified residuei749 – 7491Phosphotyrosine; by autocatalysis1 Publication
Modified residuei753 – 7531Phosphotyrosine; by autocatalysis1 Publication
Modified residuei754 – 7541Phosphotyrosine; by autocatalysis1 Publication
Modified residuei872 – 8721Phosphotyrosine; by autocatalysis By similarity
Modified residuei935 – 9351Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated on Tyr-749, Tyr-753 and Tyr-754 in the activation loop allowing full activity. Autophosphorylated on Tyr-872 leading to recruitment of downstream partners of the signaling cascade such as PLCG2 By similarity.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ12866.
PaxDbiQ12866.
PRIDEiQ12866.

PTM databases

PhosphoSiteiQ12866.

Expressioni

Tissue specificityi

Not expressed in normal B- and T-lymphocytes but is expressed in numerous neoplastic B- and T-cell lines. Highly expressed in testis, ovary, prostate, lung, and kidney, with lower expression in spleen, small intestine, colon, and liver.

Gene expression databases

ArrayExpressiQ12866.
BgeeiQ12866.
CleanExiHS_MERTK.
GenevestigatoriQ12866.

Organism-specific databases

HPAiHPA036196.

Interactioni

Subunit structurei

Interacts (upon activation) with TNK2; stimulates TNK2 autophosphorylation. Interacts (via N-terminus) with extracellular ligands LGALS3, TUB, TULP1 and GAS6 By similarity. Interacts with VAV1 in a phosphotyrosine-independent manner.4 Publications

Protein-protein interaction databases

BioGridi115724. 8 interactions.
IntActiQ12866. 3 interactions.
STRINGi9606.ENSP00000295408.

Structurei

Secondary structure

1
999
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi388 – 3947
Beta strandi396 – 40611
Beta strandi417 – 42812
Beta strandi431 – 44111
Beta strandi446 – 4494
Beta strandi453 – 4597
Beta strandi461 – 4677
Beta strandi476 – 4794
Turni577 – 5804
Helixi584 – 5863
Beta strandi587 – 5948
Beta strandi601 – 6077
Beta strandi613 – 6208
Helixi628 – 64215
Beta strandi654 – 6574
Beta strandi667 – 6726
Helixi679 – 6857
Beta strandi688 – 6925
Helixi697 – 71519
Turni716 – 7183
Helixi726 – 7283
Beta strandi729 – 7313
Beta strandi737 – 7393
Helixi764 – 7663
Helixi769 – 7735
Helixi779 – 79416
Helixi806 – 8083
Helixi809 – 8146
Beta strandi822 – 8243
Helixi827 – 8359
Helixi841 – 8433
Helixi847 – 86014

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DBJNMR-A373-483[»]
2P0CX-ray2.40A/B570-864[»]
3BPRX-ray2.80A/B/C/D570-864[»]
3BRBX-ray1.90A/B570-864[»]
3TCPX-ray2.69A/B570-864[»]
4M3QX-ray2.72A/B570-864[»]
4MH7X-ray2.51A/B570-864[»]
4MHAX-ray2.59A/B570-864[»]
ProteinModelPortaliQ12866.
SMRiQ12866. Positions 103-281, 283-492, 575-900.

Miscellaneous databases

EvolutionaryTraceiQ12866.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 186106Ig-like C2-type 1Add
BLAST
Domaini197 – 27377Ig-like C2-type 2Add
BLAST
Domaini286 – 38196Fibronectin type-III 1Add
BLAST
Domaini386 – 48499Fibronectin type-III 2Add
BLAST
Domaini587 – 858272Protein kinaseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000231685.
HOVERGENiHBG006346.
InParanoidiQ12866.
KOiK05117.
OMAiNEIGWSA.
OrthoDBiEOG77DJ5C.
PhylomeDBiQ12866.
TreeFamiTF317402.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 2 hits.
SM00409. IG. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50853. FN3. 2 hits.
PS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q12866-1 [UniParc]FASTAAdd to Basket

« Hide

MGPAPLPLLL GLFLPALWRR AITEAREEAK PYPLFPGPFP GSLQTDHTPL    50
LSLPHASGYQ PALMFSPTQP GRPHTGNVAI PQVTSVESKP LPPLAFKHTV 100
GHIILSEHKG VKFNCSISVP NIYQDTTISW WKDGKELLGA HHAITQFYPD 150
DEVTAIIASF SITSVQRSDN GSYICKMKIN NEEIVSDPIY IEVQGLPHFT 200
KQPESMNVTR NTAFNLTCQA VGPPEPVNIF WVQNSSRVNE QPEKSPSVLT 250
VPGLTEMAVF SCEAHNDKGL TVSKGVQINI KAIPSPPTEV SIRNSTAHSI 300
LISWVPGFDG YSPFRNCSIQ VKEADPLSNG SVMIFNTSAL PHLYQIKQLQ 350
ALANYSIGVS CMNEIGWSAV SPWILASTTE GAPSVAPLNV TVFLNESSDN 400
VDIRWMKPPT KQQDGELVGY RISHVWQSAG ISKELLEEVG QNGSRARISV 450
QVHNATCTVR IAAVTRGGVG PFSDPVKIFI PAHGWVDYAP SSTPAPGNAD 500
PVLIIFGCFC GFILIGLILY ISLAIRKRVQ ETKFGNAFTE EDSELVVNYI 550
AKKSFCRRAI ELTLHSLGVS EELQNKLEDV VIDRNLLILG KILGEGEFGS 600
VMEGNLKQED GTSLKVAVKT MKLDNSSQRE IEEFLSEAAC MKDFSHPNVI 650
RLLGVCIEMS SQGIPKPMVI LPFMKYGDLH TYLLYSRLET GPKHIPLQTL 700
LKFMVDIALG MEYLSNRNFL HRDLAARNCM LRDDMTVCVA DFGLSKKIYS 750
GDYYRQGRIA KMPVKWIAIE SLADRVYTSK SDVWAFGVTM WEIATRGMTP 800
YPGVQNHEMY DYLLHGHRLK QPEDCLDELY EIMYSCWRTD PLDRPTFSVL 850
RLQLEKLLES LPDVRNQADV IYVNTQLLES SEGLAQGSTL APLDLNIDPD 900
SIIASCTPRA AISVVTAEVH DSKPHEGRYI LNGGSEEWED LTSAPSAAVT 950
AEKNSVLPGE RLVRNGVSWS HSSMLPLGSS LPDELLFADD SSEGSEVLM 999
Length:999
Mass (Da):110,249
Last modified:November 13, 2007 - v2
Checksum:i05BC339F05DFD355
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201R → S.2 Publications
Corresponds to variant rs35898499 [ dbSNP | Ensembl ].
VAR_021039
Natural varianti118 – 1181S → N.3 Publications
Corresponds to variant rs13027171 [ dbSNP | Ensembl ].
VAR_021040
Natural varianti185 – 1851V → M.1 Publication
Corresponds to variant rs56205303 [ dbSNP | Ensembl ].
VAR_041741
Natural varianti214 – 2141F → V Found in a patient with Leber congenital amaurosis. 1 Publication
VAR_067194
Natural varianti282 – 2821A → T.2 Publications
Corresponds to variant rs7588635 [ dbSNP | Ensembl ].
VAR_021041
Natural varianti289 – 2891E → K.1 Publication
VAR_041742
Natural varianti293 – 2931R → H.2 Publications
Corresponds to variant rs34072093 [ dbSNP | Ensembl ].
VAR_021042
Natural varianti329 – 3291N → S.
Corresponds to variant rs34943572 [ dbSNP | Ensembl ].
VAR_051698
Natural varianti446 – 4461A → G in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
VAR_041743
Natural varianti452 – 4521V → L.1 Publication
Corresponds to variant rs34010621 [ dbSNP | Ensembl ].
VAR_041744
Natural varianti466 – 4661R → K.2 Publications
Corresponds to variant rs7604639 [ dbSNP | Ensembl ].
VAR_021043
Natural varianti498 – 4981N → S.2 Publications
Corresponds to variant rs35858762 [ dbSNP | Ensembl ].
VAR_021044
Natural varianti518 – 5181I → V.2 Publications
Corresponds to variant rs2230515 [ dbSNP | Ensembl ].
VAR_021045
Natural varianti540 – 5401E → K in RP38. 1 Publication
Corresponds to variant rs113485015 [ dbSNP | Ensembl ].
VAR_021046
Natural varianti661 – 6611S → C in RP38. 1 Publication
VAR_021047
Natural varianti662 – 6621Q → E.1 Publication
Corresponds to variant rs56209758 [ dbSNP | Ensembl ].
VAR_041745
Natural varianti708 – 7081A → S in a head & Neck squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_041746
Natural varianti823 – 8231E → Q.1 Publication
Corresponds to variant rs55924349 [ dbSNP | Ensembl ].
VAR_041747
Natural varianti865 – 8651R → W.1 Publication
Corresponds to variant rs2230516 [ dbSNP | Ensembl ].
VAR_020285
Natural varianti870 – 8701V → I.1 Publication
Corresponds to variant rs2230517 [ dbSNP | Ensembl ].
VAR_029237
Natural varianti871 – 8711I → T in RP38. 1 Publication
VAR_021048
Natural varianti871 – 8711I → V.1 Publication
VAR_021049
Natural varianti958 – 9581P → L Found in a patient with Leber congenital amaurosis. 1 Publication
Corresponds to variant rs201460398 [ dbSNP | Ensembl ].
VAR_067195

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401A → G in AAB60430. 1 Publication
Sequence conflicti143 – 1431A → R in AAB60430. 1 Publication
Sequence conflicti247 – 2471S → G in AAB60430. 1 Publication
Sequence conflicti274 – 2741K → Q in AAB60430. 1 Publication
Sequence conflicti328 – 3281S → G in AAB60430. 1 Publication
Sequence conflicti628 – 6281Q → H in AAB60430. 1 Publication
Sequence conflicti794 – 7941A → R in AAB60430. 1 Publication
Sequence conflicti888 – 8881S → P in AAB60430. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08023 mRNA. Translation: AAB60430.1.
AH010001 Genomic DNA. Translation: AAG33129.1.
AC093675 Genomic DNA. No translation available.
AC104651 Genomic DNA. No translation available.
CCDSiCCDS2094.1.
PIRiI38547.
RefSeqiNP_006334.2. NM_006343.2.
UniGeneiHs.306178.

Genome annotation databases

EnsembliENST00000295408; ENSP00000295408; ENSG00000153208.
ENST00000421804; ENSP00000389152; ENSG00000153208.
GeneIDi10461.
KEGGihsa:10461.
UCSCiuc002thk.1. human.

Polymorphism databases

DMDMi160332297.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Mutations of the MERTK gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08023 mRNA. Translation: AAB60430.1 .
AH010001 Genomic DNA. Translation: AAG33129.1 .
AC093675 Genomic DNA. No translation available.
AC104651 Genomic DNA. No translation available.
CCDSi CCDS2094.1.
PIRi I38547.
RefSeqi NP_006334.2. NM_006343.2.
UniGenei Hs.306178.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DBJ NMR - A 373-483 [» ]
2P0C X-ray 2.40 A/B 570-864 [» ]
3BPR X-ray 2.80 A/B/C/D 570-864 [» ]
3BRB X-ray 1.90 A/B 570-864 [» ]
3TCP X-ray 2.69 A/B 570-864 [» ]
4M3Q X-ray 2.72 A/B 570-864 [» ]
4MH7 X-ray 2.51 A/B 570-864 [» ]
4MHA X-ray 2.59 A/B 570-864 [» ]
ProteinModelPortali Q12866.
SMRi Q12866. Positions 103-281, 283-492, 575-900.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115724. 8 interactions.
IntActi Q12866. 3 interactions.
STRINGi 9606.ENSP00000295408.

Chemistry

BindingDBi Q12866.
ChEMBLi CHEMBL5331.
GuidetoPHARMACOLOGYi 1837.

Protein family/group databases

MEROPSi I43.001.

PTM databases

PhosphoSitei Q12866.

Polymorphism databases

DMDMi 160332297.

Proteomic databases

MaxQBi Q12866.
PaxDbi Q12866.
PRIDEi Q12866.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295408 ; ENSP00000295408 ; ENSG00000153208 .
ENST00000421804 ; ENSP00000389152 ; ENSG00000153208 .
GeneIDi 10461.
KEGGi hsa:10461.
UCSCi uc002thk.1. human.

Organism-specific databases

CTDi 10461.
GeneCardsi GC02P112656.
GeneReviewsi MERTK.
H-InvDB HIX0002374.
HGNCi HGNC:7027. MERTK.
HPAi HPA036196.
MIMi 604705. gene.
613862. phenotype.
neXtProti NX_Q12866.
Orphaneti 791. Retinitis pigmentosa.
PharmGKBi PA30759.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000231685.
HOVERGENi HBG006346.
InParanoidi Q12866.
KOi K05117.
OMAi NEIGWSA.
OrthoDBi EOG77DJ5C.
PhylomeDBi Q12866.
TreeFami TF317402.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
Reactomei REACT_12051. Cell surface interactions at the vascular wall.
SignaLinki Q12866.

Miscellaneous databases

ChiTaRSi MERTK. human.
EvolutionaryTracei Q12866.
GeneWikii MERTK.
GenomeRNAii 10461.
NextBioi 39667.
PROi Q12866.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q12866.
Bgeei Q12866.
CleanExi HS_MERTK.
Genevestigatori Q12866.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
InterProi IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF00041. fn3. 1 hit.
PF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00060. FN3. 2 hits.
SM00409. IG. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50853. FN3. 2 hits.
PS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and mRNA expression analysis of a novel human protooncogene, c-mer."
    Graham D.K., Dawson T.L., Mullaney D.L., Snodgrass H.R., Earp H.S.
    Cell Growth Differ. 5:647-657(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-118.
    Tissue: Peripheral blood leukocyte.
  2. Erratum
    Graham D.K., Dawson T.L., Mullaney D.L., Snodgrass H.R., Earp H.S.
    Cell Growth Differ. 5:1022-1022(1994)
  3. "Mutations in MERTK, the human orthologue of the RCS rat retinal dystrophy gene, cause retinitis pigmentosa."
    Gal A., Li Y., Thompson D.A., Weir J., Orth U., Jacobson S.G., Apfelstedt-Sylla E., Vollrath D.
    Nat. Genet. 26:270-271(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-999, VARIANTS RP38 LYS-540; CYS-661 AND THR-871, VARIANTS SER-20; ASN-118; THR-282; HIS-293; LYS-466; SER-498; VAL-518 AND VAL-871.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Identification of the major autophosphorylation sites of Nyk/Mer, an NCAM-related receptor tyrosine kinase."
    Ling L., Templeton D., Kung H.J.
    J. Biol. Chem. 271:18355-18362(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION AT TYR-749; TYR-753 AND TYR-754.
  6. "Identification of Gas6 as a ligand for Mer, a neural cell adhesion molecule related receptor tyrosine kinase implicated in cellular transformation."
    Chen J., Carey K., Godowski P.J.
    Oncogene 14:2033-2039(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAS6.
  7. "An SH2 domain-dependent, phosphotyrosine-independent interaction between Vav1 and the Mer receptor tyrosine kinase: a mechanism for localizing guanine nucleotide-exchange factor action."
    Mahajan N.P., Earp H.S.
    J. Biol. Chem. 278:42596-42603(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VAV1.
  8. "Activated tyrosine kinase Ack1 promotes prostate tumorigenesis: role of Ack1 in polyubiquitination of tumor suppressor Wwox."
    Mahajan N.P., Whang Y.E., Mohler J.L., Earp H.S.
    Cancer Res. 65:10514-10523(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNK2.
  9. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-442.
    Tissue: Plasma.
  10. "Signalling and functional diversity within the Axl subfamily of receptor tyrosine kinases."
    Hafizi S., Dahlback B.
    Cytokine Growth Factor Rev. 17:295-304(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  11. Cited for: FUNCTION AS CELL ENTRY FACTOR IN FILOVIRUS INFECTION.
  12. Cited for: REVIEW ON FUNCTION.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543 AND SER-935, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Galectin-3 is a new MerTK-specific eat-me signal."
    Caberoy N.B., Alvarado G., Bigcas J.L., Li W.
    J. Cell. Physiol. 227:401-407(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LGALS3.
  15. "Solution structures of the FN3 domain of human proto-oncogene tyrosine-protein kinase MER precursor."
    RIKEN structural genomics initiative (RSGI)
    Submitted (DEC-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 366-483.
  16. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-20; ASN-118; MET-185; THR-282; LYS-289; HIS-293; GLY-446; LEU-452; LYS-466; SER-498; VAL-518; GLU-662; SER-708; GLN-823; TRP-865 AND ILE-870.
  17. "Detection of variants in 15 genes in 87 unrelated Chinese patients with Leber congenital amaurosis."
    Li L., Xiao X., Li S., Jia X., Wang P., Guo X., Jiao X., Zhang Q., Hejtmancik J.F.
    PLoS ONE 6:E19458-E19458(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VAL-214 AND LEU-958.

Entry informationi

Entry nameiMERTK_HUMAN
AccessioniPrimary (citable) accession number: Q12866
Secondary accession number(s): Q9HBB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 13, 2007
Last modified: September 3, 2014
This is version 165 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 2
    Human chromosome 2: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi