Q12866 (MERTK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Mer
EC=2.7.10.1

Alternative name(s):
Proto-oncogene c-Mer
Receptor tyrosine kinase MerTK

Gene names

Name:	MERTK
Synonyms:	MER

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	999 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	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. Ref.6 Ref.7 Ref.8 Ref.14
Subcellular location	Membrane; Single-pass type I membrane protein By similarity.
Tissue specificity	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.
Post-translational modification	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. Ref.5
Involvement in disease	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. Ref.3
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily. Contains 2 fibronectin type-III domains. Contains 2 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Proto-oncogene Retinitis pigmentosa
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic cell clearance Inferred from electronic annotation. Source: Compara blood coagulation Traceable author statement. Source: Reactome cell surface receptor signaling pathway Traceable author statement Ref.1. Source: ProtInc cell-cell signaling Traceable author statement Ref.1. Source: ProtInc leukocyte migration Traceable author statement. Source: Reactome natural killer cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of lymphocyte activation Inferred from electronic annotation. Source: Compara phagocytosis Inferred from mutant phenotype PubMed 19204785. Source: BHF-UCL platelet activation Inferred from electronic annotation. Source: Compara positive regulation of phagocytosis Inferred from direct assay PubMed 18395422. Source: UniProtKB protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara retina development in camera-type eye Inferred from electronic annotation. Source: Compara secretion by cell Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara substrate adhesion-dependent cell spreading Inferred from electronic annotation. Source: Compara vagina development Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay PubMed 18395422. Source: UniProtKB extracellular space Inferred from direct assay PubMed 18395422. Source: UniProtKB integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc photoreceptor outer segment Inferred from electronic annotation. Source: Compara rhabdomere Inferred from direct assay PubMed 19204785. Source: BHF-UCL
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW transmembrane receptor protein tyrosine kinase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 999

979

Tyrosine-protein kinase Mer

PRO_0000024443

Regions

Topological domain

21 – 505

485

Extracellular Potential

Transmembrane

506 – 526

21

Helical; Potential

Topological domain

527 – 999

473

Cytoplasmic Potential

Domain

81 – 186

106

Ig-like C2-type 1

Domain

197 – 273

77

Ig-like C2-type 2

Domain

284 – 379

96

Fibronectin type-III 1

Domain

383 – 482

100

Fibronectin type-III 2

Domain

587 – 858

272

Protein kinase

Nucleotide binding

593 – 601

9

ATP By similarity

Sites

Active site

723

1

Proton acceptor By similarity

Binding site

615

1

ATP By similarity

Amino acid modifications

Modified residue

543

1

Phosphoserine Ref.13

Modified residue

749

1

Phosphotyrosine; by autocatalysis Ref.5

Modified residue

753

1

Phosphotyrosine; by autocatalysis Ref.5

Modified residue

754

1

Phosphotyrosine; by autocatalysis Ref.5

Modified residue

872

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

935

1

Phosphoserine Ref.13

Glycosylation

114

1

N-linked (GlcNAc...) Potential

Glycosylation

170

1

N-linked (GlcNAc...) Potential

Glycosylation

207

1

N-linked (GlcNAc...) Potential

Glycosylation

215

1

N-linked (GlcNAc...) Potential

Glycosylation

234

1

N-linked (GlcNAc...) Potential

Glycosylation

294

1

N-linked (GlcNAc...) Potential

Glycosylation

316

1

N-linked (GlcNAc...) Potential

Glycosylation

329

1

N-linked (GlcNAc...) Potential

Glycosylation

336

1

N-linked (GlcNAc...) Potential

Glycosylation

354

1

N-linked (GlcNAc...) Potential

Glycosylation

389

1

N-linked (GlcNAc...) Potential

Glycosylation

395

1

N-linked (GlcNAc...) Potential

Glycosylation

442

1

N-linked (GlcNAc...) Ref.9

Glycosylation

454

1

N-linked (GlcNAc...) Potential

Disulfide bond

115 ↔ 175

By similarity

Disulfide bond

218 ↔ 262

By similarity

Natural variations

Natural variant

20

1

R → S. Ref.3 Ref.16
Corresponds to variant rs35898499 [ dbSNP | Ensembl ].

VAR_021039

Natural variant

118

1

S → N. Ref.1 Ref.3 Ref.16
Corresponds to variant rs13027171 [ dbSNP | Ensembl ].

VAR_021040

Natural variant

185

1

V → M. Ref.16
Corresponds to variant rs56205303 [ dbSNP | Ensembl ].

VAR_041741

Natural variant

214

1

F → V Found in a patient with Leber congenital amaurosis. Ref.17

VAR_067194

Natural variant

282

1

A → T. Ref.3 Ref.16
Corresponds to variant rs7588635 [ dbSNP | Ensembl ].

VAR_021041

Natural variant

289

1

E → K. Ref.16

VAR_041742

Natural variant

293

1

R → H. Ref.3 Ref.16
Corresponds to variant rs34072093 [ dbSNP | Ensembl ].

VAR_021042

Natural variant

329

1

N → S.
Corresponds to variant rs34943572 [ dbSNP | Ensembl ].

VAR_051698

Natural variant

446

1

A → G in a renal clear cell carcinoma sample; somatic mutation. Ref.16

VAR_041743

Natural variant

452

1

V → L. Ref.16
Corresponds to variant rs34010621 [ dbSNP | Ensembl ].

VAR_041744

Natural variant

466

1

R → K. Ref.3 Ref.16
Corresponds to variant rs7604639 [ dbSNP | Ensembl ].

VAR_021043

Natural variant

498

1

N → S. Ref.3 Ref.16
Corresponds to variant rs35858762 [ dbSNP | Ensembl ].

VAR_021044

Natural variant

518

1

I → V. Ref.3 Ref.16
Corresponds to variant rs2230515 [ dbSNP | Ensembl ].

VAR_021045

Natural variant

540

1

E → K in RP38. Ref.3

VAR_021046

Natural variant

661

1

S → C in RP38. Ref.3

VAR_021047

Natural variant

662

1

Q → E. Ref.16
Corresponds to variant rs56209758 [ dbSNP | Ensembl ].

VAR_041745

Natural variant

708

1

A → S in a head & Neck squamous cell carcinoma sample; somatic mutation. Ref.16

VAR_041746

Natural variant

823

1

E → Q. Ref.16
Corresponds to variant rs55924349 [ dbSNP | Ensembl ].

VAR_041747

Natural variant

865

1

R → W. Ref.16
Corresponds to variant rs2230516 [ dbSNP | Ensembl ].

VAR_020285

Natural variant

870

1

V → I. Ref.16
Corresponds to variant rs2230517 [ dbSNP | Ensembl ].

VAR_029237

Natural variant

871

1

I → T in RP38. Ref.3

VAR_021048

Natural variant

871

1

I → V. Ref.3

VAR_021049

Natural variant

958

1

P → L Found in a patient with Leber congenital amaurosis. Ref.17

VAR_067195

Experimental info

Sequence conflict

140

1

A → G in AAB60430. Ref.1

Sequence conflict

143

1

A → R in AAB60430. Ref.1

Sequence conflict

247

1

S → G in AAB60430. Ref.1

Sequence conflict

274

1

K → Q in AAB60430. Ref.1

Sequence conflict

328

1

S → G in AAB60430. Ref.1

Sequence conflict

628

1

Q → H in AAB60430. Ref.1

Sequence conflict

794

1

A → R in AAB60430. Ref.1

Sequence conflict

888

1

S → P in AAB60430. Ref.1

Secondary structure

1

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999

Helix Strand Turn

Details...

Beta strand

388 – 394

7

Beta strand

396 – 406

11

Beta strand

417 – 428

12

Beta strand

431 – 441

11

Beta strand

446 – 449

4

Beta strand

453 – 459

7

Beta strand

461 – 467

7

Beta strand

476 – 479

4

Turn

577 – 580

4

Helix

584 – 586

3

Beta strand

587 – 594

8

Beta strand

601 – 607

7

Beta strand

613 – 620

8

Helix

628 – 642

15

Beta strand

654 – 657

4

Beta strand

667 – 672

6

Helix

679 – 685

7

Beta strand

688 – 692

5

Helix

697 – 715

19

Turn

716 – 718

3

Helix

726 – 728

3

Beta strand

729 – 731

3

Beta strand

737 – 739

3

Helix

764 – 766

3

Helix

769 – 773

5

Helix

779 – 794

16

Helix

806 – 808

3

Helix

809 – 814

6

Helix

827 – 835

9

Helix

841 – 843

3

Helix

847 – 860

14

Sequences

	Sequence		Length	Mass (Da)
	Q12866 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 05BC339F05DFD355	FASTA	999	110,249
	10 20 30 40 50 60 MGPAPLPLLL GLFLPALWRR AITEAREEAK PYPLFPGPFP GSLQTDHTPL LSLPHASGYQ 70 80 90 100 110 120 PALMFSPTQP GRPHTGNVAI PQVTSVESKP LPPLAFKHTV GHIILSEHKG VKFNCSISVP 130 140 150 160 170 180 NIYQDTTISW WKDGKELLGA HHAITQFYPD DEVTAIIASF SITSVQRSDN GSYICKMKIN 190 200 210 220 230 240 NEEIVSDPIY IEVQGLPHFT KQPESMNVTR NTAFNLTCQA VGPPEPVNIF WVQNSSRVNE 250 260 270 280 290 300 QPEKSPSVLT VPGLTEMAVF SCEAHNDKGL TVSKGVQINI KAIPSPPTEV SIRNSTAHSI 310 320 330 340 350 360 LISWVPGFDG YSPFRNCSIQ VKEADPLSNG SVMIFNTSAL PHLYQIKQLQ ALANYSIGVS 370 380 390 400 410 420 CMNEIGWSAV SPWILASTTE GAPSVAPLNV TVFLNESSDN VDIRWMKPPT KQQDGELVGY 430 440 450 460 470 480 RISHVWQSAG ISKELLEEVG QNGSRARISV QVHNATCTVR IAAVTRGGVG PFSDPVKIFI 490 500 510 520 530 540 PAHGWVDYAP SSTPAPGNAD PVLIIFGCFC GFILIGLILY ISLAIRKRVQ ETKFGNAFTE 550 560 570 580 590 600 EDSELVVNYI AKKSFCRRAI ELTLHSLGVS EELQNKLEDV VIDRNLLILG KILGEGEFGS 610 620 630 640 650 660 VMEGNLKQED GTSLKVAVKT MKLDNSSQRE IEEFLSEAAC MKDFSHPNVI RLLGVCIEMS 670 680 690 700 710 720 SQGIPKPMVI LPFMKYGDLH TYLLYSRLET GPKHIPLQTL LKFMVDIALG MEYLSNRNFL 730 740 750 760 770 780 HRDLAARNCM LRDDMTVCVA DFGLSKKIYS GDYYRQGRIA KMPVKWIAIE SLADRVYTSK 790 800 810 820 830 840 SDVWAFGVTM WEIATRGMTP YPGVQNHEMY DYLLHGHRLK QPEDCLDELY EIMYSCWRTD 850 860 870 880 890 900 PLDRPTFSVL RLQLEKLLES LPDVRNQADV IYVNTQLLES SEGLAQGSTL APLDLNIDPD 910 920 930 940 950 960 SIIASCTPRA AISVVTAEVH DSKPHEGRYI LNGGSEEWED LTSAPSAAVT AEKNSVLPGE 970 980 990 RLVRNGVSWS HSSMLPLGSS LPDELLFADD SSEGSEVLM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY. 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]	"Tyro3 family-mediated cell entry of Ebola and Marburg viruses." Shimojima M., Takada A., Ebihara H., Neumann G., Fujioka K., Irimura T., Jones S., Feldmann H., Kawaoka Y. J. Virol. 80:10109-10116(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS CELL ENTRY FACTOR IN FILOVIRUS INFECTION.
[12]	"Immunobiology of the TAM receptors." Lemke G., Rothlin C.V. Nat. Rev. Immunol. 8:327-336(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543 AND SER-935, MASS SPECTROMETRY.
[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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Mutations of the MERTK gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U08023 mRNA. Translation: AAB60430.1.
AH010001 Genomic DNA. Translation: AAG33129.1.
AC093675 Genomic DNA. No translation available.
AC104651 Genomic DNA. No translation available.

IPI

IPI00029756.

PIR

I38547.

RefSeq

NP_006334.2. NM_006343.2.

UniGene

Hs.306178.

3D structure databases

PDBe
RCSB PDB
PDBj

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	574-864	[»]
3BRB	X-ray	1.90	A/B	570-864	[»]
3TCP	X-ray	2.69	A/B	570-864	[»]

ProteinModelPortal

Q12866.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q12866. 3 interactions.

STRING

9606.ENSP00000295408.

Protein family/group databases

MEROPS

I43.001.

PTM databases

PhosphoSite

Q12866.

Polymorphism databases

DMDM

160332297.

Proteomic databases

PaxDb

Q12866.

PRIDE

Q12866.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295408; ENSP00000295408; ENSG00000153208.
ENST00000421804; ENSP00000389152; ENSG00000153208.

GeneID

10461.

KEGG

hsa:10461.

UCSC

uc002thk.1. human.

Organism-specific databases

CTD

10461.

GeneCards

GC02P112656.

H-InvDB

HIX0002374.

HGNC

HGNC:7027. MERTK.

HPA

HPA036196.

MIM

604705. gene.
613862. phenotype.

neXtProt

NX_Q12866.

Orphanet

791. Retinitis pigmentosa.

PharmGKB

PA30759.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000231685.

HOVERGEN

HBG006346.

InParanoid

Q12866.

KO

K05117.

OMA

TGPKHIP.

OrthoDB

EOG4Z8XW3.

PhylomeDB

Q12866.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q12866.

Bgee

Q12866.

CleanEx

HS_MERTK.

Genevestigator

Q12866.

GermOnline

ENSG00000153208. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 4 hits.

InterPro

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_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

Pfam

PF00041. fn3. 1 hit.
PF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PRINTS

PR00109. TYRKINASE.

SMART

SM00060. FN3. 2 hits.
SM00409. IG. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.
SSF56112. Kinase_like. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

BindingDB

Q12866.

ChEMBL

CHEMBL5331.

ChiTaRS

MERTK. human.

EvolutionaryTrace

Q12866.

GenomeRNAi

10461.

NextBio

39667.

SOURCE

Search...

Entry information

Entry name

MERTK_HUMAN

Accession

Primary (citable) accession number: Q12866
Secondary accession number(s): Q9HBB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 13, 2007
Last modified:	May 1, 2013
This is version 150 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.