Reviewed, UniProtKB/Swiss-Prot Q9UM73 (ALK_HUMAN)

Names and origin

Protein names

Recommended name:
    ALK tyrosine kinase receptor
    EC=2.7.10.1
Alternative name(s):
    Anaplastic lymphoma kinase
    CD_antigen=CD246

Gene names

Name:

ALK

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1620 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	Orphan receptor with a tyrosine-protein kinase activity. Appears to play an important role in the normal development and function of the nervous system. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif. Ref.7
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Homodimer. When bound to ligand.
Subcellular location	Membrane; Single-pass type I membrane protein. Ref.1
Tissue specificity	Expressed in brain and CNS. Also expressed in the small intestine and testis, but not in normal lymphoid cells. Ref.1
Post-translational modification	N-glycosylated. Ref.1
Involvement in disease	A chromosomal aberration involving ALK is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with NPM1. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. The constitutively active fusion proteins are responsible for 5-10% of non-Hodgkin lymphomas. A chromosomal aberration involving ALK is associated with inflammatory myofibroblastic tumors (IMTs). Translocation t(2;11)(p23;p15) with CARS; translocation t(2;4)(p23;q21) with SEC31A. A chromosomal aberration involving ALK is associated with anaplastic large-cell lymphoma (ALCL). Translocation t(2;17)(p23;q25) with ALO17.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. Contains 1 LDL-receptor class A domain. Contains 2 MAM domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Repeat Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	brain development Ref.3 Traceable author statement. Source: ProtInc protein amino acid N-linked glycosylation Ref.1 Inferred from mutant phenotype. Source: UniProtKB protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro transmembrane receptor protein tyrosine kinase signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular component	integral to plasma membrane Ref.3 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct receptor signaling protein tyrosine kinase activity Ref.3 Traceable author statement. Source: ProtInc transmembrane receptor protein tyrosine kinase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTPRB	P23467	1	EBI-357361,EBI-1265766
PTPRG	P23470	1	EBI-357361,EBI-2258115
PTPRJ	Q12913	1	EBI-357361,EBI-2264500

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 1620	1602	ALK tyrosine kinase receptor		PRO_0000016740
Regions
	Topological domain	19 – 1038	1020	Extracellular Potential
	Transmembrane	1039 – 1059	21	Potential
	Topological domain	1060 – 1620	561	Cytoplasmic Potential
	Domain	264 – 427	164	MAM 1
	Domain	437 – 473	37	LDL-receptor class A
	Domain	478 – 636	159	MAM 2
	Domain	1116 – 1392	277	Protein kinase
	Nucleotide binding	1122 – 1130	9	ATP By similarity
	Compositional bias	816 – 940	125	Gly-rich
Sites
	Active site	1249	1	Proton acceptor By similarity
	Binding site	1150	1	ATP By similarity
Amino acid modifications
	Modified residue	211	1	Phosphoserine Ref.12
	Modified residue	1078	1	Phosphotyrosine Ref.10 Ref.13
	Modified residue	1092	1	Phosphotyrosine Ref.10
	Modified residue	1096	1	Phosphotyrosine Ref.10 Ref.13
	Modified residue	1131	1	Phosphotyrosine Ref.10
	Modified residue	1278	1	Phosphotyrosine Ref.10 Ref.13
	Modified residue	1282	1	Phosphotyrosine; by autocatalysis Ref.10 Ref.13
	Modified residue	1283	1	Phosphotyrosine Ref.13
	Modified residue	1359	1	Phosphotyrosine Ref.13
	Modified residue	1507	1	Phosphotyrosine Ref.10 Ref.13
	Modified residue	1584	1	Phosphotyrosine Ref.10
	Modified residue	1604	1	Phosphotyrosine Ref.10
	Glycosylation	169	1	N-linked (GlcNAc...) Potential
	Glycosylation	244	1	N-linked (GlcNAc...) Potential
	Glycosylation	285	1	N-linked (GlcNAc...) Potential
	Glycosylation	324	1	N-linked (GlcNAc...) Potential
	Glycosylation	411	1	N-linked (GlcNAc...) Potential
	Glycosylation	424	1	N-linked (GlcNAc...) Potential
	Glycosylation	445	1	N-linked (GlcNAc...) Potential
	Glycosylation	563	1	N-linked (GlcNAc...) Potential
	Glycosylation	571	1	N-linked (GlcNAc...) Potential
	Glycosylation	627	1	N-linked (GlcNAc...) Potential
	Glycosylation	709	1	N-linked (GlcNAc...) Potential
	Glycosylation	808	1	N-linked (GlcNAc...) Potential
	Glycosylation	863	1	N-linked (GlcNAc...) Potential
	Glycosylation	864	1	N-linked (GlcNAc...) Potential
	Glycosylation	886	1	N-linked (GlcNAc...) Potential
	Glycosylation	986	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	90	1	S → L		VAR_041477
	Natural variant	163	1	V → L		VAR_041478
	Natural variant	296	1	E → Q		VAR_041479
	Natural variant	476	1	V → A: dbSNP rs35093491. Ref.15		VAR_041480
	Natural variant	560	1	L → F in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.15		VAR_041481
	Natural variant	680	1	T → I: dbSNP rs35228363. Ref.15		VAR_041482
	Natural variant	704	1	A → T		VAR_041483
	Natural variant	877	1	A → S in an ovarian serous carcinoma sample; somatic mutation. Ref.15		VAR_041484
	Natural variant	1012	1	T → M		VAR_041485
	Natural variant	1121	1	G → D		VAR_041486
	Natural variant	1274	1	A → T: dbSNP rs45502292. Ref.15		VAR_041487
	Natural variant	1328	1	M → L		VAR_041488
	Natural variant	1376	1	F → S: dbSNP rs17694720.		VAR_055987
	Natural variant	1416	1	K → N		VAR_041489
	Natural variant	1419	1	E → K		VAR_041490
	Natural variant	1429	1	Q → R		VAR_041491
	Natural variant	1461	1	V → I: dbSNP rs1670283. Ref.5		VAR_031042
	Natural variant	1491	1	K → R: dbSNP rs1881420. Ref.15 Ref.3 Ref.4		VAR_031043
	Natural variant	1529	1	D → E: dbSNP rs1881421. Ref.15 Ref.3 Ref.4		VAR_031044
	Natural variant	1599	1	P → H: dbSNP rs1881423.		VAR_055988
Experimental info
	Sequence conflict	36	1	P → S in AAB71619. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UM73-1 [UniParc]. Last modified March 6, 2007. Version 2. Checksum: A4B96DFF6D329777	FASTA	1,620	176,428
	10 20 30 40 50 60 MGAIGLLWLL PLLLSTAAVG SGMGTGQRAG SPAAGPPLQP REPLSYSRLQ RKSLAVDFVV 70 80 90 100 110 120 PSLFRVYARD LLLPPSSSEL KAGRPEARGS LALDCAPLLR LLGPAPGVSW TAGSPAPAEA 130 140 150 160 170 180 RTLSRVLKGG SVRKLRRAKQ LVLELGEEAI LEGCVGPPGE AAVGLLQFNL SELFSWWIRQ 190 200 210 220 230 240 GEGRLRIRLM PEKKASEVGR EGRLSAAIRA SQPRLLFQIF GTGHSSLESP TNMPSPSPDY 250 260 270 280 290 300 FTWNLTWIMK DSFPFLSHRS RYGLECSFDF PCELEYSPPL HDLRNQSWSW RRIPSEEASQ 310 320 330 340 350 360 MDLLDGPGAE RSKEMPRGSF LLLNTSADSK HTILSPWMRS SSEHCTLAVS VHRHLQPSGR 370 380 390 400 410 420 YIAQLLPHNE AAREILLMPT PGKHGWTVLQ GRIGRPDNPF RVALEYISSG NRSLSAVDFF 430 440 450 460 470 480 ALKNCSEGTS PGSKMALQSS FTCWNGTVLQ LGQACDFHQD CAQGEDESQM CRKLPVGFYC 490 500 510 520 530 540 NFEDGFCGWT QGTLSPHTPQ WQVRTLKDAR FQDHQDHALL LSTTDVPASE SATVTSATFP 550 560 570 580 590 600 APIKSSPCEL RMSWLIRGVL RGNVSLVLVE NKTGKEQGRM VWHVAAYEGL SLWQWMVLPL 610 620 630 640 650 660 LDVSDRFWLQ MVAWWGQGSR AIVAFDNISI SLDCYLTISG EDKILQNTAP KSRNLFERNP 670 680 690 700 710 720 NKELKPGENS PRQTPIFDPT VHWLFTTCGA SGPHGPTQAQ CNNAYQNSNL SVEVGSEGPL 730 740 750 760 770 780 KGIQIWKVPA TDTYSISGYG AAGGKGGKNT MMRSHGVSVL GIFNLEKDDM LYILVGQQGE 790 800 810 820 830 840 DACPSTNQLI QKVCIGENNV IEEEIRVNRS VHEWAGGGGG GGGATYVFKM KDGVPVPLII 850 860 870 880 890 900 AAGGGGRAYG AKTDTFHPER LENNSSVLGL NGNSGAAGGG GGWNDNTSLL WAGKSLQEGA 910 920 930 940 950 960 TGGHSCPQAM KKWGWETRGG FGGGGGGCSS GGGGGGYIGG NAASNNDPEM DGEDGVSFIS 970 980 990 1000 1010 1020 PLGILYTPAL KVMEGHGEVN IKHYLNCSHC EVDECHMDPE SHKVICFCDH GTVLAEDGVS 1030 1040 1050 1060 1070 1080 CIVSPTPEPH LPLSLILSVV TSALVAALVL AFSGIMIVYR RKHQELQAMQ MELQSPEYKL 1090 1100 1110 1120 1130 1140 SKLRTSTIMT DYNPNYCFAG KTSSISDLKE VPRKNITLIR GLGHGAFGEV YEGQVSGMPN 1150 1160 1170 1180 1190 1200 DPSPLQVAVK TLPEVCSEQD ELDFLMEALI ISKFNHQNIV RCIGVSLQSL PRFILLELMA 1210 1220 1230 1240 1250 1260 GGDLKSFLRE TRPRPSQPSS LAMLDLLHVA RDIACGCQYL EENHFIHRDI AARNCLLTCP 1270 1280 1290 1300 1310 1320 GPGRVAKIGD FGMARDIYRA SYYRKGGCAM LPVKWMPPEA FMEGIFTSKT DTWSFGVLLW 1330 1340 1350 1360 1370 1380 EIFSLGYMPY PSKSNQEVLE FVTSGGRMDP PKNCPGPVYR IMTQCWQHQP EDRPNFAIIL 1390 1400 1410 1420 1430 1440 ERIEYCTQDP DVINTALPIE YGPLVEEEEK VPVRPKDPEG VPPLLVSQQA KREEERSPAA 1450 1460 1470 1480 1490 1500 PPPLPTTSSG KAAKKPTAAE VSVRVPRGPA VEGGHVNMAF SQSNPPSELH KVHGSRNKPT 1510 1520 1530 1540 1550 1560 SLWNPTYGSW FTEKPTKKNN PIAKKEPHDR GNLGLEGSCT VPPNVATGRL PGASLLLEPS 1570 1580 1590 1600 1610 1620 SLTANMKEVP LFRLRHFPCG NVNYGYQQQG LPLEAATAPG AGHYEDTILK SKNSMNQPGP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ALK, the chromosome 2 gene locus altered by the t(2;5) in non-Hodgkin's lymphoma, encodes a novel neural receptor tyrosine kinase that is highly related to leukocyte tyrosine kinase (LTK)." Morris S.W., Naeve C.W., Mathew P., James P.L., Kirstein M.N., Cui X., Witte D.P. Oncogene 14:2175-2188(1997) [PubMed: 9174053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
[2]	Erratum Morris S.W., Naeve C.W., Mathew P., James P.L., Kirstein M.N., Cui X., Witte D.P. Oncogene 15:2883-2883(1997)
[3]	"Molecular characterization of ALK, a receptor tyrosine kinase expressed specifically in the nervous system." Iwahara T., Fujimoto J., Wen D., Cupples R., Bucay N., Arakawa T., Mori S., Ratzkin B., Yamamoto T. Oncogene 14:439-449(1997) [PubMed: 9053841] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-1491 AND GLU-1529.
[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-1491 AND GLU-1529. Tissue: Brain.
[5]	"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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-1461.
[6]	"Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin's lymphoma." Morris S.W., Kirstein M.N., Valentine M.B., Dittmer K.G., Shapiro D.N., Saltman D.L., Look A.T. Science 263:1281-1284(1994) [PubMed: 8122112] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH NPM1.
[7]	"The cytoplasmic truncated receptor tyrosine kinase ALK homodimer immortalizes and cooperates with ras in cellular transformation." Simonitsch I., Polgar D., Hajek M., Duchek P., Skrzypek B., Fassl S., Lamprecht A., Schmidt G., Krupitza G., Cerni C. FASEB J. 15:1416-1418(2001) [PubMed: 11387242] [Abstract] Cited for: FUNCTION AS AN ONCOGENE.
[8]	"Identification of novel fusion partners of ALK, the anaplastic lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory myofibroblastic tumor." Cools J., Wlodarska I., Somers R., Mentens N., Pedeutour F., Maes B., De Wolf-Peeters C., Pauwels P., Hagemeijer A., Marynen P. Genes Chromosomes Cancer 34:354-362(2002) [PubMed: 12112524] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH ALO17 AND CARS.
[9]	"Unique substrate specificity of anaplastic lymphoma kinase (ALK): development of phosphoacceptor peptides for the assay of ALK activity." Donella-Deana A., Marin O., Cesaro L., Gunby R.H., Ferrarese A., Coluccia A.M., Tartari C.J., Mologni L., Scapozza L., Gambacorti-Passerini C., Pinna L.A. Biochemistry 44:8533-8542(2005) [PubMed: 15938644] [Abstract] Cited for: SUBSTRATE SPECIFICITY.
[10]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1078; TYR-1092; TYR-1096; TYR-1131; TYR-1278; TYR-1282; TYR-1507; TYR-1584 AND TYR-1604, MASS SPECTROMETRY.
[11]	"Fusion of the SEC31L1 and ALK genes in an inflammatory myofibroblastic tumor." Panagopoulos I., Nilsson T., Domanski H.A., Isaksson M., Lindblom P., Mertens F., Mandahl N. Int. J. Cancer 118:1181-1186(2006) [PubMed: 16161041] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH SEC31A.
[12]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1078; TYR-1096; TYR-1278; TYR-1282; TYR-1283; TYR-1359 AND TYR-1507, MASS SPECTROMETRY.
[14]	"Solution structure of the complex of the PTB domain of SNT-2 and 19-residue peptide (aa 1571-1589) of HALK." RIKEN structural genomics initiative (RSGI) Submitted (APR-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1571-1589.
[15]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-90; LEU-163; GLN-296; ALA-476; PHE-560; ILE-680; THR-704; SER-877; MET-1012; ASP-1121; THR-1274; LEU-1328; ASN-1416; LYS-1419; ARG-1429; ARG-1491 AND GLU-1529.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

U62540 mRNA. Translation: AAB71619.1.
U66559 mRNA. Translation: AAC51104.1.
AB209477 mRNA. Translation: BAD92714.1. Different initiation.
AC106870 Genomic DNA. Translation: AAX93126.1.
AC093756 Genomic DNA. Translation: AAX88892.1.
AC074096 Genomic DNA. Translation: AAY15027.1.

IPI

IPI00395632.

RefSeq

NP_004295.2.

UniGene

Hs.654469

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YS5	NMR	-	B	1571-1589	[»]
2YT2	NMR	-	A	1571-1589	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UM73. 61 interactions.

STRING

Q9UM73.

PTM databases

PhosphoSite

Q9UM73.

Proteomic databases

PRIDE

Q9UM73.

Genome annotation databases

Ensembl

ENST00000389048; ENSP00000373700; ENSG00000171094; Homo sapiens. [Genome view]
ENST00000415678; ENSP00000399568; ENSG00000171094; Homo sapiens. [Genome view]
ENST00000431873; ENSP00000414027; ENSG00000171094; Homo sapiens. [Genome view]
ENST00000438993; ENSP00000403217; ENSG00000171094; Homo sapiens. [Genome view]
ENST00000442523; ENSP00000403741; ENSG00000171094; Homo sapiens. [Genome view]
ENST00000453137; ENSP00000387488; ENSG00000171094; Homo sapiens. [Genome view]

GeneID

238.

KEGG

hsa:238.

UCSC

uc002rmy.1. human.

Organism-specific databases

CTD

238.

GeneCards

GC02M029327.

H-InvDB

HIX0024259.
HIX0030037.

HGNC

HGNC:427. ALK.

HPA

HPA010694.

MIM

105590. gene.

Orphanet

98841. Anaplastic large cell lymphoma.
635. Neuroblastoma.

PharmGKB

PA24719.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9UM73.

HOVERGEN

Q9UM73.

Enzyme and pathway databases

BRENDA

2.7.10.1. 247.

Gene expression databases

ArrayExpress

Q9UM73.

Bgee

Q9UM73.

CleanEx

HS_ALK.

Genevestigator

Q9UM73.

GermOnline

ENSG00000171094. Homo sapiens.

Family and domain databases

InterPro

IPR002172. LDL_rcpt_classA_cys-rich.
IPR000998. MAM.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR002011. Recept_tyr_kinase-II_CS.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]

Pfam

PF00629. MAM. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PRINTS

PR00109. TYRKINASE.

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00192. LDLa. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS01209. LDLRA_1. False negative.
PS50068. LDLRA_2. False negative.
PS00740. MAM_1. False negative.
PS50060. MAM_2. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00171. Adenosine triphosphate.

NextBio

948.

SOURCE

Search...

Entry information

Entry name

ALK_HUMAN

Accession

Primary (citable) accession number: Q9UM73
Secondary accession number(s): Q4ZFX9 , Q53QQ6, Q53RZ4, Q59FI3, Q9Y4K6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	March 6, 2007
Last modified:	October 13, 2009
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.