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Q9UM73

- ALK_HUMAN

UniProt

Q9UM73 - ALK_HUMAN

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Protein

ALK tyrosine kinase receptor

Gene

ALK

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

Functioni

Neuronal orphan receptor tyrosine kinase that is essentially and transiently expressed in specific regions of the central and peripheral nervous systems and plays an important role in the genesis and differentiation of the nervous system. Transduces signals from ligands at the cell surface, through specific activation of the mitogen-activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif. Following activation by ligand, ALK induces tyrosine phosphorylation of CBL, FRS2, IRS1 and SHC1, as well as of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Acts as a receptor for ligands pleiotrophin (PTN), a secreted growth factor, and midkine (MDK), a PTN-related factor, thus participating in PTN and MDK signal transduction. PTN-binding induces MAPK pathway activation, which is important for the anti-apoptotic signaling of PTN and regulation of cell proliferation. MDK-binding induces phosphorylation of the ALK target insulin receptor substrate (IRS1), activates mitogen-activated protein kinases (MAPKs) and PI3-kinase, resulting also in cell proliferation induction. Drives NF-kappa-B activation, probably through IRS1 and the activation of the AKT serine/threonine kinase. Recruitment of IRS1 to activated ALK and the activation of NF-kappa-B are essential for the autocrine growth and survival signaling of MDK.11 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by ligand-binding and subsequent phosphorylation. Inactivated through dephosphorylation by receptor protein tyrosine phosphatase beta and zeta complex (PTPRB/PTPRZ1) when there is no stimulation by a ligand. Staurosporine, crizotinib and CH5424802 act as inhibitors of ALK kinase activity.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1124 – 11241ATP; via carbonyl oxygen
Binding sitei1150 – 11501ATPPROSITE-ProRule annotation
Binding sitei1150 – 11501Inhibitor2 Publications
Binding sitei1199 – 11991Inhibitor; via amide nitrogen2 Publications
Binding sitei1203 – 12031Inhibitor2 Publications
Binding sitei1210 – 12101Inhibitor2 Publications
Active sitei1249 – 12491Proton acceptorPROSITE-ProRule annotation
Binding sitei1270 – 12701ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1197 – 11993ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. NF-kappaB-inducing kinase activity Source: UniProtKB
  3. protein tyrosine kinase activity Source: MGI
  4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of MAPK activity Source: UniProtKB
  2. cell proliferation Source: UniProtKB
  3. neuron development Source: UniProtKB
  4. NIK/NF-kappaB signaling Source: GOC
  5. peptidyl-tyrosine phosphorylation Source: GOC
  6. phosphorylation Source: UniProtKB
  7. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  8. protein autophosphorylation Source: UniProtKB
  9. regulation of apoptotic process Source: UniProtKB
  10. signal transduction Source: UniProtKB
  11. transmembrane receptor protein tyrosine kinase signaling pathway Source: InterPro
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.
SignaLinkiQ9UM73.

Names & Taxonomyi

Protein namesi
Recommended name:
ALK tyrosine kinase receptor (EC:2.7.10.1)
Alternative name(s):
Anaplastic lymphoma kinase
CD_antigen: CD246
Gene namesi
Name:ALK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:427. ALK.

Subcellular locationi

Cell membrane 2 Publications; Single-pass type I membrane protein 2 Publications
Note: Membrane attachment was crucial for promotion of neuron-like differentiation and cell proliferation arrest through specific activation of the MAP kinase pathway.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 10381020ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1039 – 105921HelicalSequence AnalysisAdd
BLAST
Topological domaini1060 – 1620561CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. integral component of plasma membrane Source: UniProtKB
  3. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

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.
Neuroblastoma 3 (NBLST3) [MIM:613014]: A common neoplasm of early childhood arising from embryonic cells that form the primitive neural crest and give rise to the adrenal medulla and the sympathetic nervous system.3 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1091 – 10911D → N in NBLST3; somatic mutation. 1 Publication
VAR_063850
Natural varianti1128 – 11281G → A in NBLST3. 1 Publication
VAR_063851
Natural varianti1151 – 11511T → M in NBLST3. 1 Publication
VAR_063852
Natural varianti1166 – 11661M → R in NBLST3; somatic mutation. 1 Publication
VAR_063853
Natural varianti1171 – 11711I → N in NBLST3; somatic mutation. 1 Publication
VAR_063854
Natural varianti1174 – 11741F → C in NBLST3. 1 Publication
VAR_063855
Natural varianti1174 – 11741F → I in NBLST3; somatic mutation. 1 Publication
VAR_063856
Natural varianti1174 – 11741F → L in NBLST3; somatic mutation; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments. 2 Publications
VAR_063857
Natural varianti1174 – 11741F → V in NBLST3; somatic mutation; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments. 1 Publication
VAR_063858
Natural varianti1192 – 11921R → P in NBLST3. 2 Publications
VAR_063859
Natural varianti1234 – 12341A → T in NBLST3; somatic mutation. 1 Publication
VAR_063860
Natural varianti1245 – 12451F → C in NBLST3; somatic mutation. 2 Publications
VAR_063861
Natural varianti1245 – 12451F → V in NBLST3; somatic mutation.
VAR_063862
Natural varianti1250 – 12501I → T in NBLST3; somatic mutation. 1 Publication
VAR_063863
Natural varianti1275 – 12751R → Q in NBLST3; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments. 3 Publications
VAR_063865
Natural varianti1278 – 12781Y → S in NBLST3; somatic mutation. 1 Publication
VAR_063866
The ALK signaling pathway plays an important role in glioblastoma, the most common malignant brain tumor of adults and one of the most lethal cancers. It regulates both glioblastoma migration and growth.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1507 – 15071Y → F: Impairs interaction with SHC1. 1 Publication

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

MIMi613014. phenotype.
Orphaneti300895. ALK-positive anaplastic large cell lymphoma.
364043. ALK-positive large B-cell lymphoma.
178342. Inflammatory myofibroblastic tumor.
635. Neuroblastoma.
357191. Selection of therapeutic option in non-small cell lung carcinoma.
PharmGKBiPA24719.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 16201602ALK tyrosine kinase receptorPRO_0000016740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence Analysis
Modified residuei211 – 2111Phosphoserine
Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi411 – 4111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi424 – 4241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi563 – 5631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi571 – 5711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi627 – 6271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi709 – 7091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi808 – 8081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi863 – 8631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi864 – 8641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi886 – 8861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi986 – 9861N-linked (GlcNAc...)Sequence Analysis
Modified residuei1078 – 10781Phosphotyrosine1 Publication
Modified residuei1092 – 10921Phosphotyrosine
Modified residuei1096 – 10961Phosphotyrosine2 Publications
Modified residuei1131 – 11311Phosphotyrosine1 Publication
Modified residuei1278 – 12781Phosphotyrosine1 Publication
Modified residuei1282 – 12821Phosphotyrosine; by autocatalysis
Modified residuei1283 – 12831Phosphotyrosine
Modified residuei1359 – 13591Phosphotyrosine
Modified residuei1507 – 15071Phosphotyrosine1 Publication
Modified residuei1584 – 15841Phosphotyrosine
Modified residuei1604 – 16041Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity. In cells not stimulated by a ligand, receptor protein tyrosine phosphatase beta and zeta complex (PTPRB/PTPRZ1) dephosphorylates ALK at the sites in ALK that are undergoing autophosphorylation through autoactivation. Phosphorylation at Tyr-1507 is critical for SHC1 association.6 Publications
N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9UM73.
PRIDEiQ9UM73.

PTM databases

PhosphoSiteiQ9UM73.

Expressioni

Tissue specificityi

Expressed in brain and CNS. Also expressed in the small intestine and testis, but not in normal lymphoid cells.1 Publication

Gene expression databases

BgeeiQ9UM73.
CleanExiHS_ALK.
ExpressionAtlasiQ9UM73. baseline and differential.
GenevestigatoriQ9UM73.

Organism-specific databases

HPAiHPA010694.

Interactioni

Subunit structurei

Homodimer. Homodimerizes when bound to ligand. Interacts with FRS2, IRS1, MDK, PTN and SHC1. Interacts with CBL, PIK3R1 and PLCG1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-357361,EBI-352572
PTPRZ1P234712EBI-357361,EBI-2263175

Protein-protein interaction databases

BioGridi106739. 46 interactions.
DIPiDIP-5954N.
IntActiQ9UM73. 7 interactions.
MINTiMINT-1133857.
STRINGi9606.ENSP00000373700.

Structurei

Secondary structure

1
1620
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1087 – 10926Combined sources
Beta strandi1096 – 10983Combined sources
Beta strandi1101 – 11033Combined sources
Helixi1105 – 11073Combined sources
Helixi1113 – 11153Combined sources
Beta strandi1116 – 11216Combined sources
Beta strandi1126 – 11283Combined sources
Beta strandi1130 – 11356Combined sources
Beta strandi1137 – 11404Combined sources
Beta strandi1145 – 11517Combined sources
Helixi1158 – 117316Combined sources
Beta strandi1182 – 11865Combined sources
Beta strandi1188 – 11914Combined sources
Beta strandi1193 – 11975Combined sources
Helixi1204 – 12107Combined sources
Beta strandi1215 – 12173Combined sources
Helixi1223 – 124220Combined sources
Helixi1252 – 12543Combined sources
Beta strandi1255 – 12584Combined sources
Beta strandi1260 – 12634Combined sources
Beta strandi1266 – 12683Combined sources
Helixi1272 – 12787Combined sources
Beta strandi1280 – 12823Combined sources
Helixi1288 – 12903Combined sources
Helixi1293 – 12953Combined sources
Helixi1298 – 13036Combined sources
Helixi1308 – 132316Combined sources
Helixi1335 – 13439Combined sources
Helixi1356 – 136510Combined sources
Helixi1370 – 13723Combined sources
Helixi1376 – 138813Combined sources
Helixi1390 – 13934Combined sources
Beta strandi1574 – 15763Combined sources
Beta strandi1582 – 15843Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KUPNMR-B1571-1589[»]
2KUQNMR-A1571-1589[»]
2XB7X-ray2.50A1094-1407[»]
2XBAX-ray1.95A1094-1407[»]
2XP2X-ray1.90A1093-1411[»]
2YFXX-ray1.70A1093-1411[»]
2YHVX-ray1.90A1093-1411[»]
2YJRX-ray1.90A1093-1411[»]
2YJSX-ray1.90A1093-1411[»]
2YS5NMR-B1571-1589[»]
2YT2NMR-A1571-1589[»]
3AOXX-ray1.75A1069-1411[»]
3L9PX-ray1.80A1072-1410[»]
3LCSX-ray1.95A1072-1410[»]
3LCTX-ray2.10A1072-1410[»]
4ANLX-ray1.70A1093-1411[»]
4ANQX-ray1.76A1093-1411[»]
4ANSX-ray1.85A1093-1411[»]
4CCBX-ray2.03A1093-1411[»]
4CCUX-ray2.00A1093-1411[»]
4CD0X-ray2.23A1093-1411[»]
4CLIX-ray2.05A1093-1411[»]
4CLJX-ray1.66A1093-1411[»]
4CMOX-ray1.83A1093-1411[»]
4CMTX-ray1.73A1093-1411[»]
4CMUX-ray1.80A1093-1411[»]
4CNHX-ray1.90A/B1093-1411[»]
4CTBX-ray1.79A1093-1411[»]
4CTCX-ray2.03A1093-1411[»]
4DCEX-ray2.03A/B1078-1410[»]
4FNWX-ray1.75A1084-1410[»]
4FNXX-ray1.70A1084-1410[»]
4FNYX-ray2.45A1084-1410[»]
4FNZX-ray2.60A1084-1410[»]
4FOBX-ray1.90A1058-1410[»]
4FOCX-ray1.70A1058-1410[»]
4FODX-ray2.00A1078-1410[»]
4JOAX-ray2.70A1072-1410[»]
4MKCX-ray2.01A1072-1410[»]
ProteinModelPortaliQ9UM73.
SMRiQ9UM73. Positions 1096-1480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UM73.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini264 – 427164MAM 1PROSITE-ProRule annotationAdd
BLAST
Domaini437 – 47337LDL-receptor class AAdd
BLAST
Domaini478 – 636159MAM 2PROSITE-ProRule annotationAdd
BLAST
Domaini1116 – 1392277Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1197 – 11993Inhibitor binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi816 – 940125Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 1 LDL-receptor class A domain.Curated
Contains 2 MAM domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000231766.
HOVERGENiHBG018726.
InParanoidiQ9UM73.
KOiK05119.
OMAiLIQKVCI.
OrthoDBiEOG7GN2KT.
PhylomeDBiQ9UM73.
TreeFamiTF351636.

Family and domain databases

Gene3Di4.10.400.10. 1 hit.
InterProiIPR026830. ALK.
IPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR002172. LDrepeatLR_classA_rpt.
IPR000998. MAM_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.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PANTHERiPTHR24416:SF276. PTHR24416:SF276. 1 hit.
PfamiPF00629. MAM. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00192. LDLa. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57424. SSF57424. 1 hit.
PROSITEiPS50060. 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]

Sequencei

Sequence statusi: Complete.

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

Q9UM73-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAIGLLWLL PLLLSTAAVG SGMGTGQRAG SPAAGPPLQP REPLSYSRLQ
60 70 80 90 100
RKSLAVDFVV PSLFRVYARD LLLPPSSSEL KAGRPEARGS LALDCAPLLR
110 120 130 140 150
LLGPAPGVSW TAGSPAPAEA RTLSRVLKGG SVRKLRRAKQ LVLELGEEAI
160 170 180 190 200
LEGCVGPPGE AAVGLLQFNL SELFSWWIRQ GEGRLRIRLM PEKKASEVGR
210 220 230 240 250
EGRLSAAIRA SQPRLLFQIF GTGHSSLESP TNMPSPSPDY FTWNLTWIMK
260 270 280 290 300
DSFPFLSHRS RYGLECSFDF PCELEYSPPL HDLRNQSWSW RRIPSEEASQ
310 320 330 340 350
MDLLDGPGAE RSKEMPRGSF LLLNTSADSK HTILSPWMRS SSEHCTLAVS
360 370 380 390 400
VHRHLQPSGR YIAQLLPHNE AAREILLMPT PGKHGWTVLQ GRIGRPDNPF
410 420 430 440 450
RVALEYISSG NRSLSAVDFF ALKNCSEGTS PGSKMALQSS FTCWNGTVLQ
460 470 480 490 500
LGQACDFHQD CAQGEDESQM CRKLPVGFYC NFEDGFCGWT QGTLSPHTPQ
510 520 530 540 550
WQVRTLKDAR FQDHQDHALL LSTTDVPASE SATVTSATFP APIKSSPCEL
560 570 580 590 600
RMSWLIRGVL RGNVSLVLVE NKTGKEQGRM VWHVAAYEGL SLWQWMVLPL
610 620 630 640 650
LDVSDRFWLQ MVAWWGQGSR AIVAFDNISI SLDCYLTISG EDKILQNTAP
660 670 680 690 700
KSRNLFERNP NKELKPGENS PRQTPIFDPT VHWLFTTCGA SGPHGPTQAQ
710 720 730 740 750
CNNAYQNSNL SVEVGSEGPL KGIQIWKVPA TDTYSISGYG AAGGKGGKNT
760 770 780 790 800
MMRSHGVSVL GIFNLEKDDM LYILVGQQGE DACPSTNQLI QKVCIGENNV
810 820 830 840 850
IEEEIRVNRS VHEWAGGGGG GGGATYVFKM KDGVPVPLII AAGGGGRAYG
860 870 880 890 900
AKTDTFHPER LENNSSVLGL NGNSGAAGGG GGWNDNTSLL WAGKSLQEGA
910 920 930 940 950
TGGHSCPQAM KKWGWETRGG FGGGGGGCSS GGGGGGYIGG NAASNNDPEM
960 970 980 990 1000
DGEDGVSFIS PLGILYTPAL KVMEGHGEVN IKHYLNCSHC EVDECHMDPE
1010 1020 1030 1040 1050
SHKVICFCDH GTVLAEDGVS CIVSPTPEPH LPLSLILSVV TSALVAALVL
1060 1070 1080 1090 1100
AFSGIMIVYR RKHQELQAMQ MELQSPEYKL SKLRTSTIMT DYNPNYCFAG
1110 1120 1130 1140 1150
KTSSISDLKE VPRKNITLIR GLGHGAFGEV YEGQVSGMPN DPSPLQVAVK
1160 1170 1180 1190 1200
TLPEVCSEQD ELDFLMEALI ISKFNHQNIV RCIGVSLQSL PRFILLELMA
1210 1220 1230 1240 1250
GGDLKSFLRE TRPRPSQPSS LAMLDLLHVA RDIACGCQYL EENHFIHRDI
1260 1270 1280 1290 1300
AARNCLLTCP GPGRVAKIGD FGMARDIYRA SYYRKGGCAM LPVKWMPPEA
1310 1320 1330 1340 1350
FMEGIFTSKT DTWSFGVLLW EIFSLGYMPY PSKSNQEVLE FVTSGGRMDP
1360 1370 1380 1390 1400
PKNCPGPVYR IMTQCWQHQP EDRPNFAIIL ERIEYCTQDP DVINTALPIE
1410 1420 1430 1440 1450
YGPLVEEEEK VPVRPKDPEG VPPLLVSQQA KREEERSPAA PPPLPTTSSG
1460 1470 1480 1490 1500
KAAKKPTAAE ISVRVPRGPA VEGGHVNMAF SQSNPPSELH KVHGSRNKPT
1510 1520 1530 1540 1550
SLWNPTYGSW FTEKPTKKNN PIAKKEPHDR GNLGLEGSCT VPPNVATGRL
1560 1570 1580 1590 1600
PGASLLLEPS SLTANMKEVP LFRLRHFPCG NVNYGYQQQG LPLEAATAPG
1610 1620
AGHYEDTILK SKNSMNQPGP
Length:1,620
Mass (Da):176,442
Last modified:May 18, 2010 - v3
Checksum:i0733D6C4FD212F41
GO

Sequence cautioni

The sequence BAD92714.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361P → S in AAB71619. (PubMed:9174053)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901S → L.1 Publication
Corresponds to variant rs34617074 [ dbSNP | Ensembl ].
VAR_041477
Natural varianti163 – 1631V → L.1 Publication
Corresponds to variant rs55697431 [ dbSNP | Ensembl ].
VAR_041478
Natural varianti296 – 2961E → Q.1 Publication
Corresponds to variant rs56077855 [ dbSNP | Ensembl ].
VAR_041479
Natural varianti476 – 4761V → A.1 Publication
Corresponds to variant rs35093491 [ dbSNP | Ensembl ].
VAR_041480
Natural varianti560 – 5601L → F in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
VAR_041481
Natural varianti680 – 6801T → I.1 Publication
Corresponds to variant rs35228363 [ dbSNP | Ensembl ].
VAR_041482
Natural varianti704 – 7041A → T.1 Publication
Corresponds to variant rs34829159 [ dbSNP | Ensembl ].
VAR_041483
Natural varianti868 – 8681L → Q.
Corresponds to variant rs55941323 [ dbSNP | Ensembl ].
VAR_061288
Natural varianti877 – 8771A → S in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
VAR_041484
Natural varianti1012 – 10121T → M.1 Publication
Corresponds to variant rs35073634 [ dbSNP | Ensembl ].
VAR_041485
Natural varianti1091 – 10911D → N in NBLST3; somatic mutation. 1 Publication
VAR_063850
Natural varianti1121 – 11211G → D.1 Publication
Corresponds to variant rs55760835 [ dbSNP | Ensembl ].
VAR_041486
Natural varianti1128 – 11281G → A in NBLST3. 1 Publication
VAR_063851
Natural varianti1151 – 11511T → M in NBLST3. 1 Publication
VAR_063852
Natural varianti1166 – 11661M → R in NBLST3; somatic mutation. 1 Publication
VAR_063853
Natural varianti1171 – 11711I → N in NBLST3; somatic mutation. 1 Publication
VAR_063854
Natural varianti1174 – 11741F → C in NBLST3. 1 Publication
VAR_063855
Natural varianti1174 – 11741F → I in NBLST3; somatic mutation. 1 Publication
VAR_063856
Natural varianti1174 – 11741F → L in NBLST3; somatic mutation; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments. 2 Publications
VAR_063857
Natural varianti1174 – 11741F → V in NBLST3; somatic mutation; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments. 1 Publication
VAR_063858
Natural varianti1192 – 11921R → P in NBLST3. 2 Publications
VAR_063859
Natural varianti1234 – 12341A → T in NBLST3; somatic mutation. 1 Publication
VAR_063860
Natural varianti1245 – 12451F → C in NBLST3; somatic mutation. 2 Publications
VAR_063861
Natural varianti1245 – 12451F → V in NBLST3; somatic mutation.
VAR_063862
Natural varianti1250 – 12501I → T in NBLST3; somatic mutation. 1 Publication
VAR_063863
Natural varianti1274 – 12741A → T.1 Publication
Corresponds to variant rs45502292 [ dbSNP | Ensembl ].
VAR_041487
Natural varianti1275 – 12751R → L Observed in neuroblastoma. 1 Publication
VAR_063864
Natural varianti1275 – 12751R → Q in NBLST3; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments. 3 Publications
VAR_063865
Natural varianti1278 – 12781Y → S in NBLST3; somatic mutation. 1 Publication
VAR_063866
Natural varianti1328 – 13281M → L.1 Publication
Corresponds to variant rs56160491 [ dbSNP | Ensembl ].
VAR_041488
Natural varianti1376 – 13761F → S.
Corresponds to variant rs17694720 [ dbSNP | Ensembl ].
VAR_055987
Natural varianti1416 – 14161K → N.1 Publication
Corresponds to variant rs55782189 [ dbSNP | Ensembl ].
VAR_041489
Natural varianti1419 – 14191E → K.1 Publication
Corresponds to variant rs56181542 [ dbSNP | Ensembl ].
VAR_041490
Natural varianti1429 – 14291Q → R.1 Publication
Corresponds to variant rs55906201 [ dbSNP | Ensembl ].
VAR_041491
Natural varianti1461 – 14611I → V.4 Publications
Corresponds to variant rs1670283 [ dbSNP | Ensembl ].
VAR_031042
Natural varianti1491 – 14911K → R.3 Publications
Corresponds to variant rs1881420 [ dbSNP | Ensembl ].
VAR_031043
Natural varianti1529 – 15291D → E.3 Publications
Corresponds to variant rs1881421 [ dbSNP | Ensembl ].
VAR_031044
Natural varianti1599 – 15991P → H.
Corresponds to variant rs1881423 [ dbSNP | Ensembl ].
VAR_055988

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33172.1.
RefSeqiNP_004295.2. NM_004304.4.
UniGeneiHs.654469.

Genome annotation databases

EnsembliENST00000389048; ENSP00000373700; ENSG00000171094.
GeneIDi238.
KEGGihsa:238.
UCSCiuc002rmy.3. human.

Polymorphism databases

DMDMi296439447.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS33172.1.
RefSeqi NP_004295.2. NM_004304.4.
UniGenei Hs.654469.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KUP NMR - B 1571-1589 [» ]
2KUQ NMR - A 1571-1589 [» ]
2XB7 X-ray 2.50 A 1094-1407 [» ]
2XBA X-ray 1.95 A 1094-1407 [» ]
2XP2 X-ray 1.90 A 1093-1411 [» ]
2YFX X-ray 1.70 A 1093-1411 [» ]
2YHV X-ray 1.90 A 1093-1411 [» ]
2YJR X-ray 1.90 A 1093-1411 [» ]
2YJS X-ray 1.90 A 1093-1411 [» ]
2YS5 NMR - B 1571-1589 [» ]
2YT2 NMR - A 1571-1589 [» ]
3AOX X-ray 1.75 A 1069-1411 [» ]
3L9P X-ray 1.80 A 1072-1410 [» ]
3LCS X-ray 1.95 A 1072-1410 [» ]
3LCT X-ray 2.10 A 1072-1410 [» ]
4ANL X-ray 1.70 A 1093-1411 [» ]
4ANQ X-ray 1.76 A 1093-1411 [» ]
4ANS X-ray 1.85 A 1093-1411 [» ]
4CCB X-ray 2.03 A 1093-1411 [» ]
4CCU X-ray 2.00 A 1093-1411 [» ]
4CD0 X-ray 2.23 A 1093-1411 [» ]
4CLI X-ray 2.05 A 1093-1411 [» ]
4CLJ X-ray 1.66 A 1093-1411 [» ]
4CMO X-ray 1.83 A 1093-1411 [» ]
4CMT X-ray 1.73 A 1093-1411 [» ]
4CMU X-ray 1.80 A 1093-1411 [» ]
4CNH X-ray 1.90 A/B 1093-1411 [» ]
4CTB X-ray 1.79 A 1093-1411 [» ]
4CTC X-ray 2.03 A 1093-1411 [» ]
4DCE X-ray 2.03 A/B 1078-1410 [» ]
4FNW X-ray 1.75 A 1084-1410 [» ]
4FNX X-ray 1.70 A 1084-1410 [» ]
4FNY X-ray 2.45 A 1084-1410 [» ]
4FNZ X-ray 2.60 A 1084-1410 [» ]
4FOB X-ray 1.90 A 1058-1410 [» ]
4FOC X-ray 1.70 A 1058-1410 [» ]
4FOD X-ray 2.00 A 1078-1410 [» ]
4JOA X-ray 2.70 A 1072-1410 [» ]
4MKC X-ray 2.01 A 1072-1410 [» ]
ProteinModelPortali Q9UM73.
SMRi Q9UM73. Positions 1096-1480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106739. 46 interactions.
DIPi DIP-5954N.
IntActi Q9UM73. 7 interactions.
MINTi MINT-1133857.
STRINGi 9606.ENSP00000373700.

Chemistry

BindingDBi Q9UM73.
ChEMBLi CHEMBL2111387.
DrugBanki DB00171. Adenosine triphosphate.
DB08865. Crizotinib.
GuidetoPHARMACOLOGYi 1839.

PTM databases

PhosphoSitei Q9UM73.

Polymorphism databases

DMDMi 296439447.

Proteomic databases

PaxDbi Q9UM73.
PRIDEi Q9UM73.

Protocols and materials databases

DNASUi 238.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389048 ; ENSP00000373700 ; ENSG00000171094 .
GeneIDi 238.
KEGGi hsa:238.
UCSCi uc002rmy.3. human.

Organism-specific databases

CTDi 238.
GeneCardsi GC02M029327.
GeneReviewsi ALK.
H-InvDB HIX0024259.
HIX0030037.
HGNCi HGNC:427. ALK.
HPAi HPA010694.
MIMi 105590. gene.
613014. phenotype.
neXtProti NX_Q9UM73.
Orphaneti 300895. ALK-positive anaplastic large cell lymphoma.
364043. ALK-positive large B-cell lymphoma.
178342. Inflammatory myofibroblastic tumor.
635. Neuroblastoma.
357191. Selection of therapeutic option in non-small cell lung carcinoma.
PharmGKBi PA24719.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118818.
HOGENOMi HOG000231766.
HOVERGENi HBG018726.
InParanoidi Q9UM73.
KOi K05119.
OMAi LIQKVCI.
OrthoDBi EOG7GN2KT.
PhylomeDBi Q9UM73.
TreeFami TF351636.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
SignaLinki Q9UM73.

Miscellaneous databases

ChiTaRSi ALK. human.
EvolutionaryTracei Q9UM73.
GeneWikii Anaplastic_lymphoma_kinase.
GenomeRNAii 238.
NextBioi 948.
PROi Q9UM73.
SOURCEi Search...

Gene expression databases

Bgeei Q9UM73.
CleanExi HS_ALK.
ExpressionAtlasi Q9UM73. baseline and differential.
Genevestigatori Q9UM73.

Family and domain databases

Gene3Di 4.10.400.10. 1 hit.
InterProi IPR026830. ALK.
IPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR002172. LDrepeatLR_classA_rpt.
IPR000998. MAM_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.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view ]
PANTHERi PTHR24416:SF276. PTHR24416:SF276. 1 hit.
Pfami PF00629. MAM. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00192. LDLa. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57424. SSF57424. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, VARIANT VAL-1461.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-1461; 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 VAL-1461; 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH NPM1, VARIANT VAL-1461.
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ONCOGENE.
  8. "Activation of anaplastic lymphoma kinase receptor tyrosine kinase induces neuronal differentiation through the mitogen-activated protein kinase pathway."
    Souttou B., Carvalho N.B., Raulais D., Vigny M.
    J. Biol. Chem. 276:9526-9531(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, FUNCTION.
  9. "Identification of anaplastic lymphoma kinase as a receptor for the growth factor pleiotrophin."
    Stoica G.E., Kuo A., Aigner A., Sunitha I., Souttou B., Malerczyk C., Caughey D.J., Wen D., Karavanov A., Riegel A.T., Wellstein A.
    J. Biol. Chem. 276:16772-16779(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTN, FUNCTION.
  10. "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] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH ALO17 AND CARS.
  11. "Pleiotrophin signaling through anaplastic lymphoma kinase is rate-limiting for glioblastoma growth."
    Powers C., Aigner A., Stoica G.E., McDonnell K., Wellstein A.
    J. Biol. Chem. 277:14153-14158(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Anti-apoptotic signaling of pleiotrophin through its receptor, anaplastic lymphoma kinase."
    Bowden E.T., Stoica G.E., Wellstein A.
    J. Biol. Chem. 277:35862-35868(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Midkine binds to anaplastic lymphoma kinase (ALK) and acts as a growth factor for different cell types."
    Stoica G.E., Kuo A., Powers C., Bowden E.T., Sale E.B., Riegel A.T., Wellstein A.
    J. Biol. Chem. 277:35990-35998(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MDK, FUNCTION.
  14. "ALK receptor tyrosine kinase promotes cell growth and neurite outgrowth."
    Motegi A., Fujimoto J., Kotani M., Sakuraba H., Yamamoto T.
    J. Cell Sci. 117:3319-3329(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBL; IRS1; PIK3R1; PLCG1 AND SHC1, FUNCTION IN PHOSPHORYLATION OF CBL; IRS1 AND SHC1.
  15. "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] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY, PHOSPHORYLATION AT TYR-1278.
  16. "Differential induction of glioblastoma migration and growth by two forms of pleiotrophin."
    Lu K.V., Jong K.A., Kim G.Y., Singh J., Dia E.Q., Yoshimoto K., Wang M.Y., Cloughesy T.F., Nelson S.F., Mischel P.S.
    J. Biol. Chem. 280:26953-26964(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN GLIOBLASTOMA.
  17. "Role of the subcellular localization of ALK tyrosine kinase domain in neuronal differentiation of PC12 cells."
    Gouzi J.Y., Moog-Lutz C., Vigny M., Brunet-de Carvalho N.
    J. Cell Sci. 118:5811-5823(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT, ENZYME REGULATION, FUNCTION.
  18. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1078; TYR-1096; TYR-1131 AND TYR-1604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH SEC31A.
  20. "ALK activation induces Shc and FRS2 recruitment: Signaling and phenotypic outcomes in PC12 cells differentiation."
    Degoutin J., Vigny M., Gouzi J.Y.
    FEBS Lett. 581:727-734(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FRS2 AND SHC1, PHOSPHORYLATION AT TYR-1507, MUTAGENESIS OF TYR-1507, FUNCTION IN PHOSPHORYLATION OF FRS2; MAPK1/ERK2; MAPK3/ERK1 AND SHC1.
  21. "Anaplastic lymphoma kinase is activated through the pleiotrophin/receptor protein-tyrosine phosphatase beta/zeta signaling pathway: an alternative mechanism of receptor tyrosine kinase activation."
    Perez-Pinera P., Zhang W., Chang Y., Vega J.A., Deuel T.F.
    J. Biol. Chem. 282:28683-28690(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, ENZYME REGULATION.
  22. "Recruitment of insulin receptor substrate-1 and activation of NF-kappaB essential for midkine growth signaling through anaplastic lymphoma kinase."
    Kuo A.H., Stoica G.E., Riegel A.T., Wellstein A.
    Oncogene 26:859-869(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRS1 AND SHC, PHOSPHORYLATION AT TYR-1096, FUNCTION.
  23. "Anaplastic lymphoma kinase: signalling in development and disease."
    Palmer R.H., Vernersson E., Grabbe C., Hallberg B.
    Biochem. J. 420:345-361(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  24. "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.
  25. "Crystal structure of the ALK (anaplastic lymphoma kinase) catalytic domain."
    Lee C.C., Jia Y., Li N., Sun X., Ng K., Ambing E., Gao M.Y., Hua S., Chen C., Kim S., Michellys P.Y., Lesley S.A., Harris J.L., Spraggon G.
    Biochem. J. 430:425-437(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1072-1410.
  26. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1094-1407 IN COMPLEX WITH INHIBITOR.
  27. "Structural basis for the recognition of nucleophosmin-anaplastic lymphoma kinase oncoprotein by the phosphotyrosine binding domain of Suc1-associated neurotrophic factor-induced tyrosine-phosphorylated target-2."
    Koshiba S., Li H., Motoda Y., Tomizawa T., Kasai T., Tochio N., Yabuki T., Harada T., Watanabe S., Tanaka A., Shirouzu M., Kigawa T., Yamamoto T., Yokoyama S.
    J. Struct. Funct. Genomics 11:125-141(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1571-1589.
  28. "Structure of L1196M mutant anaplastic lymphoma kinase in complex with crizotinib."
    Mctigue M., Deng Y., Liu W., Brooun A.
    Submitted (MAY-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1093-1411 IN COMPLEX WITH CRIZOTINIB.
  29. "CH5424802, a selective ALK inhibitor capable of blocking the resistant gatekeeper mutant."
    Sakamoto H., Tsukaguchi T., Hiroshima S., Kodama T., Kobayashi T., Fukami T.A., Oikawa N., Tsukuda T., Ishii N., Aoki Y.
    Cancer Cell 19:679-690(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1069-1411 IN COMPLEX WITH INHIBITOR, ENZYME REGULATION.
  30. "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] 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.
  31. Cited for: VARIANTS NBLST3 ASN-1091; ALA-1128; ARG-1166; ASN-1171; ILE-1174; PRO-1192; CYS-1245; VAL-1245 THR-1250 AND GLN-1275.
  32. Cited for: VARIANTS NBLST3 VAL-1174; LEU-1174; CYS-1174; PRO-1192; GLN-1275 AND SER-1278, VARIANT LEU-1275.
  33. Cited for: VARIANTS NBLST3 MET-1151; LEU-1174; THR-1234; CYS-1245 AND GLN-1275.
  34. "The constitutive activity of the ALK mutated at positions F1174 or R1275 impairs receptor trafficking."
    Mazot P., Cazes A., Boutterin M.C., Figueiredo A., Raynal V., Combaret V., Hallberg B., Palmer R.H., Delattre O., Janoueix-Lerosey I., Vigny M.
    Oncogene 30:2017-2025(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS NBLST3 LEU-1174; VAL-1174 AND GLN-1275.

Entry informationi

Entry nameiALK_HUMAN
AccessioniPrimary (citable) accession number: Q9UM73
Secondary accession number(s): Q4ZFX9
, Q53QQ6, Q53RZ4, Q59FI3, Q9Y4K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 151 of the entry and version 3 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 cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  8. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3