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Reviewed, UniProtKB/Swiss-Prot Q9UM73 (ALK_HUMAN)

Last modified October 13, 2009. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ALK tyrosine kinase receptor
    EC=2.7.10.1
Alternative name(s):
    Anaplastic lymphoma kinase
    CD_antigen=CD246
Gene names
Name: ALK
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1620 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 16201602ALK tyrosine kinase receptor
PRO_0000016740

Regions

Topological domain19 – 10381020Extracellular Potential
Transmembrane1039 – 105921 Potential
Topological domain1060 – 1620561Cytoplasmic Potential
Domain264 – 427164MAM 1
Domain437 – 47337LDL-receptor class A
Domain478 – 636159MAM 2
Domain1116 – 1392277Protein kinase
Nucleotide binding1122 – 11309ATP By similarity
Compositional bias816 – 940125Gly-rich

Sites

Active site12491Proton acceptor By similarity
Binding site11501ATP By similarity

Amino acid modifications

Modified residue2111Phosphoserine Ref.12
Modified residue10781Phosphotyrosine Ref.10 Ref.13
Modified residue10921Phosphotyrosine Ref.10
Modified residue10961Phosphotyrosine Ref.10 Ref.13
Modified residue11311Phosphotyrosine Ref.10
Modified residue12781Phosphotyrosine Ref.10 Ref.13
Modified residue12821Phosphotyrosine; by autocatalysis Ref.10 Ref.13
Modified residue12831Phosphotyrosine Ref.13
Modified residue13591Phosphotyrosine Ref.13
Modified residue15071Phosphotyrosine Ref.10 Ref.13
Modified residue15841Phosphotyrosine Ref.10
Modified residue16041Phosphotyrosine Ref.10
Glycosylation1691N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation4111N-linked (GlcNAc...) Potential
Glycosylation4241N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation5631N-linked (GlcNAc...) Potential
Glycosylation5711N-linked (GlcNAc...) Potential
Glycosylation6271N-linked (GlcNAc...) Potential
Glycosylation7091N-linked (GlcNAc...) Potential
Glycosylation8081N-linked (GlcNAc...) Potential
Glycosylation8631N-linked (GlcNAc...) Potential
Glycosylation8641N-linked (GlcNAc...) Potential
Glycosylation8861N-linked (GlcNAc...) Potential
Glycosylation9861N-linked (GlcNAc...) Potential

Natural variations

Natural variant901S → L
VAR_041477
Natural variant1631V → L
VAR_041478
Natural variant2961E → Q
VAR_041479
Natural variant4761V → A: dbSNP rs35093491. Ref.15
VAR_041480
Natural variant5601L → F in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.15
VAR_041481
Natural variant6801T → I: dbSNP rs35228363. Ref.15
VAR_041482
Natural variant7041A → T
VAR_041483
Natural variant8771A → S in an ovarian serous carcinoma sample; somatic mutation. Ref.15
VAR_041484
Natural variant10121T → M
VAR_041485
Natural variant11211G → D
VAR_041486
Natural variant12741A → T: dbSNP rs45502292. Ref.15
VAR_041487
Natural variant13281M → L
VAR_041488
Natural variant13761F → S: dbSNP rs17694720.
VAR_055987
Natural variant14161K → N
VAR_041489
Natural variant14191E → K
VAR_041490
Natural variant14291Q → R
VAR_041491
Natural variant14611V → I: dbSNP rs1670283. Ref.5
VAR_031042
Natural variant14911K → R: dbSNP rs1881420. Ref.15 Ref.3 Ref.4
VAR_031043
Natural variant15291D → E: dbSNP rs1881421. Ref.15 Ref.3 Ref.4
VAR_031044
Natural variant15991P → H: dbSNP rs1881423.
VAR_055988

Experimental info

Sequence conflict361P → S in AAB71619. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UM73-1 [UniParc].

Last modified March 6, 2007. Version 2.
Checksum: A4B96DFF6D329777

FASTA1,620176,428
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.

Cross-references

Sequence databases

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.
IPIIPI00395632.
RefSeqNP_004295.2.
UniGeneHs.654469

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2YS5NMR-B1571-1589[»]
2YT2NMR-A1571-1589[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9UM73. 61 interactions.
STRINGQ9UM73.

PTM databases

PhosphoSiteQ9UM73.

Proteomic databases

PRIDEQ9UM73.

Genome annotation databases

EnsemblENST00000389048; 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]
GeneID238.
KEGGhsa:238.
UCSCuc002rmy.1. human.

Organism-specific databases

CTD238.
GeneCardsGC02M029327.
H-InvDBHIX0024259.
HIX0030037.
HGNCHGNC:427. ALK.
HPAHPA010694.
MIM105590. gene.
Orphanet98841. Anaplastic large cell lymphoma.
635. Neuroblastoma.
PharmGKBPA24719.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9UM73.
HOVERGENQ9UM73.

Enzyme and pathway databases

BRENDA2.7.10.1. 247.

Gene expression databases

ArrayExpressQ9UM73.
BgeeQ9UM73.
CleanExHS_ALK.
GenevestigatorQ9UM73.
GermOnlineENSG00000171094. Homo sapiens.

Family and domain databases

InterProIPR002172. 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]
PfamPF00629. MAM. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00192. LDLa. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS01209. 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]
ProtoNetSearch...

Other Resources

DrugBankDB00171. Adenosine triphosphate.
NextBio948.
SOURCESearch...

Entry information

Entry nameALK_HUMAN
AccessionPrimary (citable) accession number: Q9UM73
Secondary accession number(s): Q4ZFX9 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents