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Q7RTN6 (STRAA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
STE20-related kinase adapter protein alpha

Short name=STRAD alpha
Alternative name(s):
STE20-related adapter protein
Serologically defined breast cancer antigen NY-BR-96
Gene names
Name:STRADA
Synonyms:LYK5, STRAD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation. Ref.7 Ref.8 Ref.12

Subunit structure

Component of a trimeric complex composed of STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm and stimulates its catalytic activity. Ref.12

Subcellular location

Nucleus. Cytoplasm Ref.7 Ref.8.

Domain

The protein kinase domain is predicted to be catalytically inactive.

Involvement in disease

A homozygous 7-kb deletion involving STRADA is a cause of a syndrome characterized by polyhydramnios, megalencephaly and symptomatic epilepsy.

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 protein kinase domain.

Binary interactions

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.7 (identifier: Q7RTN6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.2 Ref.3 (identifier: Q7RTN6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     5-41: Missing.
     368-417: PSASTLLNHSFFKQIKRRASEALPELLRPVTPITNFEGSQSQDHSGIFGL → YPCWPGPGLRESRGCSGG
     418-431: Missing.
Isoform 3 Ref.3 (identifier: Q7RTN6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     5-41: Missing.
Isoform 4 (identifier: Q7RTN6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     32-75: Missing.
     338-431: DSPSHPYHRT...EELEVDDWEF → PVPAPS
Note: No experimental confirmation available.
Isoform 5 (identifier: Q7RTN6-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
Isoform 6 (identifier: Q7RTN6-6)

The sequence of this isoform differs from the canonical sequence as follows:
     13-41: Missing.
     338-431: DSPSHPYHRT...EELEVDDWEF → PVPAPS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431STE20-related kinase adapter protein alpha
PRO_0000260035

Regions

Domain69 – 379311Protein kinase

Amino acid modifications

Modified residue3291Phosphothreonine; by LKB1 Ref.7
Modified residue4191Phosphothreonine; by LKB1 Ref.7

Natural variations

Alternative sequence1 – 5858Missing in isoform 5.
VSP_044278
Alternative sequence5 – 4137Missing in isoform 2 and isoform 3. Ref.2 Ref.3
VSP_052219
Alternative sequence13 – 4129Missing in isoform 6.
VSP_044717
Alternative sequence32 – 7544Missing in isoform 4.
VSP_043707
Alternative sequence338 – 43194DSPSH…DDWEF → PVPAPS in isoform 4 and isoform 6.
VSP_043708
Alternative sequence368 – 41750PSAST…GIFGL → YPCWPGPGLRESRGCSGG in isoform 2. Ref.3
VSP_052220
Alternative sequence418 – 43114Missing in isoform 2. Ref.3
VSP_052221
Natural variant131R → W. Ref.13
Corresponds to variant rs35808156 [ dbSNP | Ensembl ].
VAR_041377
Natural variant601S → I. Ref.13
Corresponds to variant rs56271007 [ dbSNP | Ensembl ].
VAR_041378
Natural variant641P → S. Ref.13
Corresponds to variant rs55695051 [ dbSNP | Ensembl ].
VAR_041379

Experimental info

Mutagenesis1851Y → F: Suppresses STK11/LKB1 activation without affecting complex assembly. Ref.12
Mutagenesis2311H → A: Inhibits interaction with STK11/LKB1; when associated with A-. Ref.12
Mutagenesis2331F → A: Inhibits interaction with STK11/LKB1; when associated with A-. Ref.12
Mutagenesis2411L → A: Inhibits interaction with STK11/LKB1. Ref.12
Mutagenesis2511Q → A: Inhibits interaction with STK11/LKB1. Ref.12
Mutagenesis3291T → A: Loss of STK11/LKB1-mediated phosphorylation. Ref.7
Mutagenesis4191T → A: Loss of STK11/LKB1-mediated phosphorylation. Ref.7
Sequence conflict1631F → S in BAG62879. Ref.3
Sequence conflict3391S → W in AAG48269. Ref.1
Sequence conflict3631N → H in BAC11349. Ref.3
Sequence conflict3881E → K in AAG48269. Ref.1

Secondary structure

...................................................... 431
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 9CC0A78D9CC6FC2C

FASTA43148,369
        10         20         30         40         50         60 
MSFLVSKPER IRRWVSEKFI VEGLRDLELF GEQPPGDTRR KTNDASSESI ASFSKQEVMS 

        70         80         90        100        110        120 
SFLPEGGCYE LLTVIGKGFE DLMTVNLARY KPTGEYVTVR RINLEACSNE MVTFLQGELH 

       130        140        150        160        170        180 
VSKLFNHPNI VPYRATFIAD NELWVVTSFM AYGSAKDLIC THFMDGMNEL AIAYILQGVL 

       190        200        210        220        230        240 
KALDYIHHMG YVHRSVKASH ILISVDGKVY LSGLRSNLSM ISHGQRQRVV HDFPKYSVKV 

       250        260        270        280        290        300 
LPWLSPEVLQ QNLQGYDAKS DIYSVGITAC ELANGHVPFK DMPATQMLLE KLNGTVPCLL 

       310        320        330        340        350        360 
DTSTIPAEEL TMSPSRSVAN SGLSDSLTTS TPRPSNGDSP SHPYHRTFSP HFHHFVEQCL 

       370        380        390        400        410        420 
QRNPDARPSA STLLNHSFFK QIKRRASEAL PELLRPVTPI TNFEGSQSQD HSGIFGLVTN 

       430 
LEELEVDDWE F 

« Hide

Isoform 2 [UniParc].

Checksum: B4A9F1EDE0E86EF4
Show »

FASTA34838,597
Isoform 3 [UniParc].

Checksum: 35C80CA906403ADC
Show »

FASTA39443,962
Isoform 4 [UniParc].

Checksum: 164D23B3189837FC
Show »

FASTA29933,277
Isoform 5 [UniParc].

Checksum: 3E2837347D7BC42C
Show »

FASTA37341,701
Isoform 6 [UniParc].

Checksum: 12F519738B45CDF6
Show »

FASTA31434,625

References

« Hide 'large scale' references
[1]"Humoral immunity to human breast cancer: antigen definition and quantitative analysis of mRNA expression."
Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O., Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.
Cancer Immun. 1:4-4(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Mammary tumor.
[2]"Cloning, characterization and localization of lyk5 gene."
Shan Y.X., Huang C.Q., Yu L.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 6).
Tissue: Synovium and Teratocarcinoma.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Lymph node.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD."
Baas A.F., Boudeau J., Sapkota G.P., Smit L., Medema R., Morrice N.A., Alessi D.R., Clevers H.C.
EMBO J. 22:3062-3072(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STK11/LKB1, MUTAGENESIS OF THR-329 AND THR-419, PHOSPHORYLATION AT THR-329 AND THR-419.
[8]"MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm."
Boudeau J., Baas A.F., Deak M., Morrice N.A., Kieloch A., Schutkowski M., Prescott A.R., Clevers H.C., Alessi D.R.
EMBO J. 22:5102-5114(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STK11/LKB1 AND CAB39.
[9]"Polyhydramnios, megalencephaly and symptomatic epilepsy caused by a homozygous 7-kilobase deletion in LYK5."
Puffenberger E.G., Strauss K.A., Ramsey K.E., Craig D.W., Stephan D.A., Robinson D.L., Hendrickson C.L., Gottlieb S., Ramsay D.A., Siu V.M., Heuer G.G., Crino P.B., Morton D.H.
Brain 130:1929-1941(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PMSE.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Crystal structure of MO25 alpha in complex with the C-terminus of the pseudo kinase STE20-related adaptor."
Milburn C.C., Boudeau J., Deak M., Alessi D.R., van Aalten D.M.
Nat. Struct. Mol. Biol. 11:193-200(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CAB39.
[12]"Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation."
Zeqiraj E., Filippi B.M., Deak M., Alessi D.R., van Aalten D.M.
Science 326:1707-1711(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 59-431 IN COMPLEX WITH STK11/LKB1 AND CAB39, IDENTIFICATION IN A COMPLEX WITH STK11/LKB1 AND CAB39, FUNCTION, MUTAGENESIS OF TYR-185; HIS-231; PHE-233; LEU-241 AND GLN-251.
[13]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-13; ILE-60 AND SER-64.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF308302 mRNA. Translation: AAG48269.1.
AY290821 mRNA. Translation: AAP42280.1.
AK074771 mRNA. Translation: BAC11197.1.
AK075005 mRNA. Translation: BAC11349.1.
AK293160 mRNA. Translation: BAG56704.1.
AK301331 mRNA. Translation: BAG62879.1.
AL832407 mRNA. Translation: CAI46194.1.
AC015651 Genomic DNA. No translation available.
AC046185 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94283.1.
BK001542 mRNA. Translation: DAA01797.1.
CCDSCCDS11642.1. [Q7RTN6-2]
CCDS32703.1. [Q7RTN6-1]
CCDS42367.1. [Q7RTN6-5]
CCDS54156.1. [Q7RTN6-4]
CCDS58585.1. [Q7RTN6-6]
RefSeqNP_001003786.1. NM_001003786.2. [Q7RTN6-3]
NP_001003787.1. NM_001003787.2. [Q7RTN6-1]
NP_001003788.1. NM_001003788.2. [Q7RTN6-5]
NP_001159441.1. NM_001165969.1. [Q7RTN6-6]
NP_001159442.1. NM_001165970.1. [Q7RTN6-4]
NP_699166.2. NM_153335.5. [Q7RTN6-2]
XP_005257856.1. XM_005257799.1. [Q7RTN6-5]
UniGeneHs.514402.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UPKX-ray1.85B420-431[»]
2WTKX-ray2.65B/E59-431[»]
3GNIX-ray2.35B59-431[»]
ProteinModelPortalQ7RTN6.
SMRQ7RTN6. Positions 60-431.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124934. 7 interactions.
DIPDIP-35775N.
IntActQ7RTN6. 2 interactions.
MINTMINT-1338485.
STRING9606.ENSP00000336655.

Chemistry

ChEMBLCHEMBL1795198.

PTM databases

PhosphoSiteQ7RTN6.

Polymorphism databases

DMDM74759034.

Proteomic databases

MaxQBQ7RTN6.
PaxDbQ7RTN6.
PRIDEQ7RTN6.

Protocols and materials databases

DNASU92335.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336174; ENSP00000336655; ENSG00000266173. [Q7RTN6-1]
ENST00000375840; ENSP00000365000; ENSG00000266173. [Q7RTN6-5]
ENST00000392950; ENSP00000376677; ENSG00000266173. [Q7RTN6-2]
ENST00000447001; ENSP00000398841; ENSG00000266173. [Q7RTN6-4]
ENST00000582137; ENSP00000462922; ENSG00000266173. [Q7RTN6-6]
GeneID92335.
KEGGhsa:92335.
UCSCuc002jbm.3. human. [Q7RTN6-1]
uc002jbo.3. human. [Q7RTN6-3]
uc002jbp.3. human. [Q7RTN6-2]
uc010wpq.2. human. [Q7RTN6-4]

Organism-specific databases

CTD92335.
GeneCardsGC17M061780.
HGNCHGNC:30172. STRADA.
HPAHPA031637.
MIM608626. gene.
611087. phenotype.
neXtProtNX_Q7RTN6.
PharmGKBPA164726342.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000237355.
HOVERGENHBG055069.
InParanoidQ7RTN6.
KOK08271.
OMAFFKQIKR.
PhylomeDBQ7RTN6.
TreeFamTF319817.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ7RTN6.

Gene expression databases

ArrayExpressQ7RTN6.
BgeeQ7RTN6.
CleanExHS_STRADA.
GenevestigatorQ7RTN6.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTRADA. human.
EvolutionaryTraceQ7RTN6.
GeneWikiLYK5.
GenomeRNAi92335.
NextBio35536174.
PROQ7RTN6.
SOURCESearch...

Entry information

Entry nameSTRAA_HUMAN
AccessionPrimary (citable) accession number: Q7RTN6
Secondary accession number(s): B4DDE3 expand/collapse secondary AC list , B4DW17, J3KTC9, Q5JPI2, Q7Z4K9, Q8NC31, Q8NCF1, Q9H272
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM