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Q7M6U3 (TEX14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Inactive serine/threonine-protein kinase TEX14
Alternative name(s):
Testis-expressed sequence 14
Testis-expressed sequence 14 protein
Gene names
Name:Tex14
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro. Ref.5 Ref.7 Ref.8 Ref.11

Subunit structure

Interacts with KIF23 and RBM44. Interacts with CEP55; inhibiting interaction between CEP55 and PDCD6IP/ALIX and TSG101. Ref.6 Ref.8 Ref.9

Subcellular location

Cytoplasm. Midbody. Chromosomecentromerekinetochore. Note: Detected in the intercellular bridges that connect male germ cell daughter cells after cell division. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11

Tissue specificity

Detected in testis and spermatogonia. Not detectable in the other tissues tested. Ref.1 Ref.3 Ref.5

Developmental stage

Detected at low levels in developing testis at 5 and 10 days after birth. Highly expressed in testis 15 and 20 days after birth. Highly expressed in pachytene, diplotene and meiotically dividing spermatocytes and in early round spermatids. Ref.3

Domain

The protein kinase domain is predicted to be catalytically inactive.

The GPPX3Y motif mediates interaction with CEP55 (Ref.8).

Post-translational modification

Phosphorylated on Thr residues by CDK1 during early phases of mitosis, promoting the interaction with PLK1 and recruitment to kinetochores. Phosphorylated on Ser-431 by PLK1 during late prometaphase promotes the rapid depletion from kinetochores and its subsequent degradation by the APC/C complex. Ref.11

Disruption phenotype

Male mice are sterile, due to the absence of intercellular bridges. Intercellular bridges do not form during spermatogenesis, and male mice are sterile. In females, embryonic intercellular bridges are also absent, mice have fewer oocytes, but they are fertile. Ref.5 Ref.7

Miscellaneous

Used as a marker for intercellular bridges (Ref.10).

Sequence similarities

Belongs to the protein kinase superfamily.

Contains 3 ANK repeats.

Contains 1 protein kinase domain.

Caution

Ser-370 is present instead of the conserved Asp which is expected to be an active site residue.

Sequence caution

The sequence CAI35965.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Kinetochore
   Coding sequence diversityAlternative splicing
   DomainANK repeat
Repeat
   LigandATP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processattachment of spindle microtubules to kinetochore

Inferred from mutant phenotype Ref.11. Source: UniProtKB

intercellular bridge organization

Inferred from direct assay Ref.5. Source: UniProtKB

male meiosis

Inferred from mutant phenotype Ref.5. Source: UniProtKB

mitotic sister chromatid separation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

mitotic spindle assembly checkpoint

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of cytokinesis

Inferred from direct assay Ref.8. Source: MGI

negative regulation of protein binding

Inferred from direct assay Ref.8. Source: MGI

   Cellular_componentcell

Inferred from mutant phenotype Ref.11. Source: UniProtKB

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

intercellular bridge

Inferred from direct assay Ref.5Ref.6. Source: UniProtKB

kinetochore

Inferred from direct assay Ref.11. Source: UniProtKB

midbody

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

protein kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cep55Q8BT0711EBI-6674575,EBI-2552328

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7M6U3-1)

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 (identifier: Q7M6U3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-218: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14501450Inactive serine/threonine-protein kinase TEX14
PRO_0000246996

Regions

Repeat27 – 5428ANK 1
Repeat55 – 8430ANK 2
Repeat88 – 11730ANK 3
Domain199 – 512314Protein kinase
Nucleotide binding205 – 2139ATP By similarity
Motif791 – 7977GPPX3Y
Motif889 – 8979D-box

Sites

Binding site2671ATP By similarity

Amino acid modifications

Modified residue4311Phosphoserine; by PLK1 Ref.11

Natural variations

Alternative sequence1 – 218218Missing in isoform 2.
VSP_019870

Experimental info

Mutagenesis4311S → A: Reduced phosphorylation by PLK1 and abolishes depletion from kinetochores and subsequent degradation by the APC/C complex. Ref.11
Mutagenesis4311S → D or E: Mimicks phosphorylation state; inducing early depletion from kinetochores and subsequent degradation by the APC/C complex. Ref.11
Mutagenesis7911G → A: Does not affect interaction with CEP55. Ref.8
Mutagenesis7921P → A: Abolishes interaction with CEP55. Ref.8
Mutagenesis7971Y → A: Abolishes interaction with CEP55. Ref.8
Mutagenesis889 – 8979Missing: Prevents degradation during metaphase. Ref.11
Sequence conflict3241T → A in AAK31963. Ref.1

Sequences

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

Last modified July 25, 2006. Version 2.
Checksum: 0628605EBE0FF0A4

FASTA1,450162,541
        10         20         30         40         50         60 
MSRGAPFPVP CPVLLGTFTD DSLEAQLHEY AKQGNCVKLK KILKKGVCVD AVNTQGQSAL 

        70         80         90        100        110        120 
FVAALLGHVK LVDVLVDYGS DPNHRCFDGS TPVHAAAFSG NQWILSKLLT AGGDLRLHDE 

       130        140        150        160        170        180 
KGRNPQAWAL TAGKDRSTQM VEFMQRCTSH MKAIIQGFSY DLLKKIDSPQ RLIGSPPWFG 

       190        200        210        220        230        240 
SLIQGSPNSS PNRQLKPGII SAQNIYSFGF GKFYLTSGMQ LTYPGSLPVI GEKEVVQADD 

       250        260        270        280        290        300 
EPTFSFFSGP YMVMTNLVWN RSRVTVKELN LPTRPHCSRL RLADLLIAEQ EHSSNLRHPN 

       310        320        330        340        350        360 
LLQLMAVCLS RDLEKIRLVY ERITVGTLFS VLHERRSQFP VLHMEVIVHL LLQVADALIY 

       370        380        390        400        410        420 
LHSRGFIHRS LSSYAVHIVS AGEARLTNLE YLTESQDSGA HRNVTRMPLP TQLYNWAAPE 

       430        440        450        460        470        480 
VVLQKAATVK SDIYSFSVII QEILTDSIPW NGLDGSLVKE TIALGNYLEA DVRLPEPYYD 

       490        500        510        520        530        540 
IVKSGIHAKQ KNRTMNLQDI RYILKNDLKE FIGAQKTQPT ESPRGQSYEP HPDVNICLGL 

       550        560        570        580        590        600 
TSEYQKDPPD LDIKELKEMG SQPHSPTDHS FLTVKPTLAP QTLDSSLSAQ KPDNANVPSP 

       610        620        630        640        650        660 
PAACLAEEVR SPTASQDSLC SFEINEIYSG CLTLGTDKEE ECLGTAASPE GDRPNQGDEL 

       670        680        690        700        710        720 
PSLEEELDKM ERELHCFCEE DKSISEVDTD LLFEDDDWQS DSLGSLNLPE PTREAKGKTS 

       730        740        750        760        770        780 
SWSKTDEYVS KCVLNLKISQ VMMQQSAEWL RKLEQEVEEL EWAQKELDSQ CSSLRDASLK 

       790        800        810        820        830        840 
FANAKFQPAV GPPSLAYLPP VMQLPGLKQP ENGGTWLTLA RSPGNEREFQ EGHFSKKPEK 

       850        860        870        880        890        900 
LSACGWKPFT QVSEESRGDC SELNNQLPTL RGPGKQSTGE QLPSTQEARE SLEKNTNQNS 

       910        920        930        940        950        960 
RSMASVSSEI YATKSRNNED NGEAHLKWRL AVKEMAEKAV SGQLLLPPWN PQSSAPFESK 

       970        980        990       1000       1010       1020 
VENESTPLPR PPIRGPESTE WQHILEYQRE NDEPKGNTKF GKMDNSDCDK NKHSRWTGLQ 

      1030       1040       1050       1060       1070       1080 
RFTGIRYPFF RNHEQPEQNE ASQASCDTSV GTEKFYSTSS PIGDDFERFQ DSFAQRQGYV 

      1090       1100       1110       1120       1130       1140 
EENFQIREIF EKNAEILTKP QFQAIQCAED KQDETLGETP KELKEKNTSL TDIQDLSSIT 

      1150       1160       1170       1180       1190       1200 
YDQDGYFKET SYKTPKLKHA PTSASTPLSP ESISSAASHY EDCLENTTFH VKRGSTFCWN 

      1210       1220       1230       1240       1250       1260 
GQEAMRTLSA KFTTVRERAK SLESLLASSK SLPAKLTDSK RLCMLSETGS SNVSAAFVTS 

      1270       1280       1290       1300       1310       1320 
THATKRKSLP RELAEATSQQ HLDELPPPAQ ELLDEIEQLK QQQVSSLASH ENTARDLSVT 

      1330       1340       1350       1360       1370       1380 
NKDKKHLEEQ ETNSSKDSSF LSSREIQDLE DTERAHSSLD EDLERFLQSP EENTALLDPT 

      1390       1400       1410       1420       1430       1440 
KGSTREKKNK DQDVVEQKRK KKESIKPERR ESDSSLGTLE EDELKPCFWK RLGWSEPSRI 

      1450 
IVLDQSDLSD 

« Hide

Isoform 2 [UniParc].

Checksum: A2CDBD69A483AF39
Show »

FASTA1,232138,851

References

« Hide 'large scale' references
[1]"An abundance of X-linked genes expressed in spermatogonia."
Wang P.J., McCarrey J.R., Yang F., Page D.C.
Nat. Genet. 27:422-426(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Tissue: Testis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Sequence and expression of testis-expressed gene 14 (Tex14): a gene encoding a protein kinase preferentially expressed during spermatogenesis."
Wu M.-H., Rajkovic A., Burns K.H., Yan W., Lin Y.-N., Matzuk M.M.
Gene Expr. Patterns 3:231-236(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-227 (ISOFORM 1), IDENTIFICATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-1396.
Strain: C57BL/6J.
Tissue: Egg.
[5]"TEX14 is essential for intercellular bridges and fertility in male mice."
Greenbaum M.P., Yan W., Wu M.H., Lin Y.N., Agno J.E., Sharma M., Braun R.E., Rajkovic A., Matzuk M.M.
Proc. Natl. Acad. Sci. U.S.A. 103:4982-4987(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ABSENCE OF PROTEIN KINASE ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[6]"Conversion of midbodies into germ cell intercellular bridges."
Greenbaum M.P., Ma L., Matzuk M.M.
Dev. Biol. 305:389-396(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KIF23.
[7]"Mouse TEX14 is required for embryonic germ cell intercellular bridges but not female fertility."
Greenbaum M.P., Iwamori N., Agno J.E., Matzuk M.M.
Biol. Reprod. 80:449-457(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
[8]"TEX14 interacts with CEP55 to block cell abscission."
Iwamori T., Iwamori N., Ma L., Edson M.A., Greenbaum M.P., Matzuk M.M.
Mol. Cell. Biol. 30:2280-2292(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CEP55, MUTAGENESIS OF GLY-791; PRO-792 AND TYR-797.
[9]"Identification and characterization of RBM44 as a novel intercellular bridge protein."
Iwamori T., Lin Y.N., Ma L., Iwamori N., Matzuk M.M.
PLoS ONE 6:E17066-E17066(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBM44.
[10]"Mouse germ cell clusters form by aggregation as well as clonal divisions."
Mork L., Tang H., Batchvarov I., Capel B.
Mech. Dev. 128:591-596(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Tex14, a plk1-regulated protein, is required for kinetochore-microtubule attachment and regulation of the spindle assembly checkpoint."
Mondal G., Ohashi A., Yang L., Rowley M., Couch F.J.
Mol. Cell 45:680-695(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-431, MUTAGENESIS OF SER-431 AND 889-ARG--ASN-897.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF285584 mRNA. Translation: AAK31963.1.
AL596086, AL669902 Genomic DNA. Translation: CAI35127.1.
AL669902 Genomic DNA. Translation: CAI35965.1. Different initiation.
AL669902, AL596086 Genomic DNA. Translation: CAI35966.1.
CU406969, CU406988 Genomic DNA. Translation: CAQ52018.1.
CU406988, CU406969 Genomic DNA. Translation: CAQ52278.1.
AY193717 mRNA. Translation: AAN86761.1.
AY193718 mRNA. Translation: AAN86762.1.
BK000966 mRNA. Translation: DAA01357.1.
BK000967 mRNA. Translation: DAA01358.1.
AK139808 mRNA. Translation: BAE24144.1.
CCDSCCDS48877.1. [Q7M6U3-1]
RefSeqNP_001186222.1. NM_001199293.1.
NP_113563.2. NM_031386.2. [Q7M6U3-1]
XP_006534611.1. XM_006534548.1. [Q7M6U3-2]
XP_006534612.1. XM_006534549.1. [Q7M6U3-2]
XP_006536545.1. XM_006536482.1. [Q7M6U3-2]
XP_006536546.1. XM_006536483.1. [Q7M6U3-2]
UniGeneMm.440758.

3D structure databases

ProteinModelPortalQ7M6U3.
SMRQ7M6U3. Positions 23-133, 225-533.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ7M6U3. 2 interactions.

PTM databases

PhosphoSiteQ7M6U3.

Proteomic databases

PaxDbQ7M6U3.
PRIDEQ7M6U3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000060835; ENSMUSP00000054444; ENSMUSG00000010342. [Q7M6U3-1]
GeneID83560.
KEGGmmu:83560.
UCSCuc007ktr.2. mouse. [Q7M6U3-1]

Organism-specific databases

CTD56155.
MGIMGI:1933227. Tex14.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00390000015123.
HOVERGENHBG094035.
InParanoidQ7M6U3.
KOK17540.
OMAFSFFSGP.
OrthoDBEOG75F4C9.
PhylomeDBQ7M6U3.
TreeFamTF328704.

Gene expression databases

ArrayExpressQ7M6U3.
BgeeQ7M6U3.
CleanExMM_TEX14.
GenevestigatorQ7M6U3.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio350646.
PROQ7M6U3.
SOURCESearch...

Entry information

Entry nameTEX14_MOUSE
AccessionPrimary (citable) accession number: Q7M6U3
Secondary accession number(s): B2KGL0 expand/collapse secondary AC list , Q3UT36, Q5NC10, Q5NC11, Q8CGK1, Q8CGK2, Q99MV8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: July 9, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot