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Q60592

- MAST2_MOUSE

UniProt

Q60592 - MAST2_MOUSE

Protein

Microtubule-associated serine/threonine-protein kinase 2

Gene

Mast2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Cofactori

    Magnesium.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei482 – 4821ATPBy similarityPROSITE-ProRule annotation
    Active sitei576 – 5761Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi459 – 4679ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. microtubule binding Source: MGI
    4. protein binding Source: IntAct
    5. protein serine/threonine kinase activity Source: MGI

    GO - Biological processi

    1. protein phosphorylation Source: UniProtKB
    2. regulation of interleukin-12 biosynthetic process Source: UniProtKB
    3. spermatid differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated serine/threonine-protein kinase 2 (EC:2.7.11.1)
    Gene namesi
    Name:Mast2Imported
    Synonyms:Mast2051 Publication
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:894676. Mast2.

    Subcellular locationi

    Membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmcytoskeleton 1 Publication. Cell junction 1 Publication
    Note: Colocalizes with beta 2-syntrophin and utrophin at neuromuscular junctions.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB-KW
    3. membrane Source: UniProtKB-SubCell
    4. microtubule cytoskeleton Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi482 – 4832KK → RA: Abolishes LPS-stimulated IL12B synthesis. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17341734Microtubule-associated serine/threonine-protein kinase 2PRO_0000086313Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141PhosphoserineBy similarity
    Modified residuei88 – 881PhosphoserineBy similarity
    Modified residuei149 – 1491PhosphoserineBy similarity
    Modified residuei841 – 8411PhosphoserineBy similarity
    Modified residuei970 – 9701PhosphoserineBy similarity
    Modified residuei1275 – 12751Phosphoserine2 Publications
    Modified residuei1446 – 14461PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylated and ubiquitinated. N-terminal ubiquitination leads to degradation of MAST2 by proteasome-mediated proteolysis. N-terminal phosphorylation appears to be a prerequisite for ubiquitination.3 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ60592.
    PRIDEiQ60592.

    PTM databases

    PhosphoSiteiQ60592.

    Expressioni

    Tissue specificityi

    Detected in round spermatids and residual bodies but not epididymal spermatozoa (at protein level). Expressed in adult but not fetal testis with levels increasing in parallel with testicular development. Also expressed at high levels in heart, lower levels in all other tissues tested.3 Publications

    Gene expression databases

    CleanExiMM_MAST2.
    GenevestigatoriQ60592.

    Interactioni

    Subunit structurei

    Interacts with CDHR2.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PTENP604844EBI-493888,EBI-696162From a different organism.
    UBBP0CG472EBI-493888,EBI-413034From a different organism.

    Protein-protein interaction databases

    BioGridi201600. 1 interaction.
    IntActiQ60592. 7 interactions.
    MINTiMINT-152278.
    STRINGi10090.ENSMUSP00000102095.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60592.
    SMRiQ60592. Positions 265-788, 1037-1131.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini453 – 726274Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini727 – 79569AGC-kinase C-terminalAdd
    BLAST
    Domaini1042 – 113089PDZPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000046662.
    HOVERGENiHBG052414.
    KOiK08789.

    Family and domain databases

    Gene3Di1.20.1480.20. 1 hit.
    2.30.42.10. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR015022. MA_Ser/Thr_Kinase_dom.
    IPR028779. MAST2.
    IPR023142. MAST_pre-PK_dom.
    IPR001478. PDZ.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24356:SF136. PTHR24356:SF136. 1 hit.
    PfamiPF08926. DUF1908. 1 hit.
    PF00595. PDZ. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00228. PDZ. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF140482. SSF140482. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS50106. PDZ. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60592-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVTGLSPLLF RKLSNPDIFA PTGKVKLQRQ LSQDDCKLRR GSLASSLSGK     50
    QLLPLSSSVH SSVGQVTWQS TGEASNLVRM RNQSLGQSAP SLTAGLKELS 100
    LPRRGSFCRT SNRKSLIVTS STSPTLPRPH SPLHGHTGNS PLDSPRNFSP 150
    NAPAHFSFVP ARRTDGRRWS LASLPSSGYG TNTPSSTVSS SCSSQEKLHQ 200
    LPFQPTADEL HFLTKHFSTE NVPDEEGRRS PRMRPRSRSL SPGRSPVSFD 250
    SEIIMMNHVY KERFPKATAQ MEERPSLTFI SSNTPDSVLP LADGALSFIH 300
    HQVIEMARDC LDKSRSGLIT SHYFYELQEN LEKLLQDAHE RSESSDVAFV 350
    IQLVKKLMII IARPARLLEC LEFDPEEFYH LLEAAEGHAK EGHGIKCDIP 400
    RYIVSQLGLT RDPLEEMAQL SSYDSPDTPE TDDSVEGRGV SQPSQKTPSE 450
    EDFETIKLIS NGAYGAVFLV RHKSTRQRFA MKKINKQNLI LRNQIQQAFV 500
    ERDILTFAEN PFVVSMFCSF ETKRHLCMVM EYVEGGDCAT LLKNIGALPV 550
    DMVRLYFAET VLALEYLHNY GIVHRDLKPD NLLITSMGHI KLTDFGLSKI 600
    GLMSLTTNLY EGHIEKDARE FLDKQVCGTP EYIAPEVILR QGYGKPVDWW 650
    AMGIILYEFL VGCVPFFGDT PEELFGQVIS DEIVWPEGDD ALPPDAQDLT 700
    SKLLHQNPLE RLGTSSAYEV KQHPFFMGLD WTGLLRQKAE FIPQLESEDD 750
    TSYFDTRSER YHHVDSEDEE EVSEDGCLEI RQFSSCSPRF SKVYSSMERL 800
    SLLEERRTPP PTKRSLSEEK EDHSDGLAGL KGRDRSWVIG SPEILRKRLS 850
    VSESSHTESD SSPPMTVRHR CSGLPDGPHC PEETSSTPRK QQQEGIWVLI 900
    PPSGEGSSRP VPERPLERQL KLDEEPPGQS SRCCPALETR GRGTPQLAEE 950
    ATAKAISDLA VRRARHRLLS GDSIEKRTTR PVNKVIKSAS ATALSLLIPS 1000
    EHHACSPLAS PMSPHSQSSN PSSRDSSPSR DFLPALGSLR PPIIIHRAGK 1050
    KYGFTLRAIR VYMGDTDVYT VHHMVWHVED GGPASEAGLR QGDLITHVNG 1100
    EPVHGLVHTE VVELVLKSGN KVSISTTPLE NTSIKVGPAR KGSYKAKMAR 1150
    RSKRSKGKDG QESRKRSSLF RKITKQASLL HTSRSLSSLN RSLSSGESGP 1200
    GSPTHSHSLS PRSPPQGYRV APDAVHSVGG NSSQSSSPSS SVPSSPAGSG 1250
    HTRPSSLHGL APKLQRQYRS PRRKSAGSIP LSPLAHTPSP PATAASPQRS 1300
    PSPLSGHGSQ SFPTKLHLSP PLGRQLSRPK SAEPPRSPLL KRVQSAEKLA 1350
    AALAAAEKKL APSRKHSLDL PHGELKKELT PREASPLEVV GTRSVLSGKG 1400
    PLPGKGVLQP APSRALGTLR QDRAERRESL QKQEAIREVD SSEDDTDEEP 1450
    ENSQATQEPR LSPHPEASHN LLPKGSGEGT EEDTFLHRDL KKQGPVLSGL 1500
    VTGATLGSPR VDVPGLSPRK VSRPQAFEEA TNPLQVPSLS RSGPTSPTPS 1550
    EGCWKAQHLH TQALTALCPS FSELTPTGCS AATSTSGKPG TWSWKFLIEG 1600
    PDRASTNKTI TRKGEPANSQ DTNTTVPNLL KNLSPEEEKP QPPSVPGLTH 1650
    PLLEVPSQNW PWESECEQME KEEPSLSITE VPDSSGDRRQ DIPCRAHPLS 1700
    PETRPSLLWK SQELGGQQDH QDLALTSDEL LKQT 1734
    Length:1,734
    Mass (Da):190,534
    Last modified:November 1, 1996 - v1
    Checksum:i97292FACD85F12E3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621R → RSHGHRTD in AAH60703. (PubMed:15489334)Curated
    Sequence conflicti232 – 2321R → A in AAH60703. (PubMed:15489334)Curated
    Sequence conflicti275 – 2784PSLT → LAD in AAH60703. (PubMed:15489334)Curated
    Sequence conflicti478 – 4781R → C(PubMed:16141072)Curated
    Sequence conflicti1228 – 12281Missing(PubMed:15489334)Curated
    Sequence conflicti1228 – 12281Missing(PubMed:16141072)Curated
    Sequence conflicti1502 – 15021T → S(PubMed:16141072)Curated
    Sequence conflicti1521 – 15211V → L(PubMed:15489334)Curated
    Sequence conflicti1521 – 15211V → L(PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02313 mRNA. Translation: AAC04312.1.
    BC060703 mRNA. Translation: AAH60703.1.
    AB093264 mRNA. Translation: BAC41448.1.
    PIRiA54602.
    RefSeqiNP_001036208.1. NM_001042743.2.
    NP_032667.2. NM_008641.3.
    UniGeneiMm.9287.

    Genome annotation databases

    GeneIDi17776.
    KEGGimmu:17776.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02313 mRNA. Translation: AAC04312.1 .
    BC060703 mRNA. Translation: AAH60703.1 .
    AB093264 mRNA. Translation: BAC41448.1 .
    PIRi A54602.
    RefSeqi NP_001036208.1. NM_001042743.2.
    NP_032667.2. NM_008641.3.
    UniGenei Mm.9287.

    3D structure databases

    ProteinModelPortali Q60592.
    SMRi Q60592. Positions 265-788, 1037-1131.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201600. 1 interaction.
    IntActi Q60592. 7 interactions.
    MINTi MINT-152278.
    STRINGi 10090.ENSMUSP00000102095.

    PTM databases

    PhosphoSitei Q60592.

    Proteomic databases

    PaxDbi Q60592.
    PRIDEi Q60592.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 17776.
    KEGGi mmu:17776.

    Organism-specific databases

    CTDi 23139.
    MGIi MGI:894676. Mast2.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000046662.
    HOVERGENi HBG052414.
    KOi K08789.

    Miscellaneous databases

    ChiTaRSi MAST2. mouse.
    NextBioi 292503.
    PROi Q60592.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_MAST2.
    Genevestigatori Q60592.

    Family and domain databases

    Gene3Di 1.20.1480.20. 1 hit.
    2.30.42.10. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR015022. MA_Ser/Thr_Kinase_dom.
    IPR028779. MAST2.
    IPR023142. MAST_pre-PK_dom.
    IPR001478. PDZ.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR24356:SF136. PTHR24356:SF136. 1 hit.
    Pfami PF08926. DUF1908. 1 hit.
    PF00595. PDZ. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00228. PDZ. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF140482. SSF140482. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS50106. PDZ. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel 205-kDa testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette."
      Walden P.D., Cowan N.J.
      Mol. Cell. Biol. 13:7625-7635(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Strain: Swiss WebsterImported.
      Tissue: TestisImported.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6Imported.
      Tissue: BrainImported.
    3. "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.
      , 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 302-1734.
      Tissue: Brain.
    4. "Increased activity associated with the MAST205 protein kinase complex during mammalian spermiogenesis."
      Walden P.D., Millette C.F.
      Biol. Reprod. 55:1039-1044(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    5. "Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases."
      Lumeng C., Phelps S., Crawford G.E., Walden P.D., Barald K., Chamberlain J.S.
      Nat. Neurosci. 2:611-617(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SNTB2.
    6. "Microtubule-associated serine/threonine kinase-205 kDa and Fc gamma receptor control IL-12 p40 synthesis and NF-kappa B activation."
      Zhou H., Xiong H., Li H., Plevy S.E., Walden P.D., Sassaroli M., Prestwich G.D., Unkeless J.C.
      J. Immunol. 172:2559-2568(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION, MUTAGENESIS OF 482-LYS-LYS-483.
    7. "Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and MAST205 stability."
      Xiong H., Li H., Chen Y., Zhao J., Unkeless J.C.
      J. Biol. Chem. 279:43675-43683(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION, PHOSPHORYLATION, INTERACTION WITH TRAF6.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiMAST2_MOUSE
    AccessioniPrimary (citable) accession number: Q60592
    Secondary accession number(s): Q6P9M1, Q8CHD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3