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Q60592

- MAST2_MOUSE

UniProt

Q60592 - MAST2_MOUSE

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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

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

Mg2+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 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
Complete GO annotation...

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-KW
  2. cytoplasm Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. microtubule cytoskeleton Source: MGI
Complete GO annotation...

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 – 12751Phosphoserine1 Publication
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

MaxQBiQ60592.
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 265-366, 398-770, 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.
InParanoidiQ60592.
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.
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

        10         20         30         40         50
MVTGLSPLLF RKLSNPDIFA PTGKVKLQRQ LSQDDCKLRR GSLASSLSGK
60 70 80 90 100
QLLPLSSSVH SSVGQVTWQS TGEASNLVRM RNQSLGQSAP SLTAGLKELS
110 120 130 140 150
LPRRGSFCRT SNRKSLIVTS STSPTLPRPH SPLHGHTGNS PLDSPRNFSP
160 170 180 190 200
NAPAHFSFVP ARRTDGRRWS LASLPSSGYG TNTPSSTVSS SCSSQEKLHQ
210 220 230 240 250
LPFQPTADEL HFLTKHFSTE NVPDEEGRRS PRMRPRSRSL SPGRSPVSFD
260 270 280 290 300
SEIIMMNHVY KERFPKATAQ MEERPSLTFI SSNTPDSVLP LADGALSFIH
310 320 330 340 350
HQVIEMARDC LDKSRSGLIT SHYFYELQEN LEKLLQDAHE RSESSDVAFV
360 370 380 390 400
IQLVKKLMII IARPARLLEC LEFDPEEFYH LLEAAEGHAK EGHGIKCDIP
410 420 430 440 450
RYIVSQLGLT RDPLEEMAQL SSYDSPDTPE TDDSVEGRGV SQPSQKTPSE
460 470 480 490 500
EDFETIKLIS NGAYGAVFLV RHKSTRQRFA MKKINKQNLI LRNQIQQAFV
510 520 530 540 550
ERDILTFAEN PFVVSMFCSF ETKRHLCMVM EYVEGGDCAT LLKNIGALPV
560 570 580 590 600
DMVRLYFAET VLALEYLHNY GIVHRDLKPD NLLITSMGHI KLTDFGLSKI
610 620 630 640 650
GLMSLTTNLY EGHIEKDARE FLDKQVCGTP EYIAPEVILR QGYGKPVDWW
660 670 680 690 700
AMGIILYEFL VGCVPFFGDT PEELFGQVIS DEIVWPEGDD ALPPDAQDLT
710 720 730 740 750
SKLLHQNPLE RLGTSSAYEV KQHPFFMGLD WTGLLRQKAE FIPQLESEDD
760 770 780 790 800
TSYFDTRSER YHHVDSEDEE EVSEDGCLEI RQFSSCSPRF SKVYSSMERL
810 820 830 840 850
SLLEERRTPP PTKRSLSEEK EDHSDGLAGL KGRDRSWVIG SPEILRKRLS
860 870 880 890 900
VSESSHTESD SSPPMTVRHR CSGLPDGPHC PEETSSTPRK QQQEGIWVLI
910 920 930 940 950
PPSGEGSSRP VPERPLERQL KLDEEPPGQS SRCCPALETR GRGTPQLAEE
960 970 980 990 1000
ATAKAISDLA VRRARHRLLS GDSIEKRTTR PVNKVIKSAS ATALSLLIPS
1010 1020 1030 1040 1050
EHHACSPLAS PMSPHSQSSN PSSRDSSPSR DFLPALGSLR PPIIIHRAGK
1060 1070 1080 1090 1100
KYGFTLRAIR VYMGDTDVYT VHHMVWHVED GGPASEAGLR QGDLITHVNG
1110 1120 1130 1140 1150
EPVHGLVHTE VVELVLKSGN KVSISTTPLE NTSIKVGPAR KGSYKAKMAR
1160 1170 1180 1190 1200
RSKRSKGKDG QESRKRSSLF RKITKQASLL HTSRSLSSLN RSLSSGESGP
1210 1220 1230 1240 1250
GSPTHSHSLS PRSPPQGYRV APDAVHSVGG NSSQSSSPSS SVPSSPAGSG
1260 1270 1280 1290 1300
HTRPSSLHGL APKLQRQYRS PRRKSAGSIP LSPLAHTPSP PATAASPQRS
1310 1320 1330 1340 1350
PSPLSGHGSQ SFPTKLHLSP PLGRQLSRPK SAEPPRSPLL KRVQSAEKLA
1360 1370 1380 1390 1400
AALAAAEKKL APSRKHSLDL PHGELKKELT PREASPLEVV GTRSVLSGKG
1410 1420 1430 1440 1450
PLPGKGVLQP APSRALGTLR QDRAERRESL QKQEAIREVD SSEDDTDEEP
1460 1470 1480 1490 1500
ENSQATQEPR LSPHPEASHN LLPKGSGEGT EEDTFLHRDL KKQGPVLSGL
1510 1520 1530 1540 1550
VTGATLGSPR VDVPGLSPRK VSRPQAFEEA TNPLQVPSLS RSGPTSPTPS
1560 1570 1580 1590 1600
EGCWKAQHLH TQALTALCPS FSELTPTGCS AATSTSGKPG TWSWKFLIEG
1610 1620 1630 1640 1650
PDRASTNKTI TRKGEPANSQ DTNTTVPNLL KNLSPEEEKP QPPSVPGLTH
1660 1670 1680 1690 1700
PLLEVPSQNW PWESECEQME KEEPSLSITE VPDSSGDRRQ DIPCRAHPLS
1710 1720 1730
PETRPSLLWK SQELGGQQDH QDLALTSDEL LKQT
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 265-366, 398-770, 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

MaxQBi Q60592.
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.
InParanoidi Q60592.
KOi K08789.

Miscellaneous databases

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.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 131 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