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Protein

Transient receptor potential cation channel subfamily M member 7

Gene

Trpm7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential ion channel and serine/threonine-protein kinase. Divalent cation channel permeable to calcium and magnesium. Has a central role in magnesium ion homeostasis and in the regulation of anoxic neuronal cell death. Involved in TNF-induced necroptosis downstream of MLKL by mediating calcium influx. The kinase activity is essential for the channel function. May be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1).1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1622 – 16221ATP
Binding sitei1646 – 16461ATP
Binding sitei1718 – 17181ATP
Metal bindingi1751 – 17511Zinc
Active sitei1765 – 17651Proton acceptor
Binding sitei1767 – 17671ATP
Binding sitei1775 – 17751ATP
Metal bindingi1808 – 18081Zinc
Metal bindingi1810 – 18101Zinc
Metal bindingi1814 – 18141Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1792 – 17987ATP

GO - Molecular functioni

  • actin binding Source: MGI
  • ATP binding Source: UniProtKB-KW
  • calcium channel activity Source: MGI
  • kinase activity Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • myosin binding Source: MGI
  • protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • actomyosin structure organization Source: MGI
  • calcium-dependent cell-matrix adhesion Source: MGI
  • calcium ion transport Source: MGI
  • cellular magnesium ion homeostasis Source: InterPro
  • necroptotic process Source: UniProtKB
  • protein autophosphorylation Source: MGI
  • protein phosphorylation Source: MGI
  • protein tetramerization Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Calcium transport, Ion transport, Necrosis, Transport

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3295583. TRP channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily M member 7 (EC:2.7.11.1)
Alternative name(s):
Channel-kinase 1
Long transient receptor potential channel 7
Short name:
LTrpC-7
Short name:
LTrpC7
Transient receptor potential-phospholipase C-interacting kinase
Short name:
TRP-PLIK
Gene namesi
Name:Trpm7
Synonyms:Chak, Ltrpc7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1929996. Trpm7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 755755CytoplasmicSequence analysisAdd
BLAST
Transmembranei756 – 77621HelicalSequence analysisAdd
BLAST
Topological domaini777 – 85579ExtracellularSequence analysisAdd
BLAST
Transmembranei856 – 87621HelicalSequence analysisAdd
BLAST
Topological domaini877 – 91842CytoplasmicSequence analysisAdd
BLAST
Transmembranei919 – 93921HelicalSequence analysisAdd
BLAST
Topological domaini940 – 96223ExtracellularSequence analysisAdd
BLAST
Transmembranei963 – 98321HelicalSequence analysisAdd
BLAST
Topological domaini984 – 99512CytoplasmicSequence analysisAdd
BLAST
Transmembranei996 – 101621HelicalSequence analysisAdd
BLAST
Topological domaini1017 – 103519ExtracellularSequence analysisAdd
BLAST
Intramembranei1036 – 105621Pore-formingSequence analysisAdd
BLAST
Topological domaini1057 – 107418ExtracellularSequence analysisAdd
BLAST
Transmembranei1075 – 109521HelicalSequence analysisAdd
BLAST
Topological domaini1096 – 1863768CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
  • ruffle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1797 – 17971G → D: Severe reduction of kinase activity. 1 Publication
Mutagenesisi1810 – 18101C → A: Loss of kinase activity; when associated with A-1813. 1 Publication
Mutagenesisi1813 – 18131C → A: Loss of kinase activity; when associated with A-1820. 1 Publication

Chemistry

GuidetoPHARMACOLOGYi499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18631863Transient receptor potential cation channel subfamily M member 7PRO_0000215332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei1224 – 12241Phosphoserine1 Publication
Modified residuei1255 – 12551PhosphoserineCombined sources
Modified residuei1300 – 13001Phosphoserine1 Publication
Modified residuei1385 – 13851Phosphoserine1 Publication
Modified residuei1386 – 13861Phosphoserine1 Publication
Modified residuei1404 – 14041Phosphothreonine1 Publication
Modified residuei1445 – 14451PhosphoserineCombined sources
Modified residuei1466 – 14661Phosphothreonine1 Publication
Modified residuei1498 – 14981Phosphoserine1 Publication
Modified residuei1502 – 15021PhosphoserineCombined sources
Modified residuei1567 – 15671Phosphoserine1 Publication
Modified residuei1846 – 18461Phosphoserine1 Publication
Modified residuei1849 – 18491Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ923J1.
MaxQBiQ923J1.
PaxDbiQ923J1.
PRIDEiQ923J1.

PTM databases

iPTMnetiQ923J1.
PhosphoSiteiQ923J1.

Expressioni

Tissue specificityi

Found to be expressed in brain and skeletal muscle, with stronger signals in kidney, heart, liver and spleen.1 Publication

Gene expression databases

BgeeiQ923J1.
ExpressionAtlasiQ923J1. baseline and differential.
GenevisibleiQ923J1. MM.

Interactioni

Subunit structurei

Forms heterodimers with TRPM6. Interacts with PLCB1 (By similarity). Homodimer.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ActbP607102EBI-8010314,EBI-353957
Ddb1Q3U1J42EBI-8010314,EBI-2552275
DDX3XO005712EBI-8010314,EBI-353779From a different organism.
Myh9Q8VDD54EBI-8010314,EBI-400906
RYBPQ8N4883EBI-8010314,EBI-752324From a different organism.

GO - Molecular functioni

  • actin binding Source: MGI
  • myosin binding Source: MGI

Protein-protein interaction databases

BioGridi208438. 1 interaction.
IntActiQ923J1. 105 interactions.
MINTiMINT-2524821.
STRINGi10090.ENSMUSP00000099513.

Structurei

Secondary structure

1
1863
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1555 – 15628Combined sources
Helixi1563 – 15653Combined sources
Beta strandi1576 – 15838Combined sources
Beta strandi1585 – 15884Combined sources
Helixi1590 – 15956Combined sources
Beta strandi1598 – 16003Combined sources
Beta strandi1605 – 16139Combined sources
Beta strandi1620 – 163213Combined sources
Helixi1633 – 16353Combined sources
Beta strandi1641 – 16488Combined sources
Helixi1650 – 16556Combined sources
Turni1657 – 16593Combined sources
Helixi1664 – 168926Combined sources
Beta strandi1704 – 17085Combined sources
Turni1709 – 17124Combined sources
Beta strandi1713 – 17197Combined sources
Beta strandi1726 – 17294Combined sources
Helixi1741 – 175616Combined sources
Turni1757 – 17593Combined sources
Beta strandi1760 – 17645Combined sources
Beta strandi1767 – 17693Combined sources
Beta strandi1772 – 17754Combined sources
Beta strandi1777 – 17804Combined sources
Helixi1786 – 17883Combined sources
Beta strandi1790 – 17934Combined sources
Helixi1800 – 18078Combined sources
Helixi1812 – 18165Combined sources
Beta strandi1822 – 18243Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IA9X-ray2.00A/B1549-1828[»]
1IAHX-ray2.40A/B1549-1828[»]
1IAJX-ray2.80A/B1549-1828[»]
ProteinModelPortaliQ923J1.
SMRiQ923J1. Positions 1198-1249, 1549-1828.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ923J1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1592 – 1822231Alpha-type protein kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1198 – 125053By similarityAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the protein kinase superfamily. Alpha-type protein kinase family. ALPK subfamily.Curated
Contains 1 alpha-type protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3614. Eukaryota.
ENOG410XR5B. LUCA.
GeneTreeiENSGT00760000119127.
HOVERGENiHBG055663.
InParanoidiQ923J1.
KOiK04982.
OMAiKQGPTNP.
OrthoDBiEOG7NPFSC.
PhylomeDBiQ923J1.
TreeFamiTF314204.

Family and domain databases

InterProiIPR005821. Ion_trans_dom.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
IPR029601. TRPM7.
IPR032415. TRPM_tetra.
[Graphical view]
PANTHERiPTHR13800:SF8. PTHR13800:SF8. 3 hits.
PfamiPF02816. Alpha_kinase. 1 hit.
PF00520. Ion_trans. 1 hit.
PF16519. TRPM_tetra. 1 hit.
[Graphical view]
SMARTiSM00811. Alpha_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51158. ALPHA_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q923J1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQKSWIEST LTKRECVYII PSSKDPHRCL PGCQICQQLV RCFCGRLVKQ
60 70 80 90 100
HACFTASLAM KYSDVKLGEH FNQAIEEWSV EKHTEQSPTD AYGVINFQGG
110 120 130 140 150
SHSYRAKYVR LSYDTKPEII LQLLLKEWQM ELPKLVISVH GGMQKFELHP
160 170 180 190 200
RIKQLLGKGL IKAAVTTGAW ILTGGVNTGV AKHVGDALKE HASRSSRKIC
210 220 230 240 250
TIGIAPWGVI ENRNDLVGRD VVAPYQTLLN PLSKLNVLNN LHSHFILVDD
260 270 280 290 300
GTVGKYGAEV RLRRELEKTI NQQRIHARIG QGVPVVALIF EGGPNVILTV
310 320 330 340 350
LEYLQESPPV PVVVCEGTGR AADLLAYIHK QTEEGGNLPD AAEPDIISTI
360 370 380 390 400
KKTFNFGQSE AVHLFQTMME CMKKKELITV FHIGSEDHQD IDVAILTALL
410 420 430 440 450
KGTNASAFDQ LILTLAWDRV DIAKNHVFVY GQQWLVGSLE QAMLDALVMD
460 470 480 490 500
RVSFVKLLIE NGVSMHKFLT IPRLEELYNT KQGPTNPMLF HLIRDVKQGN
510 520 530 540 550
LPPGYKITLI DIGLVIEYLM GGTYRCTYTR KRFRLIYNSL GGNNRRSGRN
560 570 580 590 600
TSSSTPQLRK SHETFGNRAD KKEKMRHNHF IKTAQPYRPK MDASMEEGKK
610 620 630 640 650
KRTKDEIVDI DDPETKRFPY PLNELLIWAC LMKRQVMARF LWQHGEESMA
660 670 680 690 700
KALVACKIYR SMAYEAKQSD LVDDTSEELK QYSNDFGQLA VELLEQSFRQ
710 720 730 740 750
DETMAMKLLT YELKNWSNST CLKLAVSSRL RPFVAHTCTQ MLLSDMWMGR
760 770 780 790 800
LNMRKNSWYK VILSILVPPA ILMLEYKTKA EMSHIPQSQD AHQMTMEDSE
810 820 830 840 850
NNFHNITEEI PMEVFKEVKI LDSSDGKNEM EIHIKSKKLP ITRKFYAFYH
860 870 880 890 900
APIVKFWFNT LAYLGFLMLY TFVVLVKMEQ LPSVQEWIVI AYIFTYAIEK
910 920 930 940 950
VREVFMSEAG KISQKIKVWF SDYFNVSDTI AIISFFVGFG LRFGAKWNYI
960 970 980 990 1000
NAYDNHVFVA GRLIYCLNII FWYVRLLDFL AVNQQAGPYV MMIGKMVANM
1010 1020 1030 1040 1050
FYIVVIMALV LLSFGVPRKA ILYPHEEPSW SLAKDIVFHP YWMIFGEVYA
1060 1070 1080 1090 1100
YEIDVCANDS TLPTICGPGT WLTPFLQAVY LFVQYIIMVN LLIAFFNNVY
1110 1120 1130 1140 1150
LQVKAISNIV WKYQRYHFIM AYHEKPVLPP PLIILSHIVS LFCCVCKRRK
1160 1170 1180 1190 1200
KDKTSDGPKL FLTEEDQKKL HDFEEQCVEM YFDEKDDKFN SGSEERIRVT
1210 1220 1230 1240 1250
FERVEQMSIQ IKEVGDRVNY IKRSLQSLDS QIGHLQDLSA LTVDTLKTLT
1260 1270 1280 1290 1300
AQKASEASKV HNEITRELSI SKHLAQNLID DVPVRPLWKK PSAVNTLSSS
1310 1320 1330 1340 1350
LPQGDRESNN PFLCNIFMKD EKDPQYNLFG QDLPVIPQRK EFNIPEAGSS
1360 1370 1380 1390 1400
CGALFPSAVS PPELRQRRHG VEMLKIFNKN QKLGSSPNSS PHMSSPPTKF
1410 1420 1430 1440 1450
SVSTPSQPSC KSHLESTTKD QEPIFYKAAE GDNIEFGAFV GHRDSMDLQR
1460 1470 1480 1490 1500
FKETSNKIRE LLSNDTPENT LKHVGAAGYS ECCKTSTSLH SVQAESCSRR
1510 1520 1530 1540 1550
ASTEDSPEVD SKAALLPDWL RDRPSNREMP SEGGTLNGLA SPFKPVLDTN
1560 1570 1580 1590 1600
YYYSAVERNN LMRLSQSIPF VPVPPRGEPV TVYRLEESSP SILNNSMSSW
1610 1620 1630 1640 1650
SQLGLCAKIE FLSKEEMGGG LRRAVKVLCT WSEHDILKSG HLYIIKSFLP
1660 1670 1680 1690 1700
EVINTWSSIY KEDTVLHLCL REIQQQRAAQ KLTFAFNQMK PKSIPYSPRF
1710 1720 1730 1740 1750
LEVFLLYCHS AGQWFAVEEC MTGEFRKYNN NNGDEIIPTN TLEEIMLAFS
1760 1770 1780 1790 1800
HWTYEYTRGE LLVLDLQGVG ENLTDPSVIK AEEKRSCDMV FGPANLGEDA
1810 1820 1830 1840 1850
IKNFRAKHHC NSCCRKLKLP DLKRNDYTPD KIIFPQDESS DLNLQSGNST
1860
KESEATNSVR LML
Length:1,863
Mass (Da):212,399
Last modified:December 1, 2001 - v1
Checksum:i87551B4431CAD773
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661K → R in AAF73131 (Ref. 3) Curated
Sequence conflicti338 – 3381L → F in BAB29509 (PubMed:16141072).Curated
Sequence conflicti723 – 7231K → E in BAC33685 (PubMed:16141072).Curated
Sequence conflicti810 – 8101I → T in BAC33685 (PubMed:16141072).Curated
Sequence conflicti1494 – 14941Missing in AAK57433 (PubMed:11161216).Curated
Sequence conflicti1494 – 14941Missing in BAC26234 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY032951 mRNA. Translation: AAK50377.1.
AF376052 mRNA. Translation: AAK57433.1.
AF149013 mRNA. Translation: AAF73131.1.
AL732330 Genomic DNA. Translation: CAM14550.1.
AK049329 mRNA. Translation: BAC33685.1.
AK029000 mRNA. Translation: BAC26234.1.
AK014698 mRNA. Translation: BAB29509.1.
BC009137 mRNA. Translation: AAH09137.1.
CCDSiCCDS16689.1.
RefSeqiNP_001157797.1. NM_001164325.1.
NP_067425.2. NM_021450.2.
UniGeneiMm.244705.

Genome annotation databases

EnsembliENSMUST00000103224; ENSMUSP00000099513; ENSMUSG00000027365.
GeneIDi58800.
KEGGimmu:58800.
UCSCiuc008mef.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY032951 mRNA. Translation: AAK50377.1.
AF376052 mRNA. Translation: AAK57433.1.
AF149013 mRNA. Translation: AAF73131.1.
AL732330 Genomic DNA. Translation: CAM14550.1.
AK049329 mRNA. Translation: BAC33685.1.
AK029000 mRNA. Translation: BAC26234.1.
AK014698 mRNA. Translation: BAB29509.1.
BC009137 mRNA. Translation: AAH09137.1.
CCDSiCCDS16689.1.
RefSeqiNP_001157797.1. NM_001164325.1.
NP_067425.2. NM_021450.2.
UniGeneiMm.244705.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IA9X-ray2.00A/B1549-1828[»]
1IAHX-ray2.40A/B1549-1828[»]
1IAJX-ray2.80A/B1549-1828[»]
ProteinModelPortaliQ923J1.
SMRiQ923J1. Positions 1198-1249, 1549-1828.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208438. 1 interaction.
IntActiQ923J1. 105 interactions.
MINTiMINT-2524821.
STRINGi10090.ENSMUSP00000099513.

Chemistry

GuidetoPHARMACOLOGYi499.

PTM databases

iPTMnetiQ923J1.
PhosphoSiteiQ923J1.

Proteomic databases

EPDiQ923J1.
MaxQBiQ923J1.
PaxDbiQ923J1.
PRIDEiQ923J1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103224; ENSMUSP00000099513; ENSMUSG00000027365.
GeneIDi58800.
KEGGimmu:58800.
UCSCiuc008mef.2. mouse.

Organism-specific databases

CTDi54822.
MGIiMGI:1929996. Trpm7.

Phylogenomic databases

eggNOGiKOG3614. Eukaryota.
ENOG410XR5B. LUCA.
GeneTreeiENSGT00760000119127.
HOVERGENiHBG055663.
InParanoidiQ923J1.
KOiK04982.
OMAiKQGPTNP.
OrthoDBiEOG7NPFSC.
PhylomeDBiQ923J1.
TreeFamiTF314204.

Enzyme and pathway databases

ReactomeiR-MMU-3295583. TRP channels.

Miscellaneous databases

EvolutionaryTraceiQ923J1.
PROiQ923J1.
SOURCEiSearch...

Gene expression databases

BgeeiQ923J1.
ExpressionAtlasiQ923J1. baseline and differential.
GenevisibleiQ923J1. MM.

Family and domain databases

InterProiIPR005821. Ion_trans_dom.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
IPR029601. TRPM7.
IPR032415. TRPM_tetra.
[Graphical view]
PANTHERiPTHR13800:SF8. PTHR13800:SF8. 3 hits.
PfamiPF02816. Alpha_kinase. 1 hit.
PF00520. Ion_trans. 1 hit.
PF16519. TRPM_tetra. 1 hit.
[Graphical view]
SMARTiSM00811. Alpha_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51158. ALPHA_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "LTRPC7 is a Mg.ATP-regulated divalent cation channel required for cell viability."
    Nadler M.J.S., Hermosura M.C., Inabe K., Perraud A.-L., Zhu Q., Stokes A.J., Kurosaki T., Kinet J.-P., Penner R., Scharenberg A.M., Fleig A.
    Nature 411:590-595(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, FUNCTION.
  2. "TRP-PLIK, a bifunctional protein with kinase and ion channel activities."
    Runnels L.W., Yue L., Clapham D.E.
    Science 291:1043-1047(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PHOSPHORYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-1797; CYS-1810 AND CYS-1813.
    Strain: BALB/cJ.
  3. Matsushita M.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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 1-372; 632-1146 AND 1243-1863.
    Strain: C57BL/6J.
    Tissue: Head and Skin.
  6. "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] OF 1687-1863.
    Strain: FVB/N.
    Tissue: Mammary gland.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1255 AND SER-1445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney and Lung.
  9. "Identification of the phosphorylation sites on intact TRPM7 channels from mammalian cells."
    Kim T.Y., Shin S.K., Song M.Y., Lee J.E., Park K.S.
    Biochem. Biophys. Res. Commun. 417:1030-1034(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1224; SER-1300; SER-1385; SER-1386; THR-1404; THR-1466; SER-1498; SER-1567; SER-1846 AND SER-1849.
  10. "Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity."
    Yamaguchi H., Matsushita M., Nairn A.C., Kuriyan J.
    Mol. Cell 7:1047-1057(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1551-1828, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiTRPM7_MOUSE
AccessioniPrimary (citable) accession number: Q923J1
Secondary accession number(s): A2AI58
, Q8C7S7, Q8CE54, Q921Y5, Q925B2, Q9CUT2, Q9JLQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 124 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

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.