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Q96QT4 (TRPM7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:TRPM7
Synonyms:CHAK1, LTRPC7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1865 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.6 Ref.7 Ref.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer. Interacts with PLCB1 By similarity. Forms heterodimers with TRPM6. Ref.8

Subcellular location

Membrane; Multi-pass membrane protein Probable.

Post-translational modification

Autophosphorylated By similarity.

Involvement in disease

Amyotrophic lateral sclerosis-parkinsonism/dementia complex 1 (ALS-PDC1) [MIM:105500]: A neurodegenerative disorder characterized by chronic, progressive and uniformly fatal amyotrophic lateral sclerosis and parkinsonism-dementia. Both diseases are known to occur in the same kindred, the same sibship and even the same individual.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Sequence similarities

In the C-terminal section; belongs to the protein kinase superfamily. Alpha-type protein kinase family. ALPK subfamily.

In the N-terminal section; belongs to the transient receptor (TC 1.A.4) family. LTrpC subfamily. TRPM7 sub-subfamily. [View classification]

Contains 1 alpha-type protein kinase domain.

Sequence caution

The sequence BAC11462.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD18773.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Necrosis
Transport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseAmyotrophic lateral sclerosis
Neurodegeneration
Parkinsonism
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionCalcium channel
Ion channel
Kinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactomyosin structure organization

Inferred from electronic annotation. Source: Ensembl

calcium ion transmembrane transport

Traceable author statement. Source: Reactome

calcium-dependent cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement. Source: Reactome

necroptotic process

Inferred from mutant phenotype Ref.12. Source: UniProtKB

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

ruffle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18651865Transient receptor potential cation channel subfamily M member 7
PRO_0000215331

Regions

Topological domain1 – 755755Cytoplasmic Potential
Transmembrane756 – 77621Helical; Potential
Topological domain777 – 85579Extracellular Potential
Transmembrane856 – 87621Helical; Potential
Topological domain877 – 91842Cytoplasmic Potential
Transmembrane919 – 93921Helical; Potential
Topological domain940 – 96223Extracellular Potential
Transmembrane963 – 98321Helical; Potential
Topological domain984 – 99512Cytoplasmic Potential
Transmembrane996 – 101621Helical; Potential
Topological domain1017 – 103519Extracellular Potential
Intramembrane1036 – 105621Pore-forming; Potential
Topological domain1057 – 107418Extracellular Potential
Transmembrane1075 – 109521Helical; Potential
Topological domain1096 – 1865770Cytoplasmic Potential
Domain1594 – 1824231Alpha-type protein kinase
Nucleotide binding1794 – 18007ATP By similarity
Coiled coil1198 – 125053 By similarity

Sites

Active site17671Proton acceptor By similarity
Metal binding17531Zinc By similarity
Metal binding18101Zinc By similarity
Metal binding18121Zinc By similarity
Metal binding18161Zinc By similarity
Binding site16241ATP By similarity
Binding site16481ATP By similarity
Binding site17201ATP By similarity
Binding site17691ATP By similarity
Binding site17771ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue12241Phosphoserine By similarity
Modified residue13011Phosphoserine By similarity
Modified residue13861Phosphoserine By similarity
Modified residue13871Phosphoserine By similarity
Modified residue14051Phosphothreonine By similarity
Modified residue14671Phosphothreonine By similarity
Modified residue14771Phosphoserine Ref.9
Modified residue15001Phosphoserine By similarity
Modified residue15041Phosphoserine By similarity
Modified residue15691Phosphoserine By similarity
Modified residue18511Phosphoserine By similarity

Natural variations

Natural variant681G → V. Ref.14
Corresponds to variant rs56064201 [ dbSNP | Ensembl ].
VAR_042395
Natural variant4061S → C in an ovarian serous carcinoma sample; somatic mutation. Ref.14
VAR_042396
Natural variant4591I → T. Ref.14
Corresponds to variant rs55924090 [ dbSNP | Ensembl ].
VAR_042397
Natural variant5741K → N. Ref.14
Corresponds to variant rs56040619 [ dbSNP | Ensembl ].
VAR_042398
Natural variant7201T → S in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.14
VAR_042399
Natural variant8301M → V in a gastric adenocarcinoma sample; somatic mutation. Ref.14
VAR_042400
Natural variant9491F → Y. Ref.14
Corresponds to variant rs55681028 [ dbSNP | Ensembl ].
VAR_042401
Natural variant10331A → G.
Corresponds to variant rs34530969 [ dbSNP | Ensembl ].
VAR_052381
Natural variant10641Q → R. Ref.14
Corresponds to variant rs56298128 [ dbSNP | Ensembl ].
VAR_042402
Natural variant11451I → V.
Corresponds to variant rs34711809 [ dbSNP | Ensembl ].
VAR_052382
Natural variant12111I → T. Ref.14
Corresponds to variant rs56090496 [ dbSNP | Ensembl ].
VAR_042403
Natural variant12541A → V. Ref.14
Corresponds to variant rs56288221 [ dbSNP | Ensembl ].
VAR_042404
Natural variant13061D → E. Ref.14
Corresponds to variant rs55970334 [ dbSNP | Ensembl ].
VAR_042405
Natural variant14441R → K. Ref.14
Corresponds to variant rs55840070 [ dbSNP | Ensembl ].
VAR_042406
Natural variant14821T → I Mutant channels are functional but show increased susceptibility to inhibition by intracellular magnesium concentrations compared to wild-type channels. Ref.4 Ref.13 Ref.14
Corresponds to variant rs8042919 [ dbSNP | Ensembl ].
VAR_019967

Experimental info

Mutagenesis16481K → R: Loss of kinase activity. Ref.6
Mutagenesis17991G → D: Loss of kinase activity. Ref.6
Sequence conflict573 – 5753EKM → KKK in BAD18773. Ref.4
Sequence conflict9981A → S Ref.5
Sequence conflict14961Missing in AAK19738. Ref.3
Sequence conflict15201D → V in AAK19738. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q96QT4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: BE732674D52D7485

FASTA1,865212,697
        10         20         30         40         50         60 
MSQKSWIEST LTKRECVYII PSSKDPHRCL PGCQICQQLV RCFCGRLVKQ HACFTASLAM 

        70         80         90        100        110        120 
KYSDVKLGDH FNQAIEEWSV EKHTEQSPTD AYGVINFQGG SHSYRAKYVR LSYDTKPEVI 

       130        140        150        160        170        180 
LQLLLKEWQM ELPKLVISVH GGMQKFELHP RIKQLLGKGL IKAAVTTGAW ILTGGVNTGV 

       190        200        210        220        230        240 
AKHVGDALKE HASRSSRKIC TIGIAPWGVI ENRNDLVGRD VVAPYQTLLN PLSKLNVLNN 

       250        260        270        280        290        300 
LHSHFILVDD GTVGKYGAEV RLRRELEKTI NQQRIHARIG QGVPVVALIF EGGPNVILTV 

       310        320        330        340        350        360 
LEYLQESPPV PVVVCEGTGR AADLLAYIHK QTEEGGNLPD AAEPDIISTI KKTFNFGQNE 

       370        380        390        400        410        420 
ALHLFQTLME CMKRKELITV FHIGSDEHQD IDVAILTALL KGTNASAFDQ LILTLAWDRV 

       430        440        450        460        470        480 
DIAKNHVFVY GQQWLVGSLE QAMLDALVMD RVAFVKLLIE NGVSMHKFLT IPRLEELYNT 

       490        500        510        520        530        540 
KQGPTNPMLF HLVRDVKQGN LPPGYKITLI DIGLVIEYLM GGTYRCTYTR KRFRLIYNSL 

       550        560        570        580        590        600 
GGNNRRSGRN TSSSTPQLRK SHESFGNRAD KKEKMRHNHF IKTAQPYRPK IDTVMEEGKK 

       610        620        630        640        650        660 
KRTKDEIVDI DDPETKRFPY PLNELLIWAC LMKRQVMARF LWQHGEESMA KALVACKIYR 

       670        680        690        700        710        720 
SMAYEAKQSD LVDDTSEELK QYSNDFGQLA VELLEQSFRQ DETMAMKLLT YELKNWSNST 

       730        740        750        760        770        780 
CLKLAVSSRL RPFVAHTCTQ MLLSDMWMGR LNMRKNSWYK VILSILVPPA ILLLEYKTKA 

       790        800        810        820        830        840 
EMSHIPQSQD AHQMTMDDSE NNFQNITEEI PMEVFKEVRI LDSNEGKNEM EIQMKSKKLP 

       850        860        870        880        890        900 
ITRKFYAFYH APIVKFWFNT LAYLGFLMLY TFVVLVQMEQ LPSVQEWIVI AYIFTYAIEK 

       910        920        930        940        950        960 
VREIFMSEAG KVNQKIKVWF SDYFNISDTI AIISFFIGFG LRFGAKWNFA NAYDNHVFVA 

       970        980        990       1000       1010       1020 
GRLIYCLNII FWYVRLLDFL AVNQQAGPYV MMIGKMVANM FYIVVIMALV LLSFGVPRKA 

      1030       1040       1050       1060       1070       1080 
ILYPHEAPSW TLAKDIVFHP YWMIFGEVYA YEIDVCANDS VIPQICGPGT WLTPFLQAVY 

      1090       1100       1110       1120       1130       1140 
LFVQYIIMVN LLIAFFNNVY LQVKAISNIV WKYQRYHFIM AYHEKPVLPP PLIILSHIVS 

      1150       1160       1170       1180       1190       1200 
LFCCICKRRK KDKTSDGPKL FLTEEDQKKL HDFEEQCVEM YFNEKDDKFH SGSEERIRVT 

      1210       1220       1230       1240       1250       1260 
FERVEQMCIQ IKEVGDRVNY IKRSLQSLDS QIGHLQDLSA LTVDTLKTLT AQKASEASKV 

      1270       1280       1290       1300       1310       1320 
HNEITRELSI SKHLAQNLID DGPVRPSVWK KHGVVNTLSS SLPQGDLESN NPFHCNILMK 

      1330       1340       1350       1360       1370       1380 
DDKDPQCNIF GQDLPAVPQR KEFNFPEAGS SSGALFPSAV SPPELRQRLH GVELLKIFNK 

      1390       1400       1410       1420       1430       1440 
NQKLGSSSTS IPHLSSPPTK FFVSTPSQPS CKSHLETGTK DQETVCSKAT EGDNTEFGAF 

      1450       1460       1470       1480       1490       1500 
VGHRDSMDLQ RFKETSNKIK ILSNNNTSEN TLKRVSSLAG FTDCHRTSIP VHSKQAEKIS 

      1510       1520       1530       1540       1550       1560 
RRPSTEDTHE VDSKAALIPD WLQDRPSNRE MPSEEGTLNG LTSPFKPAMD TNYYYSAVER 

      1570       1580       1590       1600       1610       1620 
NNLMRLSQSI PFTPVPPRGE PVTVYRLEES SPNILNNSMS SWSQLGLCAK IEFLSKEEMG 

      1630       1640       1650       1660       1670       1680 
GGLRRAVKVQ CTWSEHDILK SGHLYIIKSF LPEVVNTWSS IYKEDTVLHL CLREIQQQRA 

      1690       1700       1710       1720       1730       1740 
AQKLTFAFNQ MKPKSIPYSP RFLEVFLLYC HSAGQWFAVE ECMTGEFRKY NNNNGDEIIP 

      1750       1760       1770       1780       1790       1800 
TNTLEEIMLA FSHWTYEYTR GELLVLDLQG VGENLTDPSV IKAEEKRSCD MVFGPANLGE 

      1810       1820       1830       1840       1850       1860 
DAIKNFRAKH HCNSCCRKLK LPDLKRNDYT PDKIIFPQDE PSDLNLQPGN STKESESTNS 


VRLML 

« Hide

References

« Hide 'large scale' references
[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.
[2]Erratum
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 412:660-660(2001)
[3]"Characterization of the protein kinase activity of TRPM7/ChaK1, a protein kinase fused to the transient receptor potential ion channel."
Ryazanova L.V., Dorovkov M.V., Ansari A., Ryazanov A.G.
J. Biol. Chem. 279:3708-3716(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[4]"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] OF 1-575 AND 1096-1865, VARIANT ILE-1482.
Tissue: Colon and Placenta.
[5]"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 464-998.
Tissue: Liver.
[6]"Regulation of vertebrate cellular Mg2+ homeostasis by TRPM7."
Schmitz C., Perraud A.-L., Johnson C.O., Inabe K., Smith M.K., Penner R., Kurosaki T., Fleig A., Scharenberg A.M.
Cell 114:191-200(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-1648 AND GLY-1799.
[7]"Phosphorylation of annexin I by TRPM7 channel-kinase."
Dorovkov M.V., Ryazanov A.G.
J. Biol. Chem. 279:50643-50646(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Disruption of TRPM6/TRPM7 complex formation by a mutation in the TRPM6 gene causes hypomagnesemia with secondary hypocalcemia."
Chubanov V., Waldegger S., Mederos y Schnitzler M., Vitzthum H., Sassen M.C., Seyberth H.W., Konrad M., Gudermann T.
Proc. Natl. Acad. Sci. U.S.A. 101:2894-2899(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRPM6.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis."
Cai Z., Jitkaew S., Zhao J., Chiang H.C., Choksi S., Liu J., Ward Y., Wu L.G., Liu Z.G.
Nat. Cell Biol. 16:55-65(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"A TRPM7 variant shows altered sensitivity to magnesium that may contribute to the pathogenesis of two Guamanian neurodegenerative disorders."
Hermosura M.C., Nayakanti H., Dorovkov M.V., Calderon F.R., Ryazanov A.G., Haymer D.S., Garruto R.M.
Proc. Natl. Acad. Sci. U.S.A. 102:11510-11515(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ILE-1482, CHARACTERIZATION OF VARIANT ILE-1482.
[14]"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] VAL-68; CYS-406; THR-459; ASN-574; SER-720; VAL-830; TYR-949; ARG-1064; THR-1211; VAL-1254; GLU-1306; LYS-1444 AND ILE-1482.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY032950 mRNA. Translation: AAK44211.1.
AF346629 mRNA. Translation: AAK19738.2.
AK000124 mRNA. Translation: BAA90958.1.
AK172800 mRNA. Translation: BAD18773.1. Different initiation.
AK075193 mRNA. Translation: BAC11462.1. Different initiation.
BC051024 mRNA. Translation: AAH51024.1.
CCDSCCDS42035.1.
RefSeqNP_060142.3. NM_017672.4.
UniGeneHs.512894.

3D structure databases

ProteinModelPortalQ96QT4.
SMRQ96QT4. Positions 1198-1249, 1551-1830.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120177. 9 interactions.
IntActQ96QT4. 3 interactions.
MINTMINT-2815126.
STRING9606.ENSP00000320239.

Chemistry

ChEMBLCHEMBL1250412.
GuidetoPHARMACOLOGY499.

Protein family/group databases

TCDB1.A.4.5.1. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteQ96QT4.

Polymorphism databases

DMDM56404941.

Proteomic databases

MaxQBQ96QT4.
PaxDbQ96QT4.
PRIDEQ96QT4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313478; ENSP00000320239; ENSG00000092439.
ENST00000560638; ENSP00000452873; ENSG00000092439.
GeneID54822.
KEGGhsa:54822.
UCSCuc001zyt.4. human.

Organism-specific databases

CTD54822.
GeneCardsGC15M050852.
HGNCHGNC:17994. TRPM7.
HPAHPA035523.
HPA052173.
MIM105500. phenotype.
605692. gene.
neXtProtNX_Q96QT4.
Orphanet90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
PharmGKBPA38273.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253824.
HOGENOMHOG000230920.
HOVERGENHBG055663.
InParanoidQ96QT4.
KOK04982.
OMAKQGPTNP.
PhylomeDBQ96QT4.
TreeFamTF314204.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ96QT4.
BgeeQ96QT4.
CleanExHS_TRPM7.
GenevestigatorQ96QT4.

Family and domain databases

InterProIPR005821. Ion_trans_dom.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
[Graphical view]
PfamPF02816. Alpha_kinase. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
SMARTSM00811. Alpha_kinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51158. ALPHA_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRPM7. human.
GeneWikiTRPM7.
GenomeRNAi54822.
NextBio57577.
PROQ96QT4.
SOURCESearch...

Entry information

Entry nameTRPM7_HUMAN
AccessionPrimary (citable) accession number: Q96QT4
Secondary accession number(s): Q6ZMF5 expand/collapse secondary AC list , Q86VJ4, Q8NBW2, Q9BXB2, Q9NXQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 115 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

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

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