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Q96QT4

- TRPM7_HUMAN

UniProt

Q96QT4 - TRPM7_HUMAN

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Protein

Transient receptor potential cation channel subfamily M member 7

Gene

TRPM7

Organism
Homo sapiens (Human)
Status
Reviewed - 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).3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1624 – 16241ATPBy similarity
Binding sitei1648 – 16481ATPBy similarity
Binding sitei1720 – 17201ATPBy similarity
Metal bindingi1753 – 17531ZincBy similarity
Active sitei1767 – 17671Proton acceptorBy similarity
Binding sitei1769 – 17691ATPBy similarity
Binding sitei1777 – 17771ATPBy similarity
Metal bindingi1810 – 18101ZincBy similarity
Metal bindingi1812 – 18121ZincBy similarity
Metal bindingi1816 – 18161ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1794 – 18007ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium channel activity Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. actomyosin structure organization Source: Ensembl
  2. calcium-dependent cell-matrix adhesion Source: Ensembl
  3. calcium ion transmembrane transport Source: Reactome
  4. cellular magnesium ion homeostasis Source: InterPro
  5. ion transmembrane transport Source: Reactome
  6. necroptotic process Source: UniProtKB
  7. protein autophosphorylation Source: Ensembl
  8. transmembrane transport Source: Reactome
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

ReactomeiREACT_169333. TRP channels.

Protein family/group databases

TCDBi1.A.4.5.1. the transient receptor potential ca(2+) channel (trp-cc) family.

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
Gene namesi
Name:TRPM7
Synonyms:CHAK1, LTRPC7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:17994. 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 – 1865770CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: Reactome
  3. ruffle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1648 – 16481K → R: Loss of kinase activity. 1 Publication
Mutagenesisi1799 – 17991G → D: Loss of kinase activity. 1 Publication

Keywords - Diseasei

Amyotrophic lateral sclerosis, Neurodegeneration, Parkinsonism

Organism-specific databases

MIMi105500. phenotype.
Orphaneti90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
PharmGKBiPA38273.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18651865Transient receptor potential cation channel subfamily M member 7PRO_0000215331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei1224 – 12241PhosphoserineBy similarity
Modified residuei1301 – 13011PhosphoserineBy similarity
Modified residuei1386 – 13861PhosphoserineBy similarity
Modified residuei1387 – 13871PhosphoserineBy similarity
Modified residuei1405 – 14051PhosphothreonineBy similarity
Modified residuei1467 – 14671PhosphothreonineBy similarity
Modified residuei1477 – 14771Phosphoserine1 Publication
Modified residuei1500 – 15001PhosphoserineBy similarity
Modified residuei1504 – 15041PhosphoserineBy similarity
Modified residuei1569 – 15691PhosphoserineBy similarity
Modified residuei1851 – 18511PhosphoserineBy similarity

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96QT4.
PaxDbiQ96QT4.
PRIDEiQ96QT4.

PTM databases

PhosphoSiteiQ96QT4.

Expressioni

Gene expression databases

BgeeiQ96QT4.
CleanExiHS_TRPM7.
ExpressionAtlasiQ96QT4. baseline and differential.
GenevestigatoriQ96QT4.

Organism-specific databases

HPAiHPA035523.
HPA052173.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi120177. 11 interactions.
IntActiQ96QT4. 3 interactions.
MINTiMINT-2815126.
STRINGi9606.ENSP00000320239.

Structurei

3D structure databases

ProteinModelPortaliQ96QT4.
SMRiQ96QT4. Positions 1198-1249, 1551-1830.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1594 – 1824231Alpha-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

eggNOGiNOG253824.
GeneTreeiENSGT00760000119127.
HOGENOMiHOG000230920.
HOVERGENiHBG055663.
InParanoidiQ96QT4.
KOiK04982.
OMAiKQGPTNP.
PhylomeDBiQ96QT4.
TreeFamiTF314204.

Family and domain databases

InterProiIPR005821. Ion_trans_dom.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
IPR029601. TRPM7.
[Graphical view]
PANTHERiPTHR13800:SF8. PTHR13800:SF8. 1 hit.
PfamiPF02816. Alpha_kinase. 1 hit.
PF00520. Ion_trans. 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.

Q96QT4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQKSWIEST LTKRECVYII PSSKDPHRCL PGCQICQQLV RCFCGRLVKQ
60 70 80 90 100
HACFTASLAM KYSDVKLGDH FNQAIEEWSV EKHTEQSPTD AYGVINFQGG
110 120 130 140 150
SHSYRAKYVR LSYDTKPEVI 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
KKTFNFGQNE ALHLFQTLME CMKRKELITV FHIGSDEHQD IDVAILTALL
410 420 430 440 450
KGTNASAFDQ LILTLAWDRV DIAKNHVFVY GQQWLVGSLE QAMLDALVMD
460 470 480 490 500
RVAFVKLLIE NGVSMHKFLT IPRLEELYNT KQGPTNPMLF HLVRDVKQGN
510 520 530 540 550
LPPGYKITLI DIGLVIEYLM GGTYRCTYTR KRFRLIYNSL GGNNRRSGRN
560 570 580 590 600
TSSSTPQLRK SHESFGNRAD KKEKMRHNHF IKTAQPYRPK IDTVMEEGKK
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 ILLLEYKTKA EMSHIPQSQD AHQMTMDDSE
810 820 830 840 850
NNFQNITEEI PMEVFKEVRI LDSNEGKNEM EIQMKSKKLP ITRKFYAFYH
860 870 880 890 900
APIVKFWFNT LAYLGFLMLY TFVVLVQMEQ LPSVQEWIVI AYIFTYAIEK
910 920 930 940 950
VREIFMSEAG KVNQKIKVWF SDYFNISDTI AIISFFIGFG LRFGAKWNFA
960 970 980 990 1000
NAYDNHVFVA GRLIYCLNII FWYVRLLDFL AVNQQAGPYV MMIGKMVANM
1010 1020 1030 1040 1050
FYIVVIMALV LLSFGVPRKA ILYPHEAPSW TLAKDIVFHP YWMIFGEVYA
1060 1070 1080 1090 1100
YEIDVCANDS VIPQICGPGT WLTPFLQAVY LFVQYIIMVN LLIAFFNNVY
1110 1120 1130 1140 1150
LQVKAISNIV WKYQRYHFIM AYHEKPVLPP PLIILSHIVS LFCCICKRRK
1160 1170 1180 1190 1200
KDKTSDGPKL FLTEEDQKKL HDFEEQCVEM YFNEKDDKFH SGSEERIRVT
1210 1220 1230 1240 1250
FERVEQMCIQ IKEVGDRVNY IKRSLQSLDS QIGHLQDLSA LTVDTLKTLT
1260 1270 1280 1290 1300
AQKASEASKV HNEITRELSI SKHLAQNLID DGPVRPSVWK KHGVVNTLSS
1310 1320 1330 1340 1350
SLPQGDLESN NPFHCNILMK DDKDPQCNIF GQDLPAVPQR KEFNFPEAGS
1360 1370 1380 1390 1400
SSGALFPSAV SPPELRQRLH GVELLKIFNK NQKLGSSSTS IPHLSSPPTK
1410 1420 1430 1440 1450
FFVSTPSQPS CKSHLETGTK DQETVCSKAT EGDNTEFGAF VGHRDSMDLQ
1460 1470 1480 1490 1500
RFKETSNKIK ILSNNNTSEN TLKRVSSLAG FTDCHRTSIP VHSKQAEKIS
1510 1520 1530 1540 1550
RRPSTEDTHE VDSKAALIPD WLQDRPSNRE MPSEEGTLNG LTSPFKPAMD
1560 1570 1580 1590 1600
TNYYYSAVER NNLMRLSQSI PFTPVPPRGE PVTVYRLEES SPNILNNSMS
1610 1620 1630 1640 1650
SWSQLGLCAK IEFLSKEEMG GGLRRAVKVQ CTWSEHDILK SGHLYIIKSF
1660 1670 1680 1690 1700
LPEVVNTWSS IYKEDTVLHL CLREIQQQRA AQKLTFAFNQ MKPKSIPYSP
1710 1720 1730 1740 1750
RFLEVFLLYC HSAGQWFAVE ECMTGEFRKY NNNNGDEIIP TNTLEEIMLA
1760 1770 1780 1790 1800
FSHWTYEYTR GELLVLDLQG VGENLTDPSV IKAEEKRSCD MVFGPANLGE
1810 1820 1830 1840 1850
DAIKNFRAKH HCNSCCRKLK LPDLKRNDYT PDKIIFPQDE PSDLNLQPGN
1860
STKESESTNS VRLML
Length:1,865
Mass (Da):212,697
Last modified:December 1, 2001 - v1
Checksum:iBE732674D52D7485
GO

Sequence cautioni

The sequence BAC11462.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD18773.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti573 – 5753EKM → KKK in BAD18773. (PubMed:14702039)Curated
Sequence conflicti998 – 9981A → S(PubMed:15489334)Curated
Sequence conflicti1496 – 14961Missing in AAK19738. (PubMed:14594813)Curated
Sequence conflicti1520 – 15201D → V in AAK19738. (PubMed:14594813)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681G → V.1 Publication
Corresponds to variant rs56064201 [ dbSNP | Ensembl ].
VAR_042395
Natural varianti406 – 4061S → C in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
VAR_042396
Natural varianti459 – 4591I → T.1 Publication
Corresponds to variant rs55924090 [ dbSNP | Ensembl ].
VAR_042397
Natural varianti574 – 5741K → N.1 Publication
Corresponds to variant rs56040619 [ dbSNP | Ensembl ].
VAR_042398
Natural varianti720 – 7201T → S in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
VAR_042399
Natural varianti830 – 8301M → V in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042400
Natural varianti949 – 9491F → Y.1 Publication
Corresponds to variant rs55681028 [ dbSNP | Ensembl ].
VAR_042401
Natural varianti1033 – 10331A → G.
Corresponds to variant rs34530969 [ dbSNP | Ensembl ].
VAR_052381
Natural varianti1064 – 10641Q → R.1 Publication
Corresponds to variant rs56298128 [ dbSNP | Ensembl ].
VAR_042402
Natural varianti1145 – 11451I → V.
Corresponds to variant rs34711809 [ dbSNP | Ensembl ].
VAR_052382
Natural varianti1211 – 12111I → T.1 Publication
Corresponds to variant rs56090496 [ dbSNP | Ensembl ].
VAR_042403
Natural varianti1254 – 12541A → V.1 Publication
Corresponds to variant rs56288221 [ dbSNP | Ensembl ].
VAR_042404
Natural varianti1306 – 13061D → E.1 Publication
Corresponds to variant rs55970334 [ dbSNP | Ensembl ].
VAR_042405
Natural varianti1444 – 14441R → K.1 Publication
Corresponds to variant rs55840070 [ dbSNP | Ensembl ].
VAR_042406
Natural varianti1482 – 14821T → I Mutant channels are functional but show increased susceptibility to inhibition by intracellular magnesium concentrations compared to wild-type channels. 3 Publications
Corresponds to variant rs8042919 [ dbSNP | Ensembl ].
VAR_019967

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS42035.1.
RefSeqiNP_001288141.1. NM_001301212.1.
NP_060142.3. NM_017672.5.
UniGeneiHs.512894.

Genome annotation databases

EnsembliENST00000313478; ENSP00000320239; ENSG00000092439.
ENST00000560638; ENSP00000452873; ENSG00000092439.
GeneIDi54822.
KEGGihsa:54822.
UCSCiuc001zyt.4. human.

Polymorphism databases

DMDMi56404941.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS42035.1.
RefSeqi NP_001288141.1. NM_001301212.1.
NP_060142.3. NM_017672.5.
UniGenei Hs.512894.

3D structure databases

ProteinModelPortali Q96QT4.
SMRi Q96QT4. Positions 1198-1249, 1551-1830.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120177. 11 interactions.
IntActi Q96QT4. 3 interactions.
MINTi MINT-2815126.
STRINGi 9606.ENSP00000320239.

Chemistry

ChEMBLi CHEMBL1250412.
GuidetoPHARMACOLOGYi 499.

Protein family/group databases

TCDBi 1.A.4.5.1. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSitei Q96QT4.

Polymorphism databases

DMDMi 56404941.

Proteomic databases

MaxQBi Q96QT4.
PaxDbi Q96QT4.
PRIDEi Q96QT4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313478 ; ENSP00000320239 ; ENSG00000092439 .
ENST00000560638 ; ENSP00000452873 ; ENSG00000092439 .
GeneIDi 54822.
KEGGi hsa:54822.
UCSCi uc001zyt.4. human.

Organism-specific databases

CTDi 54822.
GeneCardsi GC15M050852.
HGNCi HGNC:17994. TRPM7.
HPAi HPA035523.
HPA052173.
MIMi 105500. phenotype.
605692. gene.
neXtProti NX_Q96QT4.
Orphaneti 90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
PharmGKBi PA38273.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG253824.
GeneTreei ENSGT00760000119127.
HOGENOMi HOG000230920.
HOVERGENi HBG055663.
InParanoidi Q96QT4.
KOi K04982.
OMAi KQGPTNP.
PhylomeDBi Q96QT4.
TreeFami TF314204.

Enzyme and pathway databases

Reactomei REACT_169333. TRP channels.

Miscellaneous databases

ChiTaRSi TRPM7. human.
GeneWikii TRPM7.
GenomeRNAii 54822.
NextBioi 57577.
PROi Q96QT4.
SOURCEi Search...

Gene expression databases

Bgeei Q96QT4.
CleanExi HS_TRPM7.
ExpressionAtlasi Q96QT4. baseline and differential.
Genevestigatori Q96QT4.

Family and domain databases

InterProi IPR005821. Ion_trans_dom.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
IPR029601. TRPM7.
[Graphical view ]
PANTHERi PTHR13800:SF8. PTHR13800:SF8. 1 hit.
Pfami PF02816. Alpha_kinase. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view ]
SMARTi SM00811. Alpha_kinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51158. ALPHA_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.
  2. "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.
  3. "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.
    , 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.
  4. "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.
  5. Cited for: FUNCTION, MUTAGENESIS OF LYS-1648 AND GLY-1799.
  6. "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.
  7. "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.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "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.
  11. "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.
  12. "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.
  13. "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.
    , 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.

Entry informationi

Entry nameiTRPM7_HUMAN
AccessioniPrimary (citable) accession number: Q96QT4
Secondary accession number(s): Q6ZMF5
, Q86VJ4, Q8NBW2, Q9BXB2, Q9NXQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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