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Protein

Glutamate receptor ionotropic, NMDA 1

Gene

Grin1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg2+ (PubMed:1350383, PubMed:1834949, PubMed:1388270, PubMed:8428958, PubMed:18177891, PubMed:28384476, PubMed:15996549, PubMed:24876489, PubMed:27135925, PubMed:27618671, PubMed:28468946). Sensitivity to glutamate and channel kinetics depend on the subunit composition (PubMed:28384476).11 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei523GlycineCombined sources2 Publications1
Binding sitei688GlycineCombined sources2 Publications1
Binding sitei732GlycineCombined sources2 Publications1

GO - Molecular functioni

  • enzyme binding Source: RGD
  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • glutamate binding Source: UniProtKB
  • glutamate receptor binding Source: RGD
  • glycine binding Source: UniProtKB
  • ionotropic glutamate receptor activity Source: RGD
  • neurotransmitter binding Source: RGD
  • NMDA glutamate receptor activity Source: UniProtKB
  • phosphatase binding Source: RGD
  • protein complex binding Source: ARUK-UCL
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • receptor binding Source: RGD
  • voltage-gated cation channel activity Source: RGD

GO - Biological processi

  • cellular response to manganese ion Source: RGD
  • ionotropic glutamate receptor signaling pathway Source: RGD
  • learning or memory Source: RGD
  • positive regulation of calcium ion transport into cytosol Source: ARUK-UCL
  • positive regulation of cell death Source: RGD
  • positive regulation of dendritic spine maintenance Source: ARUK-UCL
  • positive regulation of excitatory postsynaptic potential Source: BHF-UCL
  • positive regulation of reactive oxygen species biosynthetic process Source: ARUK-UCL
  • protein heterotetramerization Source: UniProtKB
  • protein tetramerization Source: RGD
  • response to amine Source: RGD
  • response to calcium ion Source: RGD
  • response to fungicide Source: RGD
  • response to organic cyclic compound Source: RGD
  • rhythmic process Source: RGD

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport
LigandCalcium, Magnesium

Enzyme and pathway databases

ReactomeiR-RNO-3928662. EPHB-mediated forward signaling.
R-RNO-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-RNO-442729. CREB phosphorylation through the activation of CaMKII.
R-RNO-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-RNO-5673001. RAF/MAP kinase cascade.
R-RNO-8849932. Synaptic adhesion-like molecules.

Protein family/group databases

TCDBi1.A.10.1.6. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 1
Short name:
GluN1
Alternative name(s):
Glutamate [NMDA] receptor subunit zeta-1
N-methyl-D-aspartate receptor subunit NR11 Publication
Short name:
NMD-R1
Gene namesi
Name:Grin1
Synonyms:Nmdar11 Publication
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2736. Grin1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 559Extracellular1 PublicationAdd BLAST541
Transmembranei560 – 580Helical1 PublicationAdd BLAST21
Topological domaini581 – 602Cytoplasmic1 PublicationAdd BLAST22
Intramembranei603 – 624Discontinuously helicalBy similarityAdd BLAST22
Topological domaini625 – 630Cytoplasmic1 Publication6
Transmembranei631 – 647Helical1 PublicationAdd BLAST17
Topological domaini648 – 812Extracellular1 PublicationAdd BLAST165
Transmembranei813 – 833Helical1 PublicationAdd BLAST21
Topological domaini834 – 938Cytoplasmic1 PublicationAdd BLAST105

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL330.
GuidetoPHARMACOLOGYi455.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000001158919 – 938Glutamate receptor ionotropic, NMDA 1Add BLAST920

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi61N-linked (GlcNAc...) asparagineCombined sources1
Disulfide bondi79 ↔ 308Combined sources
Glycosylationi203N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi239N-linked (GlcNAc...) asparagineCombined sources1
Glycosylationi276N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi300N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi350N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi368N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi420 ↔ 454Combined sources
Disulfide bondi436 ↔ 455Combined sources
Glycosylationi440N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi471N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi491N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi744 ↔ 798Combined sources
Modified residuei889Phosphoserine; by PKCBy similarity1
Modified residuei890Phosphoserine; by PKC1 Publication1
Modified residuei896Phosphoserine; by PKCBy similarity1
Modified residuei897Phosphoserine; by PKC1 Publication1
Isoform E (identifier: P35439-5)
Modified residuei877PhosphoserineCombined sources1
Isoform G (identifier: P35439-7)
Modified residuei898PhosphoserineCombined sources1

Post-translational modificationi

NMDA is probably regulated by C-terminal phosphorylation of an isoform of NR1 by PKC. Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB). Its phosphorylated state is influenced by the formation of the NMDAR-PPP2CB complex and the NMDAR channel activity.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP35439.
PRIDEiP35439.

PTM databases

iPTMnetiP35439.
PhosphoSitePlusiP35439.
UniCarbKBiP35439.

Expressioni

Tissue specificityi

Detected throughout the brain, in brain cortex, cerebellum, thalamus and olfactory bulb.1 Publication

Gene expression databases

BgeeiENSRNOG00000011726.
ExpressionAtlasiP35439. baseline and differential.
GenevisibleiP35439. RN.

Interactioni

Subunit structurei

Heterotetramer. Forms heterotetrameric channels composed of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:18177891, PubMed:28384476, PubMed:16281028, PubMed:15996549, PubMed:21389213, PubMed:24876489, PubMed:27135925, PubMed:28468946, Ref. 31). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), an epsilon subunit, plus GRIN3A or GRIN3B (in vitro) (PubMed:11160393, PubMed:11929923, PubMed:12391275). In vivo, the subunit composition may vary in function of the expression levels of the different subunits (Probable). Found in a complex with GRIN2A or GRIN2B, GRIN3A and PPP2CB (PubMed:11588171). Found in a complex with GRIN2A or GRIN2B and GRIN3B (By similarity). Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (By similarity). Interacts with DLG4 and MPDZ (PubMed:15312654). Interacts with LRFN1 and LRFN2 (PubMed:16495444, PubMed:16630835). Interacts with MYZAP (PubMed:18849881). Found in a complex with DLG4 and PRR7 (PubMed:27458189). Found in a complex with GRIN2B and PRR7 (PubMed:27458189). Interacts with PRR7; the interaction is reduced following NMDA receptor activity (PubMed:27458189).By similarityCurated21 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: RGD
  • glutamate receptor binding Source: RGD
  • phosphatase binding Source: RGD
  • protein complex binding Source: ARUK-UCL
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • receptor binding Source: RGD

Protein-protein interaction databases

BioGridi246573. 7 interactors.
CORUMiP35439.
DIPiDIP-674N.
IntActiP35439. 17 interactors.
MINTiMINT-101336.
STRINGi10116.ENSRNOP00000029227.

Chemistry databases

BindingDBiP35439.

Structurei

Secondary structure

1938
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 35Combined sources10
Helixi36 – 50Combined sources15
Beta strandi59 – 66Combined sources8
Helixi71 – 80Combined sources10
Helixi83 – 85Combined sources3
Beta strandi87 – 92Combined sources6
Turni98 – 103Combined sources6
Helixi104 – 112Combined sources9
Turni113 – 115Combined sources3
Beta strandi118 – 122Combined sources5
Helixi126 – 129Combined sources4
Turni131 – 133Combined sources3
Beta strandi137 – 141Combined sources5
Helixi144 – 146Combined sources3
Helixi147 – 156Combined sources10
Helixi157 – 159Combined sources3
Beta strandi163 – 170Combined sources8
Helixi171 – 185Combined sources15
Turni186 – 188Combined sources3
Beta strandi192 – 197Combined sources6
Helixi205 – 212Combined sources8
Beta strandi218 – 222Combined sources5
Helixi225 – 237Combined sources13
Beta strandi246 – 248Combined sources3
Turni251 – 254Combined sources4
Turni256 – 260Combined sources5
Beta strandi267 – 271Combined sources5
Helixi277 – 296Combined sources20
Beta strandi298 – 300Combined sources3
Helixi317 – 326Combined sources10
Beta strandi334 – 336Combined sources3
Beta strandi338 – 340Combined sources3
Beta strandi342 – 344Combined sources3
Beta strandi351 – 357Combined sources7
Beta strandi360 – 363Combined sources4
Beta strandi365 – 367Combined sources3
Beta strandi372 – 374Combined sources3
Beta strandi398 – 402Combined sources5
Turni406 – 408Combined sources3
Beta strandi409 – 413Combined sources5
Turni416 – 418Combined sources3
Beta strandi426 – 428Combined sources3
Beta strandi434 – 439Combined sources6
Beta strandi450 – 457Combined sources8
Helixi458 – 470Combined sources13
Beta strandi474 – 478Combined sources5
Beta strandi487 – 489Combined sources3
Beta strandi491 – 494Combined sources4
Beta strandi496 – 498Combined sources3
Helixi500 – 506Combined sources7
Beta strandi511 – 513Combined sources3
Helixi521 – 524Combined sources4
Beta strandi527 – 529Combined sources3
Beta strandi533 – 543Combined sources11
Beta strandi666 – 668Combined sources3
Helixi670 – 673Combined sources4
Beta strandi677 – 679Combined sources3
Beta strandi684 – 687Combined sources4
Helixi688 – 694Combined sources7
Helixi697 – 699Combined sources3
Helixi700 – 706Combined sources7
Turni707 – 709Combined sources3
Beta strandi711 – 713Combined sources3
Helixi714 – 722Combined sources9
Beta strandi727 – 732Combined sources6
Helixi733 – 742Combined sources10
Beta strandi746 – 748Combined sources3
Beta strandi753 – 758Combined sources6
Beta strandi761 – 763Combined sources3
Helixi769 – 781Combined sources13
Helixi784 – 792Combined sources9
Beta strandi794 – 796Combined sources3
Helixi805 – 813Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PB7X-ray1.35A394-544[»]
A663-800[»]
1PB8X-ray1.45A394-544[»]
A663-800[»]
1PB9X-ray1.60A394-544[»]
A663-800[»]
1PBQX-ray1.90A/B394-544[»]
A/B663-800[»]
1Y1MX-ray1.80A/B394-544[»]
A/B663-800[»]
1Y1ZX-ray1.50A394-544[»]
A663-800[»]
1Y20X-ray1.40A394-544[»]
A663-800[»]
2A5TX-ray2.00A394-544[»]
3Q41X-ray3.40A/B/C21-393[»]
4KCCX-ray1.89A394-544[»]
A663-800[»]
4KFQX-ray2.20A/B394-544[»]
A/B663-800[»]
4NF4X-ray2.00A394-544[»]
A663-800[»]
4NF5X-ray1.90A394-544[»]
A663-800[»]
4NF6X-ray2.10A394-544[»]
A663-800[»]
4NF8X-ray1.86A394-544[»]
A663-800[»]
4PE5X-ray3.96A/C23-847[»]
5DEXX-ray2.40A394-544[»]
A663-800[»]
5FXGelectron microscopy6.80A/C23-863[»]
5FXHelectron microscopy6.10A/C23-863[»]
5FXIelectron microscopy6.40A/C23-863[»]
5FXJelectron microscopy6.50A/C23-863[»]
5FXKelectron microscopy6.40A/C23-863[»]
5I56X-ray2.28A394-544[»]
A663-800[»]
5I57X-ray1.70A394-544[»]
A684-821[»]
5I58X-ray2.52A394-544[»]
A663-800[»]
5I59X-ray2.25A394-544[»]
A663-800[»]
5JTYX-ray2.72A394-544[»]
A684-821[»]
5U8CX-ray1.60A394-544[»]
A663-800[»]
5VIHX-ray2.40A394-544[»]
A663-800[»]
5VIIX-ray1.95A394-544[»]
A663-800[»]
5VIJX-ray2.10A394-544[»]
A663-800[»]
ProteinModelPortaliP35439.
SMRiP35439.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35439.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni516 – 518Glycine bindingCombined sources1 Publication3
Regioni603 – 624Pore-formingBy similarityAdd BLAST22

Domaini

A hydrophobic region that gives rise to the prediction of a transmembrane span does not cross the membrane, but is part of a discontinuously helical region that dips into the membrane and is probably part of the pore and of the selectivity filter.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000231491.
HOVERGENiHBG052638.
InParanoidiP35439.
KOiK05208.
OrthoDBiEOG091G0M5H.
PhylomeDBiP35439.
TreeFamiTF351405.

Family and domain databases

InterProiView protein in InterPro
IPR001828. ANF_lig-bd_rcpt.
IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
PfamiView protein in Pfam
PF01094. ANF_receptor. 1 hit.
PF10562. CaM_bdg_C0. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PRINTSiPR00177. NMDARECEPTOR.
SMARTiView protein in SMART
SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequences (7)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P35439-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN
60 70 80 90 100
KRHGSWKIQL NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND
110 120 130 140 150
HFTPTPVSYT AGFYRIPVLG LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV
160 170 180 190 200
WFEMMRVYNW NHIILLVSDD HEGRAAQKRL ETLLEERESK AEKVLQFDPG
210 220 230 240 250
TKNVTALLME ARELEARVII LSASEDDAAT VYRAAAMLNM TGSGYVWLVG
260 270 280 290 300
EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN
310 320 330 340 350
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN
360 370 380 390 400
YSIMNLQNRK LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI
410 420 430 440 450
VTIHQEPFVY VKPTMSDGTC KEEFTVNGDP VKKVICTGPN DTSPGSPRHT
460 470 480 490 500
VPQCCYGFCI DLLIKLARTM NFTYEVHLVA DGKFGTQERV NNSNKKEWNG
510 520 530 540 550
MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI LVKKEIPRST
560 570 580 590 600
LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA
610 620 630 640 650
LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN
660 670 680 690 700
LAAFLVLDRP EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS
710 720 730 740 750
TMYRHMEKHN YESAAEAIQA VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG
760 770 780 790 800
ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH ENGFMEDLDK TWVRYQECDS
810 820 830 840 850
RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH KDARRKQMQL
860 870 880 890 900
AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT
910 920 930
STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES
Length:938
Mass (Da):105,509
Last modified:June 1, 1994 - v1
Checksum:i613D36E38F05BC73
GO
Isoform B (identifier: P35439-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK

Show »
Length:959
Mass (Da):108,045
Checksum:iD965531F6C38EDDD
GO
Isoform C (identifier: P35439-3) [UniParc]FASTAAdd to basket
Also known as: NMDAR1-2a subunit

The sequence of this isoform differs from the canonical sequence as follows:
     864-900: Missing.

Show »
Length:901
Mass (Da):101,345
Checksum:iA320F3585664F652
GO
Isoform D (identifier: P35439-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     901-938: STGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES → QYHPTDITGPLNLSDPSVSTVV

Show »
Length:922
Mass (Da):103,615
Checksum:iE31E00296E49D08D
GO
Isoform E (identifier: P35439-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     864-885: DRKSGRAEPDPKKKATFRAITS → QYHPTDITGPLNLSDPSVSTVV
     886-938: Missing.

Show »
Length:885
Mass (Da):99,451
Checksum:i6DAA83EFC08C30D8
GO
Isoform F (identifier: P35439-6) [UniParc]FASTAAdd to basket
Also known as: NMDAR1-2b subunit

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
     864-900: Missing.

Show »
Length:922
Mass (Da):103,881
Checksum:i847CEED410182B5C
GO
Isoform G (identifier: P35439-7) [UniParc]FASTAAdd to basket
Also known as: NMDAR1-4b subunit

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
     864-885: DRKSGRAEPDPKKKATFRAITS → QYHPTDITGPLNLSDPSVSTVV
     886-938: Missing.

Show »
Length:906
Mass (Da):101,987
Checksum:i1872055038F790FF
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000140190K → KSKKRNYENLDQLSYDNKRG PK in isoform B, isoform F and isoform G. Curated1
Alternative sequenceiVSP_000141864 – 900Missing in isoform F and isoform C. CuratedAdd BLAST37
Alternative sequenceiVSP_000142864 – 885DRKSG…RAITS → QYHPTDITGPLNLSDPSVST VV in isoform E and isoform G. CuratedAdd BLAST22
Alternative sequenceiVSP_000143886 – 938Missing in isoform E and isoform G. CuratedAdd BLAST53
Alternative sequenceiVSP_000144901 – 938STGGG…RHRES → QYHPTDITGPLNLSDPSVST VV in isoform D. CuratedAdd BLAST38

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63255 mRNA. Translation: CAA44914.1.
AY157515 Genomic DNA. Translation: AAA16366.1.
X65227 mRNA. Translation: CAA46335.1.
U08261 mRNA. Translation: AAB50926.1.
U08262 mRNA. Translation: AAB50927.1.
U08263 mRNA. Translation: AAB50928.1.
U08264 mRNA. Translation: AAB50929.1.
U08265 mRNA. Translation: AAB50930.1.
U08267 mRNA. Translation: AAB50932.1.
U08268 mRNA. Translation: AAB50933.1.
S39217 mRNA. Translation: AAB22431.1.
S39218 mRNA. Translation: AAB22432.1.
S39219 mRNA. Translation: AAB22433.1.
S39220 mRNA. Translation: AAB22434.1.
S39221 mRNA. Translation: AAB22435.1.
PIRiJN0336.
JN0337.
JN0338.
JN0339.
JN0340.
JN0341.
JN0342.
S19710.
RefSeqiNP_001257531.1. NM_001270602.1. [P35439-2]
NP_001257532.1. NM_001270603.1. [P35439-6]
NP_001257534.1. NM_001270605.1. [P35439-3]
NP_001257537.1. NM_001270608.1. [P35439-7]
NP_001257539.1. NM_001270610.1. [P35439-5]
NP_001274352.1. NM_001287423.1. [P35439-4]
NP_058706.1. NM_017010.2. [P35439-1]
UniGeneiRn.9840.

Genome annotation databases

EnsembliENSRNOT00000044246; ENSRNOP00000043301; ENSRNOG00000011726. [P35439-6]
ENSRNOT00000049297; ENSRNOP00000049198; ENSRNOG00000011726. [P35439-1]
GeneIDi24408.
KEGGirno:24408.
UCSCiRGD:2736. rat. [P35439-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiNMDZ1_RAT
AccessioniPrimary (citable) accession number: P35439
Secondary accession number(s): Q62646
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 25, 2017
This is version 198 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families