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Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

Grin2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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:19910922, PubMed:21677647, PubMed:24876489, PubMed:27135925, PubMed:27916457). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable). In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death. Contributes to neural pattern formation in the developing brain. Plays a role in long-term depression (LTD) of hippocampus membrane currents and in synaptic plasticity (By similarity).By similarityCurated6 Publications

Enzyme regulationi

Channel activity is inhibited by micromolar levels of zinc ions (PubMed:19910922). Channel activity is inhibited by ifenprodil (PubMed:19910922, PubMed:21677647).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi127ZincCombined sources1 Publication1
Metal bindingi284ZincCombined sources1 Publication1
Binding sitei514GlutamateCombined sources1 Publication1
Binding sitei519GlutamateCombined sources1 Publication1
Sitei615Functional determinant of NMDA receptorsBy similarity1
Binding sitei732GlutamateCombined sources1 Publication1

GO - Molecular functioni

  • beta-catenin binding Source: RGD
  • calcium channel activity Source: RGD
  • cation channel activity Source: RGD
  • cell adhesion molecule binding Source: RGD
  • D2 dopamine receptor binding Source: RGD
  • drug binding Source: RGD
  • extracellularly glutamate-gated ion channel activity Source: RGD
  • glutamate binding Source: UniProtKB
  • glutamate-gated calcium ion channel activity Source: UniProtKB
  • glycine binding Source: RGD
  • interleukin-1 receptor binding Source: RGD
  • ionotropic glutamate receptor activity Source: RGD
  • ionotropic glutamate receptor binding Source: RGD
  • neurotransmitter binding Source: RGD
  • neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration Source: SynGO
  • neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential Source: RGD
  • NMDA glutamate receptor activity Source: UniProtKB
  • protein heterodimerization activity Source: RGD
  • receptor binding Source: RGD
  • scaffold protein binding Source: RGD
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • action potential Source: RGD
  • associative learning Source: RGD
  • behavioral fear response Source: RGD
  • behavioral response to pain Source: RGD
  • calcium ion transmembrane import into cytosol Source: UniProtKB
  • calcium ion transport Source: RGD
  • cation transport Source: RGD
  • cellular response to amino acid stimulus Source: RGD
  • cellular response to corticosterone stimulus Source: RGD
  • cellular response to curcumin Source: RGD
  • cellular response to dsRNA Source: RGD
  • cellular response to forskolin Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to lipid Source: RGD
  • cellular response to magnesium starvation Source: RGD
  • cellular response to manganese ion Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • cerebral cortex development Source: RGD
  • chemical synaptic transmission Source: RGD
  • detection of mechanical stimulus involved in sensory perception of pain Source: RGD
  • excitatory postsynaptic potential Source: RGD
  • fear response Source: RGD
  • hippocampus development Source: RGD
  • in utero embryonic development Source: RGD
  • ionotropic glutamate receptor signaling pathway Source: RGD
  • learning Source: RGD
  • learning or memory Source: ARUK-UCL
  • long-term memory Source: RGD
  • long-term synaptic potentiation Source: RGD
  • memory Source: UniProtKB
  • multicellular organismal response to stress Source: RGD
  • negative regulation of dendritic spine maintenance Source: RGD
  • NMDA selective glutamate receptor signaling pathway Source: SynGO
  • positive regulation of cell death Source: RGD
  • positive regulation of cysteine-type endopeptidase activity Source: ARUK-UCL
  • positive regulation of glutamate secretion Source: UniProtKB
  • positive regulation of long-term synaptic potentiation Source: RGD
  • positive regulation of neuron death Source: RGD
  • positive regulation of synaptic transmission Source: RGD
  • protein heterotetramerization Source: UniProtKB
  • receptor clustering Source: RGD
  • regulation of long-term neuronal synaptic plasticity Source: RGD
  • regulation of MAPK cascade Source: UniProtKB
  • regulation of postsynaptic cytosolic calcium ion concentration Source: SynGO
  • regulation of postsynaptic membrane potential Source: RGD
  • regulation of protein kinase A signaling Source: RGD
  • regulation of synaptic plasticity Source: RGD
  • response to amine Source: RGD
  • response to amphetamine Source: RGD
  • response to calcium ion Source: RGD
  • response to carbohydrate Source: RGD
  • response to cocaine Source: RGD
  • response to cytokine Source: RGD
  • response to electrical stimulus Source: RGD
  • response to ethanol Source: RGD
  • response to fungicide Source: RGD
  • response to growth hormone Source: RGD
  • response to hypoxia Source: RGD
  • response to magnesium ion Source: RGD
  • response to manganese ion Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to methylmercury Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organonitrogen compound Source: RGD
  • response to other organism Source: RGD
  • response to toxic substance Source: RGD
  • rhythmic process Source: RGD
  • sensitization Source: RGD
  • sensory organ development Source: RGD
  • startle response Source: RGD
  • suckling behavior Source: RGD

Keywordsi

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

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 2B
Short name:
GluN2B
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-2
N-methyl D-aspartate receptor subtype 2B
Short name:
NMDAR2B
Short name:
NR2B1 Publication
Gene namesi
Name:Grin2b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2738. Grin2b.

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 domaini27 – 557Extracellular1 PublicationAdd BLAST531
Transmembranei558 – 576Helical1 PublicationAdd BLAST19
Topological domaini577 – 603Cytoplasmic1 PublicationAdd BLAST27
Intramembranei604 – 623Discontinuously helical1 PublicationAdd BLAST20
Topological domaini624 – 630Cytoplasmic1 Publication7
Transmembranei631 – 646Helical1 PublicationAdd BLAST16
Topological domaini647 – 817Extracellular1 PublicationAdd BLAST171
Transmembranei818 – 837Helical1 PublicationAdd BLAST20
Topological domaini838 – 1482Cytoplasmic1 PublicationAdd BLAST645

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi60H → A: Normal zinc binding. 1 Publication1
Mutagenesisi127H → A: Reduced zinc binding. 1 Publication1
Mutagenesisi283D → A: Slightly reduced zinc binding. 1 Publication1
Mutagenesisi284E → A: Reduced zinc binding. 1 Publication1
Mutagenesisi311H → A: Normal zinc binding. 1 Publication1
Mutagenesisi359H → A: Normal zinc binding. 1 Publication1
Mutagenesisi1413S → L: Decreased localization to the cell membrane. Decreased interaction with DLG3 and DLG4. No effect on glutamate-gated calcium ion channel activity. 1 Publication1
Mutagenesisi1422L → F: No effect on localizationto the cell membrane. Decreased interaction with DLG3 and DLG4. No effect on glutamate-gated calcium ion channel activity. 1 Publication1
Mutagenesisi1450S → F: No effect on localizationto the cell membrane. Decreased interaction with DLG3 and DLG4. No effect on glutamate-gated calcium ion channel activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL311.
GuidetoPHARMACOLOGYi457.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000001157927 – 1482Glutamate receptor ionotropic, NMDA 2BAdd BLAST1456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi74N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Disulfide bondi86 ↔ 321Combined sources1 Publication
Glycosylationi341N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Glycosylationi348N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi429 ↔ 456Combined sources1 Publication
Disulfide bondi436 ↔ 457Combined sources1 Publication
Glycosylationi444N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi491N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi542N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi688N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi746 ↔ 801Combined sources1 Publication
Modified residuei882PhosphoserineCombined sources1
Modified residuei886PhosphoserineCombined sources1
Modified residuei917PhosphoserineCombined sources1
Modified residuei920PhosphoserineCombined sources1
Modified residuei962PhosphotyrosineBy similarity1
Modified residuei1039PhosphotyrosineCombined sources1
Modified residuei1058PhosphoserineBy similarity1
Modified residuei1061PhosphoserineBy similarity1
Modified residuei1064PhosphoserineBy similarity1
Modified residuei1109PhosphotyrosineBy similarity1
Modified residuei1133PhosphotyrosineBy similarity1
Modified residuei1143PhosphoserineBy similarity1
Modified residuei1155PhosphotyrosineBy similarity1
Modified residuei1255PhosphoserineCombined sources1
Modified residuei1259PhosphoserineCombined sources1
Modified residuei1303PhosphoserineCombined sources1
Modified residuei1472PhosphotyrosineBy similarity1

Post-translational modificationi

Phosphorylated on tyrosine residues (PubMed:7513428). Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity (By similarity).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ00960.
PRIDEiQ00960.

PTM databases

iPTMnetiQ00960.
PhosphoSitePlusiQ00960.
SwissPalmiQ00960.
UniCarbKBiQ00960.

Expressioni

Tissue specificityi

Detected in adult olfactory bulb, brain cortex, hippocampus, striatum, thalamus, superior colliculus, with much lower levels in inferior colliculus, midbrain and cerebellum.1 Publication

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:1350383, PubMed:19910922, PubMed:21677647, PubMed:24876489, PubMed:27135925, PubMed:27916457). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B. In vivo, the subunit composition may depend on the expression levels of the different subunits. Found in a complex with GRIN1, GRIN3A and PPP2CB. Found in a complex with GRIN1 and GRIN3B. Interacts with MAGI3. Interacts with HIP1 and NETO1. Interacts with PDZ domains of PATJ, DLG3 and DLG4. Interacts with DAPK1 (By similarity). Found in a complex with GRIN1 and PRR7 (PubMed:27458189). Interacts with PRR7 (PubMed:27458189).By similarity8 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • beta-catenin binding Source: RGD
  • cell adhesion molecule binding Source: RGD
  • D2 dopamine receptor binding Source: RGD
  • interleukin-1 receptor binding Source: RGD
  • ionotropic glutamate receptor binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • receptor binding Source: RGD
  • scaffold protein binding Source: RGD

Protein-protein interaction databases

BioGridi246575. 12 interactors.
CORUMiQ00960.
DIPiDIP-33702N.
IntActiQ00960. 19 interactors.
MINTiQ00960.
STRINGi10116.ENSRNOP00000011697.

Chemistry databases

BindingDBiQ00960.

Structurei

Secondary structure

11482
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 44Combined sources11
Helixi47 – 50Combined sources4
Helixi53 – 55Combined sources3
Beta strandi64 – 73Combined sources10
Helixi78 – 91Combined sources14
Beta strandi94 – 103Combined sources10
Helixi107 – 119Combined sources13
Beta strandi123 – 127Combined sources5
Helixi128 – 131Combined sources4
Beta strandi143 – 147Combined sources5
Helixi150 – 163Combined sources14
Beta strandi168 – 175Combined sources8
Helixi179 – 191Combined sources13
Beta strandi198 – 205Combined sources8
Beta strandi211 – 213Combined sources3
Helixi215 – 220Combined sources6
Beta strandi226 – 232Combined sources7
Helixi234 – 245Combined sources12
Turni246 – 248Combined sources3
Beta strandi251 – 253Combined sources3
Beta strandi255 – 258Combined sources4
Helixi260 – 263Combined sources4
Beta strandi265 – 267Combined sources3
Beta strandi271 – 273Combined sources3
Beta strandi275 – 281Combined sources7
Turni284 – 286Combined sources3
Helixi289 – 308Combined sources20
Turni309 – 311Combined sources3
Turni322 – 326Combined sources5
Helixi327 – 330Combined sources4
Helixi336 – 339Combined sources4
Beta strandi345 – 348Combined sources4
Beta strandi355 – 359Combined sources5
Beta strandi362 – 367Combined sources6
Beta strandi369 – 371Combined sources3
Beta strandi373 – 379Combined sources7
Beta strandi384 – 387Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JPWX-ray2.80A32-394[»]
3JPYX-ray3.21A32-394[»]
3QELX-ray2.60B/D31-394[»]
3QEMX-ray3.00B/D31-394[»]
4PE5X-ray3.96B/D27-852[»]
5B3JX-ray2.90C/D31-394[»]
5FXGelectron microscopy6.80B/D27-852[»]
5FXHelectron microscopy6.10B/D27-852[»]
5FXIelectron microscopy6.40B/D27-852[»]
5FXJelectron microscopy6.50B/D27-852[»]
5FXKelectron microscopy6.40B/D27-852[»]
5TPZX-ray3.10D32-393[»]
ProteinModelPortaliQ00960.
SMRiQ00960.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00960.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni604 – 623Pore-forming1 Publication1 PublicationAdd BLAST20
Regioni690 – 691Glutamate bindingCombined sources2
Regioni1292 – 1304Interaction with DAPK1By similarityAdd BLAST13

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1480 – 1482PDZ-binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi984 – 989Poly-His6

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.1 Publication

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ00960.
KOiK05210.
PhylomeDBiQ00960.

Family and domain databases

InterProiView protein in InterPro
IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR018884. NMDAR2_C.
IPR028082. Peripla_BP_I.
PfamiView protein in Pfam
PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PF10565. NMDAR2_C. 1 hit.
PRINTSiPR00177. NMDARECEPTOR.
SMARTiView protein in SMART
SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q00960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPSAECCSP KFWLVLAVLA VSGSKARSQK SPPSIGIAVI LVGTSDEVAI
60 70 80 90 100
KDAHEKDDFH HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA
110 120 130 140 150
DDTDQEAIAQ ILDFISAQTL TPILGIHGGS SMIMADKDES SMFFQFGPSI
160 170 180 190 200
EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ DFVNKIRSTI ENSFVGWELE
210 220 230 240 250
EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI FEVANSVGLT
260 270 280 290 300
GYGYTWIVPS LVAGDTDTVP SEFPTGLISV SYDEWDYGLP ARVRDGIAII
310 320 330 340 350
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS
360 370 380 390 400
FSEDGYQMHP KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE
410 420 430 440 450
QEDDHLSIVT LEEAPFVIVE SVDPLSGTCM RNTVPCQKRI ISENKTDEEP
460 470 480 490 500
GYIKKCCKGF CIDILKKISK SVKFTYDLYL VTNGKHGKKI NGTWNGMIGE
510 520 530 540 550
VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR SNGTVSPSAF
560 570 580 590 600
LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
610 620 630 640 650
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL
660 670 680 690 700
AAFMIQEEYV DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA
710 720 730 740 750
EMHAYMGKFN QRGVDDALLS LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT
760 770 780 790 800
IGSGKVFAST GYGIAIQKDS GWKRQVDLAI LQLFGDGEME ELEALWLTGI
810 820 830 840 850
CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH LFYWQFRHCF
860 870 880 890 900
MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR
910 920 930 940 950
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN
960 970 980 990 1000
NPPCEENLFS DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSTSSI
1010 1020 1030 1040 1050
DGLYDCDNPP FTTQPRSISK KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS
1060 1070 1080 1090 1100
GHDDLIRSDV SDISTHTVTY GNIEGNAAKR RKQQYKDSLK KRPASAKSRR
1110 1120 1130 1140 1150
EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK ENSPHWEHVD
1160 1170 1180 1190 1200
LTDIYKERSD DFKRDSVSGG GPCTNRSHLK HGTGEKHGVV GGVPAPWEKN
1210 1220 1230 1240 1250
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN
1260 1270 1280 1290 1300
LYDISEDNSL QELDQPAAPV AVTSNASSTK YPQSPTNSKA QKKNRNKLRR
1310 1320 1330 1340 1350
QHSYDTFVDL QKEEAALAPR SVSLKDKGRF MDGSPYAHMF EMPAGESSFA
1360 1370 1380 1390 1400
NKSSVPTAGH HHNNPGSGYM LSKSLYPDRV TQNPFIPTFG DDQCLLHGSK
1410 1420 1430 1440 1450
SYFFRQPTVA GASKTRPDFR ALVTNKPVVV TLHGAVPGRF QKDICIGNQS
1460 1470 1480
NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV
Length:1,482
Mass (Da):166,071
Last modified:June 1, 1994 - v1
Checksum:iAEF8B9DF3C1B0D5D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1256E → K in AAA50554 (PubMed:7524561).Curated1
Sequence conflicti1430 – 1431VT → SA in AAA50554 (PubMed:7524561).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91562 mRNA. Translation: AAA41714.1.
U11419 mRNA. Translation: AAA50554.1.
PIRiB43274.
RefSeqiNP_036706.1. NM_012574.1.
UniGeneiRn.9711.

Genome annotation databases

GeneIDi24410.
KEGGirno:24410.
UCSCiRGD:2738. rat.

Similar proteinsi

Entry informationi

Entry nameiNMDE2_RAT
AccessioniPrimary (citable) accession number: Q00960
Secondary accession number(s): Q62684
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: March 28, 2018
This is version 172 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, Direct protein sequencing, Reference proteome