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Protein

Glutamate receptor ionotropic, NMDA 2A

Gene

Grin2a

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+. Sensitivity to glutamate and channel kinetics depend on the subunit composition; channels containing GRIN1 and GRIN2A have higher sensitivity to glutamate and faster kinetics than channels formed by GRIN1 and GRIN2B (PubMed:28384476). Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (By similarity).By similarity10 Publications

Enzyme regulationi

Channel activity is inhibited by nM concentrations of Zn2+.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi44Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi128Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi266ZincCombined sources1 Publication1
Metal bindingi282ZincCombined sources1 Publication1
Binding sitei518GlutamateCombined sources3 Publications1
Sitei614Functional determinant of NMDA receptorsBy similarity1

GO - Molecular functioni

  • ATPase binding Source: RGD
  • calcium channel activity Source: RGD
  • cation channel activity Source: RGD
  • cell adhesion molecule binding Source: RGD
  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • glutamate binding Source: RGD
  • glutamate-gated calcium ion channel activity Source: UniProtKB
  • glutamate receptor binding Source: RGD
  • ionotropic glutamate receptor activity Source: RGD
  • neurotransmitter binding Source: RGD
  • NMDA glutamate receptor activity Source: UniProtKB
  • protein complex binding Source: RGD
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • receptor binding Source: RGD
  • scaffold protein binding Source: BHF-UCL
  • voltage-gated cation channel activity Source: RGD
  • zinc ion binding Source: RGD

GO - Biological processi

  • action potential Source: RGD
  • calcium ion transmembrane import into cytosol Source: UniProtKB
  • calcium ion transport Source: RGD
  • cellular response to amino acid stimulus Source: RGD
  • cellular response to dsRNA Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to lipid Source: RGD
  • cellular response to magnesium ion Source: RGD
  • cellular response to manganese ion Source: RGD
  • cellular response to zinc ion Source: RGD
  • cerebral cortex development Source: RGD
  • chemical synaptic transmission Source: RGD
  • directional locomotion Source: RGD
  • dopamine metabolic process Source: RGD
  • excitatory postsynaptic potential Source: RGD
  • hippocampus development Source: RGD
  • ionotropic glutamate receptor signaling pathway Source: RGD
  • learning Source: RGD
  • learning or memory Source: RGD
  • locomotion Source: RGD
  • long-term synaptic potentiation Source: RGD
  • memory Source: UniProtKB
  • modulation of chemical synaptic transmission Source: RGD
  • negative regulation of protein catabolic process Source: RGD
  • neurogenesis Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of cell death Source: RGD
  • positive regulation of excitatory postsynaptic potential Source: BHF-UCL
  • positive regulation of long-term synaptic potentiation Source: RGD
  • protein localization Source: RGD
  • protein tetramerization Source: RGD
  • regulation of long-term neuronal synaptic plasticity Source: RGD
  • regulation of membrane potential Source: RGD
  • regulation of postsynaptic membrane potential Source: RGD
  • regulation of sensory perception of pain Source: RGD
  • regulation of synaptic plasticity Source: RGD
  • response to amine Source: RGD
  • response to ammonium ion 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 drug Source: RGD
  • response to ethanol Source: ARUK-UCL
  • response to fungicide Source: RGD
  • response to light stimulus Source: RGD
  • response to manganese ion Source: RGD
  • response to methylmercury Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to other organism Source: RGD
  • response to wounding Source: RGD
  • rhythmic process Source: RGD
  • sensory perception of pain Source: RGD
  • serotonin metabolic process Source: RGD
  • sleep Source: RGD
  • spinal cord development Source: RGD
  • startle response Source: RGD
  • visual learning Source: RGD

Keywordsi

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

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 2A
Short name:
GluN2A1 Publication
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-1
N-methyl D-aspartate receptor subtype 2A
Short name:
NMDAR2A1 Publication
Short name:
NR2A2 Publications
Gene namesi
Name:Grin2a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2737. Grin2a.

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 domaini23 – 555ExtracellularCuratedAdd BLAST533
Transmembranei556 – 576HelicalBy similarityAdd BLAST21
Topological domaini577 – 600CytoplasmicCuratedAdd BLAST24
Intramembranei601 – 620Discontinuously helicalBy similarityAdd BLAST20
Topological domaini621 – 625CytoplasmicCurated5
Transmembranei626 – 645HelicalBy similarityAdd BLAST20
Topological domaini646 – 816ExtracellularCuratedAdd BLAST171
Transmembranei817 – 837HelicalBy similarityAdd BLAST21
Topological domaini838 – 1464CytoplasmicCuratedAdd BLAST627

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi233K → A or R: Nearly abolishes inhibition by Zn(2+). 1 Publication1
Mutagenesisi264N → W: Nearly abolishes inhibition by Zn(2+). 1 Publication1
Mutagenesisi282D → A or H: Nearly abolishes inhibition by Zn(2+). 1 Publication1
Mutagenesisi416F → A: Decreased sensitivity to glutamate. 1 Publication1
Mutagenesisi730Y → F, L or M: Strongly decreased sensitivity to glutamate. 1 Publication1
Mutagenesisi734V → A: Decreased sensitivity to glutamate. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL310.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000001157623 – 1464Glutamate receptor ionotropic, NMDA 2AAdd BLAST1442

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi75N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi87 ↔ 320Combined sources1 Publication
Glycosylationi340N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi429 ↔ 455Combined sources6 Publications
Disulfide bondi436 ↔ 456Combined sources6 Publications
Glycosylationi443N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi444N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi541N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi745 ↔ 800Combined sources4 Publications
Modified residuei882PhosphoserineCombined sources1
Modified residuei890PhosphoserineCombined sources1
Modified residuei929PhosphoserineCombined sources1
Modified residuei1025PhosphoserineCombined sources1
Modified residuei1059PhosphoserineCombined sources1
Modified residuei1062PhosphoserineCombined sources1
Modified residuei1198PhosphoserineCombined sources1
Modified residuei1291PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ00959.
PRIDEiQ00959.

PTM databases

iPTMnetiQ00959.
PhosphoSitePlusiQ00959.
SwissPalmiQ00959.
UniCarbKBiQ00959.

Expressioni

Tissue specificityi

Detected in brain cortex, olfactory bulb, hippocampus, striatum, thalamus, superior colliculus, inferior colliculus, midbrain and cerebellum (at protein level) (PubMed:9509416). Detected in brain cortex, hypothalamus and cerebellum.2 Publications

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:8428958, PubMed:28384476, PubMed:16281028, PubMed:23625947, PubMed:24462099, PubMed:27618671, PubMed:27916457, PubMed:28468946, PubMed:28760974, Ref. 24). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B (PubMed:11160393, PubMed:11588171, PubMed:12391275, PubMed:11929923). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable). Found in a complex with GRIN1, GRIN3A and PPP2CB (PubMed:11588171). Found in a complex with GRIN1 and GRIN3B (PubMed:14602821). Interacts with AIP1 (PubMed:9694864). Interacts with HIP1 and NETO1. 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 PDZ domains of PATJ and DLG4 (PubMed:7569905, PubMed:9647694). Interacts with LRFN2 (PubMed:16495444).By similarityCurated20 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • ATPase binding Source: RGD
  • cell adhesion molecule binding Source: RGD
  • glutamate receptor binding Source: RGD
  • protein complex binding Source: RGD
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • receptor binding Source: RGD
  • scaffold protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi246574. 7 interactors.
CORUMiQ00959.
DIPiDIP-34031N.
IntActiQ00959. 7 interactors.
MINTiMINT-93314.
STRINGi10116.ENSRNOP00000042235.

Chemistry databases

BindingDBiQ00959.

Structurei

Secondary structure

11464
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 40Combined sources6
Beta strandi42 – 44Combined sources3
Beta strandi68 – 73Combined sources6
Helixi79 – 91Combined sources13
Beta strandi96 – 101Combined sources6
Helixi108 – 120Combined sources13
Beta strandi124 – 128Combined sources5
Helixi129 – 132Combined sources4
Beta strandi144 – 147Combined sources4
Helixi151 – 164Combined sources14
Beta strandi169 – 177Combined sources9
Helixi180 – 193Combined sources14
Beta strandi194 – 196Combined sources3
Beta strandi198 – 200Combined sources3
Beta strandi204 – 207Combined sources4
Helixi213 – 219Combined sources7
Beta strandi225 – 230Combined sources6
Helixi233 – 245Combined sources13
Turni247 – 249Combined sources3
Beta strandi253 – 257Combined sources5
Helixi259 – 262Combined sources4
Beta strandi277 – 281Combined sources5
Beta strandi284 – 286Combined sources3
Helixi288 – 309Combined sources22
Beta strandi310 – 312Combined sources3
Turni335 – 337Combined sources3
Beta strandi338 – 340Combined sources3
Beta strandi341 – 343Combined sources3
Beta strandi346 – 348Combined sources3
Beta strandi354 – 358Combined sources5
Beta strandi362 – 366Combined sources5
Turni368 – 370Combined sources3
Beta strandi372 – 377Combined sources6
Turni379 – 382Combined sources4
Helixi402 – 404Combined sources3
Beta strandi406 – 410Combined sources5
Turni414 – 416Combined sources3
Beta strandi417 – 421Combined sources5
Turni424 – 426Combined sources3
Beta strandi434 – 447Combined sources14
Beta strandi449 – 458Combined sources10
Helixi459 – 471Combined sources13
Beta strandi475 – 479Combined sources5
Beta strandi482 – 485Combined sources4
Beta strandi488 – 491Combined sources4
Helixi495 – 501Combined sources7
Beta strandi506 – 508Combined sources3
Helixi516 – 519Combined sources4
Beta strandi522 – 524Combined sources3
Beta strandi529 – 531Combined sources3
Beta strandi533 – 538Combined sources6
Helixi668 – 671Combined sources4
Helixi673 – 675Combined sources3
Beta strandi676 – 678Combined sources3
Beta strandi686 – 688Combined sources3
Helixi689 – 697Combined sources9
Helixi699 – 705Combined sources7
Helixi706 – 708Combined sources3
Helixi713 – 721Combined sources9
Beta strandi726 – 731Combined sources6
Helixi732 – 740Combined sources9
Helixi743 – 745Combined sources3
Beta strandi747 – 751Combined sources5
Helixi752 – 754Combined sources3
Helixi755 – 757Combined sources3
Beta strandi759 – 761Combined sources3
Beta strandi764 – 766Combined sources3
Helixi772 – 784Combined sources13
Helixi787 – 795Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A5SX-ray1.70A401-539[»]
2A5TX-ray2.00B401-539[»]
4JWXX-ray1.50A404-539[»]
A661-802[»]
4NF4X-ray2.00B402-539[»]
B661-802[»]
4NF5X-ray1.90B402-539[»]
B661-802[»]
4NF6X-ray2.10B402-539[»]
B661-802[»]
4NF8X-ray1.86B402-539[»]
B661-802[»]
5DEXX-ray2.40B402-539[»]
B661-802[»]
5I56X-ray2.28B402-539[»]
B661-800[»]
5I57X-ray1.70B402-539[»]
B661-800[»]
5I58X-ray2.52B402-539[»]
B661-800[»]
5I59X-ray2.25B402-539[»]
B661-800[»]
5JTYX-ray2.72B402-539[»]
B661-800[»]
5TPWX-ray2.91B34-393[»]
5TQ0X-ray2.70B34-393[»]
5TQ2X-ray3.29B34-393[»]
5U8CX-ray1.60B402-539[»]
A661-802[»]
5VIHX-ray2.40B402-539[»]
B566-800[»]
5VIIX-ray1.95B402-539[»]
B566-800[»]
5VIJX-ray2.10B402-539[»]
B566-800[»]
ProteinModelPortaliQ00959.
SMRiQ00959.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00959.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni511 – 513Glutamate bindingCombined sources1 Publication3
Regioni599 – 620Pore-formingBy similarityAdd BLAST22
Regioni689 – 690Glutamate bindingCombined sources2 Publications2
Regioni730 – 731Glutamate bindingCombined sources2 Publications2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1462 – 1464PDZ-bindingCurated3

Domaini

Contains an N-terminal domain, a ligand-binding domain and a transmembrane domain. Agonist binding to the extracellular ligand-binding domains triggers channel gating.1 Publication
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.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ00959.
KOiK05209.
PhylomeDBiQ00959.

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.

Q00959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLGYWTLL VLPALLVWRD PAQNAAAEKG PPALNIAVLL GHSHDVTERE
60 70 80 90 100
LRNLWGPEQA TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF
110 120 130 140 150
GDDTDQEAVA QMLDFISSQT FIPILGIHGG ASMIMADKDP TSTFFQFGAS
160 170 180 190 200
IQQQATVMLK IMQDYDWHVF SLVTTIFPGY RDFISFIKTT VDNSFVGWDM
210 220 230 240 250
QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL SEARSLGLTG
260 270 280 290 300
YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT
310 320 330 340 350
TAASSMLEKF SYIPEAKASC YGQAEKPETP LHTLHQFMVN VTWDGKDLSF
360 370 380 390 400
TEEGYQVHPR LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW PRYKSFSDCE
410 420 430 440 450
PDDNHLSIVT LEEAPFVIVE DIDPLTETCV RNTVPCRKFV KINNSTNEGM
460 470 480 490 500
NVKKCCKGFC IDILKKLSRT VKFTYDLYLV TNGKHGKKVN NVWNGMIGEV
510 520 530 540 550
VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS NGTVSPSAFL
560 570 580 590 600
EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT
610 620 630 640 650
IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA
660 670 680 690 700
AFMIQEEFVD QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY
710 720 730 740 750
MHQYMTRFNQ RGVEDALVSL KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI
760 770 780 790 800
GSGYIFASTG YGIALQKGSP WKRQIDLALL QFVGDGEMEE LETLWLTGIC
810 820 830 840 850
HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL FYWKLRFCFT
860 870 880 890 900
GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS
910 920 930 940 950
AKNISNMSNM NSSRMDSPKR ATDFIQRGSL IVDMVSDKGN LIYSDNRSFQ
960 970 980 990 1000
GKDSIFGDNM NELQTFVANR HKDNLSNYVF QGQHPLTLNE SNPNTVEVAV
1010 1020 1030 1040 1050
STESKGNSRP RQLWKKSMES LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR
1060 1070 1080 1090 1100
YLPEEVAHSD ISETSSRATC HREPDNNKNH KTKDNFKRSM ASKYPKDCSD
1110 1120 1130 1140 1150
VDRTYMKTKA SSPRDKIYTI DGEKEPSFHL DPPQFVENIT LPENVGFPDT
1160 1170 1180 1190 1200
YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH
1210 1220 1230 1240 1250
SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE
1260 1270 1280 1290 1300
DQMLQETGNP ATREEVYQQD WSQNNALQFQ KNKLRINRQH SYDNILDKPR
1310 1320 1330 1340 1350
EIDLSRPSRS ISLKDRERLL EGNLYGSLFS VPSSKLLGNK SSLFPQGLED
1360 1370 1380 1390 1400
SKRSKSLLPD HASDNPFLHT YGDDQRLVIG RCPSDPYKHS LPSQAVNDSY
1410 1420 1430 1440 1450
LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNTMYS TPRVLNSCSN
1460
RRVYKKMPSI ESDV
Length:1,464
Mass (Da):165,469
Last modified:December 15, 1998 - v2
Checksum:iDC1528E1898DECA4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti246L → F in BAA02498 (PubMed:8428958).Curated1
Sequence conflicti758S → T in BAA02498 (PubMed:8428958).Curated1
Sequence conflicti758S → T in AAB58801 (Ref. 4) Curated1
Sequence conflicti990E → D in AAB58801 (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91561 mRNA. Translation: AAC03565.1.
D13211 mRNA. Translation: BAA02498.1.
AF001423 mRNA. Translation: AAB58801.1.
PIRiA43274.
RefSeqiNP_036705.3. NM_012573.3.
UniGeneiRn.9710.

Genome annotation databases

GeneIDi24409.
KEGGirno:24409.
UCSCiRGD:2737. rat.

Similar proteinsi

Entry informationi

Entry nameiNMDE1_RAT
AccessioniPrimary (citable) accession number: Q00959
Secondary accession number(s): O08948, Q63728
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 15, 1998
Last modified: November 22, 2017
This is version 169 of the entry and version 2 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