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Protein

Voltage-dependent N-type calcium channel subunit alpha-1B

Gene

Cacna1b

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

Functioni

Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei314Calcium ion selectivity and permeabilityBy similarity1
Sitei664Calcium ion selectivity and permeabilityBy similarity1
Sitei1367Calcium ion selectivity and permeabilityBy similarity1
Sitei1655Calcium ion selectivity and permeabilityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi452 – 459ATPSequence analysis8
Calcium bindingi1737 – 1748PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium ion binding Source: InterPro
  • high voltage-gated calcium channel activity Source: RGD
  • protein phosphatase 2A binding Source: RGD
  • voltage-gated calcium channel activity Source: RGD

GO - Biological processi

  • calcium ion import Source: RGD
  • calcium ion transport Source: RGD
  • membrane depolarization during action potential Source: GO_Central
  • positive regulation of neurotransmitter secretion Source: RGD
  • response to ethanol Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to testosterone Source: RGD
  • sensory perception of pain Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent N-type calcium channel subunit alpha-1B
Alternative name(s):
Brain calcium channel III
Short name:
BIII
Calcium channel, L type, alpha-1 polypeptide isoform 5
Voltage-gated calcium channel subunit alpha Cav2.2
Gene namesi
Name:Cacna1b
Synonyms:Cach5, Cacnl1a5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628852. Cacna1b.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 95CytoplasmicSequence analysisAdd BLAST95
Transmembranei96 – 114Helical; Name=S1 of repeat ISequence analysisAdd BLAST19
Topological domaini115 – 133ExtracellularSequence analysisAdd BLAST19
Transmembranei134 – 151Helical; Name=S2 of repeat ISequence analysisAdd BLAST18
Topological domaini152 – 164CytoplasmicSequence analysisAdd BLAST13
Transmembranei165 – 179Helical; Name=S3 of repeat ISequence analysisAdd BLAST15
Topological domaini180 – 186ExtracellularSequence analysis7
Transmembranei187 – 205Helical; Name=S4 of repeat ISequence analysisAdd BLAST19
Topological domaini206 – 225CytoplasmicSequence analysisAdd BLAST20
Transmembranei226 – 245Helical; Name=S5 of repeat ISequence analysisAdd BLAST20
Topological domaini246 – 331ExtracellularSequence analysisAdd BLAST86
Transmembranei332 – 356Helical; Name=S6 of repeat ISequence analysisAdd BLAST25
Topological domaini357 – 483CytoplasmicSequence analysisAdd BLAST127
Transmembranei484 – 503Helical; Name=S1 of repeat IISequence analysisAdd BLAST20
Topological domaini504 – 517ExtracellularSequence analysisAdd BLAST14
Transmembranei518 – 537Helical; Name=S2 of repeat IISequence analysisAdd BLAST20
Topological domaini538 – 545CytoplasmicSequence analysis8
Transmembranei546 – 564Helical; Name=S3 of repeat IISequence analysisAdd BLAST19
Topological domaini565 – 575ExtracellularSequence analysisAdd BLAST11
Transmembranei576 – 593Helical; Name=S4 of repeat IISequence analysisAdd BLAST18
Topological domaini594 – 612CytoplasmicSequence analysisAdd BLAST19
Transmembranei613 – 632Helical; Name=S5 of repeat IISequence analysisAdd BLAST20
Topological domaini633 – 685ExtracellularSequence analysisAdd BLAST53
Transmembranei686 – 710Helical; Name=S6 of repeat IISequence analysisAdd BLAST25
Topological domaini711 – 1143CytoplasmicSequence analysisAdd BLAST433
Transmembranei1144 – 1167Helical; Name=S1 of repeat IIISequence analysisAdd BLAST24
Topological domaini1168 – 1184ExtracellularSequence analysisAdd BLAST17
Transmembranei1185 – 1204Helical; Name=S2 of repeat IIISequence analysisAdd BLAST20
Topological domaini1205 – 1212CytoplasmicSequence analysis8
Transmembranei1213 – 1235Helical; Name=S3 of repeat IIISequence analysisAdd BLAST23
Topological domaini1236 – 1250ExtracellularSequence analysisAdd BLAST15
Transmembranei1251 – 1265Helical; Name=S4 of repeat IIISequence analysisAdd BLAST15
Topological domaini1266 – 1286CytoplasmicSequence analysisAdd BLAST21
Transmembranei1287 – 1306Helical; Name=S5 of repeat IIISequence analysisAdd BLAST20
Topological domaini1307 – 1392ExtracellularSequence analysisAdd BLAST86
Transmembranei1393 – 1417Helical; Name=S6 of repeat IIISequence analysisAdd BLAST25
Topological domaini1418 – 1474CytoplasmicSequence analysisAdd BLAST57
Transmembranei1475 – 1493Helical; Name=S1 of repeat IVSequence analysisAdd BLAST19
Topological domaini1494 – 1507ExtracellularSequence analysisAdd BLAST14
Transmembranei1508 – 1527Helical; Name=S2 of repeat IVSequence analysisAdd BLAST20
Topological domaini1528 – 1536CytoplasmicSequence analysis9
Transmembranei1537 – 1555Helical; Name=S3 of repeat IVSequence analysisAdd BLAST19
Topological domaini1556 – 1563ExtracellularSequence analysis8
Transmembranei1564 – 1582Helical; Name=S4 of repeat IVSequence analysisAdd BLAST19
Topological domaini1583 – 1601CytoplasmicSequence analysisAdd BLAST19
Transmembranei1602 – 1621Helical; Name=S5 of repeat IVSequence analysisAdd BLAST20
Topological domaini1622 – 1683ExtracellularSequence analysisAdd BLAST62
Transmembranei1684 – 1703Helical; Name=S6 of repeat IVSequence analysisAdd BLAST20
Topological domaini1704 – 2336CytoplasmicSequence analysisAdd BLAST633

GO - Cellular componenti

  • axon terminus Source: RGD
  • dendritic shaft Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • plasma membrane Source: RGD
  • protein complex Source: RGD
  • voltage-gated calcium channel complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5107.
GuidetoPHARMACOLOGYi533.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539241 – 2336Voltage-dependent N-type calcium channel subunit alpha-1BAdd BLAST2336

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22Omega-N-methylarginineBy similarity1
Glycosylationi256N-linked (GlcNAc...)Sequence analysis1
Modified residuei411PhosphoserineCombined sources1
Modified residuei746PhosphoserineCombined sources1
Modified residuei749PhosphoserineBy similarity1
Modified residuei784PhosphoserineBy similarity1
Modified residuei1067PhosphoserineBy similarity1
Glycosylationi1563N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1675N-linked (GlcNAc...)Sequence analysis1
Modified residuei1719Phosphoserine; by PKASequence analysis1
Modified residuei2065PhosphoserineBy similarity1
Modified residuei2221PhosphoserineBy similarity1
Modified residuei2230PhosphoserineBy similarity1
Modified residuei2253PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ02294.
PRIDEiQ02294.

PTM databases

iPTMnetiQ02294.
PhosphoSitePlusiQ02294.

Expressioni

Tissue specificityi

Central nervous system.

Interactioni

Subunit structurei

Multisubunit complex consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts with RIMS1. Interacts with FMR1 (via C-terminus); this interaction induces a deacrease in the number of presynaptic functional CACNA1B channels at the cell surface.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Syt1P217072EBI-540038,EBI-458098

GO - Molecular functioni

  • protein phosphatase 2A binding Source: RGD

Protein-protein interaction databases

IntActiQ02294. 4 interactors.
MINTiMINT-102470.
STRINGi10116.ENSRNOP00000006162.

Chemistry databases

BindingDBiQ02294.

Structurei

Secondary structure

12336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi364 – 403Combined sources40

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DEXX-ray2.00B358-468[»]
ProteinModelPortaliQ02294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati82 – 359IAdd BLAST278
Repeati469 – 713IIAdd BLAST245
Repeati1135 – 1421IIIAdd BLAST287
Repeati1458 – 1711IVAdd BLAST254
Domaini1724 – 1759EF-handPROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni379 – 396Binding to the beta subunitAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2049 – 2053Poly-His5
Compositional biasi2115 – 2119Poly-Ser5

Domaini

Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.

Sequence similaritiesi

Contains 1 EF-hand domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiQ02294.
PhylomeDBiQ02294.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF161. PTHR10037:SF161. 3 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: 2 isoforms may be produced.
Isoform 1 (identifier: Q02294-1) [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
MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA
60 70 80 90 100
QRARTMALYN PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM
110 120 130 140 150
ILATIIANCI VLALEQHLPD GDKTPMSERL DDTEPYFIGI FCFEAGIKII
160 170 180 190 200
ALGFVFHKGS YLRNGWNVMD FVVVLTEILA TAGTDFDLRT LRAVRVLRPL
210 220 230 240 250
KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII GLEFYMGKFH
260 270 280 290 300
KACFPNSTDA EPVGDFPCGK EAPARLCDSD TECREYWPGP NFGITNFDNI
310 320 330 340 350
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL
360 370 380 390 400
VLGVLSGEFA KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML
410 420 430 440 450
AEEDKNAEEK SPLDAVLKRA ATKKSRNDLI HAEEGEDRFV DLCAAGSPFA
460 470 480 490 500
RASLKSGKTE SSSYFRRKEK MFRFLIRRMV KAQSFYWVVL CVVALNTLCV
510 520 530 540 550
AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR SYFRSSFNCF
560 570 580 590 600
DFGVIVGSIF EVVWAAIKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV
610 620 630 640 650
VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFQD ETPTTNFDTF
660 670 680 690 700
PAAILTVFQI LTGEDWNAVM YHGIESQGGV SKGMFSSFYF IVLTLFGNYT
710 720 730 740 750
LLNVFLAIAV DNLANAQELT KDEEEMEEAA NQKLALQKAK EVAEVSPMSA
760 770 780 790 800
ANISIAARQQ NSAKARSVWE QRASQLRLQN LRASCEALYS EMDPEERLRY
810 820 830 840 850
ASTRHVRPDM KTHMDRPLVV EPGRDGLRGP AGNKSKPEGT EATEGADPPR
860 870 880 890 900
RHHRHRDRDK TSASTPAGGE QDRTDCPKAE STETGAREER ARPRRSHSKE
910 920 930 940 950
APGADTQVRC ERSRRHHRRG SPEEATEREP RRHRAHRHAQ DSSKEGKEGT
960 970 980 990 1000
APVLVPKGER RARHRGPRTG PRETENSEEP TRRHRAKHKV PPTLEPPERE
1010 1020 1030 1040 1050
VAEKESNVVE GDKETRNHQP KEPRCDLEAI AVTGVGSLHM LPSTCLQKVD
1060 1070 1080 1090 1100
EQPEDADNQR NVTRMGSQPS DPSTTVHVPV TLTGPPGEAT VVPSANTDLE
1110 1120 1130 1140 1150
GQAEGKKEAE ADDVLRRGPR PIVPYSSMFC LSPTNLLRRF CHYIVTMRYF
1160 1170 1180 1190 1200
EMVILVVIAL SSIALAAEDP VRTDSFRNNA LKYMDYIFTG VFTFEMVIKM
1210 1220 1230 1240 1250
IDLGLLLHPG AYFRDLWNIL DFIVVSGALV AFAFSSFMGG SKGKDINTIK
1260 1270 1280 1290 1300
SLRVLRVLRP LKTIKRLPKL KAVFDCVVNS LKNVLNILIV YMLFMFIFAV
1310 1320 1330 1340 1350
IAVQLFKGKF FYCTDESKEL ERDCRGQYLD YEKEEVEAQP RQWKKYDFHY
1360 1370 1380 1390 1400
DNVLWALLTL FTVSTGEGWP MVLKHSVDAT YEEQGPSPGF RMELSIFYVV
1410 1420 1430 1440 1450
YFVVFPFFFV NIFVALIIIT FQEQGDKVMS ECSLEKNERA CIDFAISAKP
1460 1470 1480 1490 1500
LTRYMPQNKQ SFQYKTWTFV VSPPFEYFIM AMIALNTVVL MMKFYDAPYE
1510 1520 1530 1540 1550
YELMLKCLNI VFTSMFSLEC ILKIIAFGVL NYFRDAWNVF DFVTVLGSIT
1560 1570 1580 1590 1600
DILVTEIANN FINLSFLRLF RAARLIKLCR QGYTIRILLW TFVQSFKALP
1610 1620 1630 1640 1650
YVCLLIAMLF FIYAIIGMQV FGNIALDDGT SINRHNNFRT FLQALMLLFR
1660 1670 1680 1690 1700
SATGEAWHEI MLSCLGNRAC DPHANASECG SDFAYFYFVS FIFLCSFLML
1710 1720 1730 1740 1750
NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA CGRISYNDMF
1760 1770 1780 1790 1800
EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR
1810 1820 1830 1840 1850
TALEIKLAPA GTKQHQCDAE LRKEISSVWA NLPQKTLDLL VPPHKPDEMT
1860 1870 1880 1890 1900
VGKVYAALMI FDFYKQNKTT RDQTHQAPGG LSQMGPVSLF HPLKATLEQT
1910 1920 1930 1940 1950
QPAVLRGARV FLRQKSATSL SNGGAIQTQE SGIKESLSWG TQRTQDVLYE
1960 1970 1980 1990 2000
ARAPLERGHS AEIPVGQPGA LAVDVQMQNM TLRGPDGEPQ PGLESQGRAA
2010 2020 2030 2040 2050
SMPRLAAETQ PAPNASPMKR SISTLAPRPH GTQLCNTVLD RPPPSQVSHH
2060 2070 2080 2090 2100
HHHRCHRRRD KKQRSLEKGP SLSVDTEGAP STAAGSGLPH GEGSTGCRRE
2110 2120 2130 2140 2150
RKQERGRSQE RRQPSSSSSE KQRFYSCDRF GSREPPQPKP SLSSHPISPT
2160 2170 2180 2190 2200
AALEPGPHPQ GSGSVNGSPL MSTSGASTPG RGGRRQLPQT PLTPRPSITY
2210 2220 2230 2240 2250
KTANSSPVHF AEGQSGLPAF SPGRLSRGLS EHNALLQKEP LSQPLASGSR
2260 2270 2280 2290 2300
IGSDPYLGQR LDSEASAHNL PEDTLTFEEA VATNSGRSSR TSYVSSLTSQ
2310 2320 2330
SHPLRRVPNG YHCTLGLSTG VRARHSYHHP DQDHWC
Length:2,336
Mass (Da):262,256
Last modified:October 1, 1996 - v1
Checksum:i8D50AF67834FD1BC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1538N → D no nucleotide entry (PubMed:1692134).Curated1
Sequence conflicti1579C → L no nucleotide entry (PubMed:1692134).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92905 mRNA. Translation: AAA42014.1.
PIRiB35901.
UniGeneiRn.85880.

Genome annotation databases

UCSCiRGD:628852. rat. [Q02294-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92905 mRNA. Translation: AAA42014.1.
PIRiB35901.
UniGeneiRn.85880.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DEXX-ray2.00B358-468[»]
ProteinModelPortaliQ02294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ02294. 4 interactors.
MINTiMINT-102470.
STRINGi10116.ENSRNOP00000006162.

Chemistry databases

BindingDBiQ02294.
ChEMBLiCHEMBL5107.
GuidetoPHARMACOLOGYi533.

PTM databases

iPTMnetiQ02294.
PhosphoSitePlusiQ02294.

Proteomic databases

PaxDbiQ02294.
PRIDEiQ02294.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:628852. rat. [Q02294-1]

Organism-specific databases

RGDi628852. Cacna1b.

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiQ02294.
PhylomeDBiQ02294.

Miscellaneous databases

PROiQ02294.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF161. PTHR10037:SF161. 3 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAC1B_RAT
AccessioniPrimary (citable) accession number: Q02294
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 143 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.