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Q9NQC3

- RTN4_HUMAN

UniProt

Q9NQC3 - RTN4_HUMAN

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Protein

Reticulon-4

Gene

RTN4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Regulates neurite fasciculation, branching and extension in the developing nervous system. Involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS. Regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex (By similarity). Isoform 2 reduces the anti-apoptotic activity of Bcl-xl and Bcl-2. This is likely consecutive to their change in subcellular location, from the mitochondria to the endoplasmic reticulum, after binding and sequestration. Isoform 2 and isoform 3 inhibit BACE1 activity and amyloid precursor protein processing.By similarity3 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. apoptotic process Source: UniProtKB
  3. axonal fasciculation Source: UniProtKB
  4. cardiac epithelial to mesenchymal transition Source: Ensembl
  5. cerebral cortex radial glia guided migration Source: UniProtKB
  6. endoplasmic reticulum tubular network organization Source: UniProtKB
  7. negative regulation of axon extension Source: UniProtKB
  8. negative regulation of axonogenesis Source: Reactome
  9. negative regulation of cell growth Source: DFLAT
  10. neurotrophin TRK receptor signaling pathway Source: Reactome
  11. regulation of apoptotic process Source: UniProtKB
  12. regulation of axonogenesis Source: Reactome
  13. regulation of branching morphogenesis of a nerve Source: UniProtKB
  14. regulation of cell migration Source: MGI
Complete GO annotation...

Keywords - Biological processi

Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_13815. Axonal growth inhibition (RHOA activation).

Names & Taxonomyi

Protein namesi
Recommended name:
Reticulon-4
Alternative name(s):
Foocen
Neurite outgrowth inhibitor
Short name:
Nogo protein
Neuroendocrine-specific protein
Short name:
NSP
Neuroendocrine-specific protein C homolog
RTN-x
Reticulon-5
Gene namesi
Name:RTN4
Synonyms:KIAA0886, NOGO
ORF Names:My043, SP1507
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:14085. RTN4.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein
Note: Anchored to the membrane of the endoplasmic reticulum through 2 putative transmembrane domains.

GO - Cellular componenti

  1. cell projection Source: Ensembl
  2. endoplasmic reticulum Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. integral component of endoplasmic reticulum membrane Source: UniProtKB
  5. intracellular Source: UniProtKB
  6. neuronal cell body Source: Ensembl
  7. nuclear envelope Source: UniProtKB
  8. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34883.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11921192Reticulon-4PRO_0000168165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine6 Publications
Modified residuei7 – 71Phosphoserine2 Publications
Modified residuei15 – 151Phosphoserine3 Publications
Modified residuei107 – 1071Phosphoserine2 Publications
Modified residuei152 – 1521PhosphoserineBy similarity
Modified residuei181 – 1811Phosphoserine1 Publication
Modified residuei182 – 1821Phosphoserine1 Publication
Modified residuei361 – 3611PhosphoserineBy similarity
Modified residuei511 – 5111PhosphoserineBy similarity
Modified residuei1104 – 11041N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NQC3.
PaxDbiQ9NQC3.
PRIDEiQ9NQC3.

PTM databases

PhosphoSiteiQ9NQC3.

Miscellaneous databases

PMAP-CutDBQ9NQC3.

Expressioni

Tissue specificityi

Isoform 1 is specifically expressed in brain and testis and weakly in heart and skeletal muscle. Isoform 2 is widely expressed except for the liver. Isoform 3 is expressed in brain, skeletal muscle and adipocytes. Isoform 4 is testis-specific.

Gene expression databases

BgeeiQ9NQC3.
ExpressionAtlasiQ9NQC3. baseline and differential.
GenevestigatoriQ9NQC3.

Organism-specific databases

HPAiCAB005388.
HPA023977.

Interactioni

Subunit structurei

Binds to RTN4R. Interacts with Bcl-xl and Bcl-2. Isoform 2 binds to NGBR and RTN3. Isoform 2 and isoform 3 interact with BACE1 and BACE2. Interacts with RTN4IP1. Interacts with ATL1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATL1Q8WXF72EBI-715972,EBI-2410266
NCK2O436392EBI-715945,EBI-713635

Protein-protein interaction databases

BioGridi121400. 71 interactions.
IntActiQ9NQC3. 26 interactions.
MINTiMINT-154434.

Structurei

Secondary structure

1
1192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni1059 – 10624
Helixi1063 – 10708
Helixi1074 – 109421
Helixi1095 – 10973
Helixi1100 – 11078

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G31NMR-A1055-1114[»]
2JV5NMR-A1055-1108[»]
DisProtiDP00524.
ProteinModelPortaliQ9NQC3.
SMRiQ9NQC3. Positions 1055-1114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NQC3.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 10181018CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1040 – 113394LumenalSequence AnalysisAdd
BLAST
Topological domaini1155 – 119238CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1019 – 103921HelicalSequence AnalysisAdd
BLAST
Transmembranei1134 – 115421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1005 – 1192188ReticulonPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 4718Poly-GluAdd
BLAST
Compositional biasi143 – 1486Poly-Pro

Domaini

Three regions, residues 59-172, 544-725 and the loop 66 amino acids, between the two transmembrane domains, known as Nogo-66 loop, appear to be responsible for the inhibitory effect on neurite outgrowth and the spreading of neurons. This Nogo-66 loop, mediates also the binding of RTN4 to its receptor (By similarity).By similarity

Sequence similaritiesi

Contains 1 reticulon domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG306139.
GeneTreeiENSGT00390000009934.
HOVERGENiHBG023134.
InParanoidiQ9NQC3.
OMAiNIHRVAT.
OrthoDBiEOG7CZK7J.
PhylomeDBiQ9NQC3.
TreeFamiTF105431.

Family and domain databases

InterProiIPR003388. Reticulon.
[Graphical view]
PANTHERiPTHR10994. PTHR10994. 1 hit.
PfamiPF02453. Reticulon. 1 hit.
[Graphical view]
PROSITEiPS50845. RETICULON. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NQC3) [UniParc]FASTAAdd to Basket

Also known as: RTN 4A, Nogo-A, RTN-xL

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
MEDLDQSPLV SSSDSPPRPQ PAFKYQFVRE PEDEEEEEEE EEEDEDEDLE
60 70 80 90 100
ELEVLERKPA AGLSAAPVPT APAAGAPLMD FGNDFVPPAP RGPLPAAPPV
110 120 130 140 150
APERQPSWDP SPVSSTVPAP SPLSAAAVSP SKLPEDDEPP ARPPPPPPAS
160 170 180 190 200
VSPQAEPVWT PPAPAPAAPP STPAAPKRRG SSGSVDETLF ALPAASEPVI
210 220 230 240 250
RSSAENMDLK EQPGNTISAG QEDFPSVLLE TAASLPSLSP LSAASFKEHE
260 270 280 290 300
YLGNLSTVLP TEGTLQENVS EASKEVSEKA KTLLIDRDLT EFSELEYSEM
310 320 330 340 350
GSSFSVSPKA ESAVIVANPR EEIIVKNKDE EEKLVSNNIL HNQQELPTAL
360 370 380 390 400
TKLVKEDEVV SSEKAKDSFN EKRVAVEAPM REEYADFKPF ERVWEVKDSK
410 420 430 440 450
EDSDMLAAGG KIESNLESKV DKKCFADSLE QTNHEKDSES SNDDTSFPST
460 470 480 490 500
PEGIKDRSGA YITCAPFNPA ATESIATNIF PLLGDPTSEN KTDEKKIEEK
510 520 530 540 550
KAQIVTEKNT STKTSNPFLV AAQDSETDYV TTDNLTKVTE EVVANMPEGL
560 570 580 590 600
TPDLVQEACE SELNEVTGTK IAYETKMDLV QTSEVMQESL YPAAQLCPSF
610 620 630 640 650
EESEATPSPV LPDIVMEAPL NSAVPSAGAS VIQPSSSPLE ASSVNYESIK
660 670 680 690 700
HEPENPPPYE EAMSVSLKKV SGIKEEIKEP ENINAALQET EAPYISIACD
710 720 730 740 750
LIKETKLSAE PAPDFSDYSE MAKVEQPVPD HSELVEDSSP DSEPVDLFSD
760 770 780 790 800
DSIPDVPQKQ DETVMLVKES LTETSFESMI EYENKEKLSA LPPEGGKPYL
810 820 830 840 850
ESFKLSLDNT KDTLLPDEVS TLSKKEKIPL QMEELSTAVY SNDDLFISKE
860 870 880 890 900
AQIRETETFS DSSPIEIIDE FPTLISSKTD SFSKLAREYT DLEVSHKSEI
910 920 930 940 950
ANAPDGAGSL PCTELPHDLS LKNIQPKVEE KISFSDDFSK NGSATSKVLL
960 970 980 990 1000
LPPDVSALAT QAEIESIVKP KVLVKEAEKK LPSDTEKEDR SPSAIFSAEL
1010 1020 1030 1040 1050
SKTSVVDLLY WRDIKKTGVV FGASLFLLLS LTVFSIVSVT AYIALALLSV
1060 1070 1080 1090 1100
TISFRIYKGV IQAIQKSDEG HPFRAYLESE VAISEELVQK YSNSALGHVN
1110 1120 1130 1140 1150
CTIKELRRLF LVDDLVDSLK FAVLMWVFTY VGALFNGLTL LILALISLFS
1160 1170 1180 1190
VPVIYERHQA QIDHYLGLAN KNVKDAMAKI QAKIPGLKRK AE
Length:1,192
Mass (Da):129,931
Last modified:November 16, 2001 - v2
Checksum:iCDE239BBF31589CA
GO
Isoform 2 (identifier: Q9NQC3-2) [UniParc]FASTAAdd to Basket

Also known as: RTN 4B, ASY, Nogo-B, RTN-xS, Foocen-M

The sequence of this isoform differs from the canonical sequence as follows:
     186-1004: Missing.

Show »
Length:373
Mass (Da):40,318
Checksum:i8A19379EF91A59B4
GO
Isoform 3 (identifier: Q9NQC3-3) [UniParc]FASTAAdd to Basket

Also known as: RTN 4C, Nogo-C, Foocen-S

The sequence of this isoform differs from the canonical sequence as follows:
     1-993: Missing.
     994-1004: AIFSAELSKTS → MDGQKKNWKDK

Show »
Length:199
Mass (Da):22,395
Checksum:iC60161DF3FB34D80
GO
Isoform 4 (identifier: Q9NQC3-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-289: Missing.

Show »
Length:960
Mass (Da):106,360
Checksum:i51B5E94CF103BA74
GO
Isoform 5 (identifier: Q9NQC3-5) [UniParc]FASTAAdd to Basket

Also known as: RTN4-B2

The sequence of this isoform differs from the canonical sequence as follows:
     205-1004: Missing.

Show »
Length:392
Mass (Da):42,274
Checksum:iD7B2AA5E839E58AD
GO
Isoform 6 (identifier: Q9NQC3-6) [UniParc]FASTAAdd to Basket

Also known as: Rtn-T

The sequence of this isoform differs from the canonical sequence as follows:
     1-206: Missing.

Show »
Length:986
Mass (Da):108,450
Checksum:i0CDE8F647036415A
GO

Sequence cautioni

The sequence AAD39920.1 differs from that shown. Reason: Frameshift at positions 1149 and 1156.
The sequence AAG43160.1 differs from that shown. Reason: Frameshift at positions 684 and 700.
The sequence AAG43160.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA74909.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071S → C in BAA83712. 1 PublicationCurated
Sequence conflicti135 – 1351E → Q in BAA83712. 1 PublicationCurated
Sequence conflicti458 – 4581S → P in CAB99248. (PubMed:10667780)Curated
Sequence conflicti564 – 5641N → S in AAK20831. (PubMed:11866689)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti357 – 3571D → V.
Corresponds to variant rs11677099 [ dbSNP | Ensembl ].
VAR_053633
Natural varianti429 – 4291L → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035904
Natural varianti899 – 8991E → Q.
Corresponds to variant rs6757519 [ dbSNP | Ensembl ].
VAR_053634
Natural varianti920 – 9201S → C.
Corresponds to variant rs6757705 [ dbSNP | Ensembl ].
VAR_053635

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 993993Missing in isoform 3. 8 PublicationsVSP_005652Add
BLAST
Alternative sequencei1 – 206206Missing in isoform 6. 2 PublicationsVSP_037112Add
BLAST
Alternative sequencei58 – 289232Missing in isoform 4. 1 PublicationVSP_005654Add
BLAST
Alternative sequencei186 – 1004819Missing in isoform 2. 7 PublicationsVSP_005655Add
BLAST
Alternative sequencei205 – 1004800Missing in isoform 5. 2 PublicationsVSP_037113Add
BLAST
Alternative sequencei994 – 100411AIFSAELSKTS → MDGQKKNWKDK in isoform 3. 8 PublicationsVSP_005653Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF087901 mRNA. Translation: AAG12205.1.
AF148537 mRNA. Translation: AAG12176.1.
AF148538 mRNA. Translation: AAG12177.1.
AJ251383 mRNA. Translation: CAB99248.1.
AJ251384 mRNA. Translation: CAB99249.1.
AJ251385 mRNA. Translation: CAB99250.1.
AB040462 mRNA. Translation: BAB18927.1.
AB040463 mRNA. Translation: BAB18928.1.
AF333336 mRNA. Translation: AAK20831.1.
AY102285 Genomic DNA. Translation: AAM64240.1.
AY102285 Genomic DNA. Translation: AAM64241.1.
AY102285 Genomic DNA. Translation: AAM64242.1.
AY102285 Genomic DNA. Translation: AAM64243.1.
AY102285 Genomic DNA. Translation: AAM64244.1.
AY102276 mRNA. Translation: AAM64245.1.
AY102277 mRNA. Translation: AAM64246.1.
AY102278 mRNA. Translation: AAM64247.1.
AY102279 mRNA. Translation: AAM64248.1.
AY123245 mRNA. Translation: AAM64249.1.
AY123246 mRNA. Translation: AAM64250.1.
AY123247 mRNA. Translation: AAM64251.1.
AY123248 mRNA. Translation: AAM64252.1.
AY123249 mRNA. Translation: AAM64253.1.
AY123250 mRNA. Translation: AAM64254.1.
AB015639 mRNA. Translation: BAA83712.1.
AF077050 mRNA. Translation: AAD27783.1.
AF132047 mRNA. Translation: AAD31021.1.
AF132048 mRNA. Translation: AAD31022.1.
AF320999 mRNA. Translation: AAG40878.1.
AB020693 mRNA. Translation: BAA74909.2. Different initiation.
AF125103 mRNA. Translation: AAD39920.1. Frameshift.
AF177332 mRNA. Translation: AAG17976.1.
AC013414 Genomic DNA. No translation available.
AC092461 Genomic DNA. No translation available.
AC093165 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00115.1.
CH471053 Genomic DNA. Translation: EAX00116.1.
CH471053 Genomic DNA. Translation: EAX00117.1.
CH471053 Genomic DNA. Translation: EAX00118.1.
CH471053 Genomic DNA. Translation: EAX00119.1.
CH471053 Genomic DNA. Translation: EAX00121.1.
CH471053 Genomic DNA. Translation: EAX00122.1.
CH471053 Genomic DNA. Translation: EAX00123.1.
CH471053 Genomic DNA. Translation: EAX00124.1.
CH471053 Genomic DNA. Translation: EAX00125.1.
CH471053 Genomic DNA. Translation: EAX00127.1.
CH471053 Genomic DNA. Translation: EAX00130.1.
CH471053 Genomic DNA. Translation: EAX00132.1.
BC001035 mRNA. Translation: AAH01035.1.
BC007109 mRNA. Translation: AAH07109.1.
BC010737 mRNA. Translation: AAH10737.1.
BC012619 mRNA. Translation: AAH12619.1.
BC014366 mRNA. Translation: AAH14366.1.
BC016165 mRNA. Translation: AAH16165.1.
BC026788 mRNA. Translation: AAH26788.1.
BC068991 mRNA. Translation: AAH68991.1.
BC150182 mRNA. Translation: AAI50183.1.
BC152425 mRNA. Translation: AAI52426.1.
BC152555 mRNA. Translation: AAI52556.1.
AF063601 mRNA. Translation: AAG43160.1. Sequence problems.
CCDSiCCDS1851.1. [Q9NQC3-2]
CCDS1852.1. [Q9NQC3-6]
CCDS42683.1. [Q9NQC3-5]
CCDS42684.1. [Q9NQC3-1]
CCDS42685.1. [Q9NQC3-3]
RefSeqiNP_008939.1. NM_007008.2. [Q9NQC3-3]
NP_065393.1. NM_020532.4. [Q9NQC3-1]
NP_722550.1. NM_153828.2. [Q9NQC3-2]
NP_997403.1. NM_207520.1. [Q9NQC3-5]
NP_997404.1. NM_207521.1. [Q9NQC3-6]
XP_005264491.1. XM_005264434.2. [Q9NQC3-6]
UniGeneiHs.637850.

Genome annotation databases

EnsembliENST00000317610; ENSP00000322147; ENSG00000115310. [Q9NQC3-2]
ENST00000337526; ENSP00000337838; ENSG00000115310. [Q9NQC3-1]
ENST00000357376; ENSP00000349944; ENSG00000115310. [Q9NQC3-6]
ENST00000357732; ENSP00000350365; ENSG00000115310. [Q9NQC3-5]
ENST00000394609; ENSP00000378107; ENSG00000115310. [Q9NQC3-3]
ENST00000394611; ENSP00000378109; ENSG00000115310. [Q9NQC3-6]
ENST00000404909; ENSP00000385650; ENSG00000115310. [Q9NQC3-6]
ENST00000405240; ENSP00000384471; ENSG00000115310. [Q9NQC3-6]
GeneIDi57142.
KEGGihsa:57142.
UCSCiuc002ryc.3. human. [Q9NQC3-3]
uc002ryd.3. human. [Q9NQC3-1]
uc002ryf.3. human. [Q9NQC3-5]
uc002ryg.3. human. [Q9NQC3-2]

Polymorphism databases

DMDMi17369290.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Protein Spotlight

Nerve regrowth: nipped by a no-go - Issue 69 of April 2006

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF087901 mRNA. Translation: AAG12205.1 .
AF148537 mRNA. Translation: AAG12176.1 .
AF148538 mRNA. Translation: AAG12177.1 .
AJ251383 mRNA. Translation: CAB99248.1 .
AJ251384 mRNA. Translation: CAB99249.1 .
AJ251385 mRNA. Translation: CAB99250.1 .
AB040462 mRNA. Translation: BAB18927.1 .
AB040463 mRNA. Translation: BAB18928.1 .
AF333336 mRNA. Translation: AAK20831.1 .
AY102285 Genomic DNA. Translation: AAM64240.1 .
AY102285 Genomic DNA. Translation: AAM64241.1 .
AY102285 Genomic DNA. Translation: AAM64242.1 .
AY102285 Genomic DNA. Translation: AAM64243.1 .
AY102285 Genomic DNA. Translation: AAM64244.1 .
AY102276 mRNA. Translation: AAM64245.1 .
AY102277 mRNA. Translation: AAM64246.1 .
AY102278 mRNA. Translation: AAM64247.1 .
AY102279 mRNA. Translation: AAM64248.1 .
AY123245 mRNA. Translation: AAM64249.1 .
AY123246 mRNA. Translation: AAM64250.1 .
AY123247 mRNA. Translation: AAM64251.1 .
AY123248 mRNA. Translation: AAM64252.1 .
AY123249 mRNA. Translation: AAM64253.1 .
AY123250 mRNA. Translation: AAM64254.1 .
AB015639 mRNA. Translation: BAA83712.1 .
AF077050 mRNA. Translation: AAD27783.1 .
AF132047 mRNA. Translation: AAD31021.1 .
AF132048 mRNA. Translation: AAD31022.1 .
AF320999 mRNA. Translation: AAG40878.1 .
AB020693 mRNA. Translation: BAA74909.2 . Different initiation.
AF125103 mRNA. Translation: AAD39920.1 . Frameshift.
AF177332 mRNA. Translation: AAG17976.1 .
AC013414 Genomic DNA. No translation available.
AC092461 Genomic DNA. No translation available.
AC093165 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00115.1 .
CH471053 Genomic DNA. Translation: EAX00116.1 .
CH471053 Genomic DNA. Translation: EAX00117.1 .
CH471053 Genomic DNA. Translation: EAX00118.1 .
CH471053 Genomic DNA. Translation: EAX00119.1 .
CH471053 Genomic DNA. Translation: EAX00121.1 .
CH471053 Genomic DNA. Translation: EAX00122.1 .
CH471053 Genomic DNA. Translation: EAX00123.1 .
CH471053 Genomic DNA. Translation: EAX00124.1 .
CH471053 Genomic DNA. Translation: EAX00125.1 .
CH471053 Genomic DNA. Translation: EAX00127.1 .
CH471053 Genomic DNA. Translation: EAX00130.1 .
CH471053 Genomic DNA. Translation: EAX00132.1 .
BC001035 mRNA. Translation: AAH01035.1 .
BC007109 mRNA. Translation: AAH07109.1 .
BC010737 mRNA. Translation: AAH10737.1 .
BC012619 mRNA. Translation: AAH12619.1 .
BC014366 mRNA. Translation: AAH14366.1 .
BC016165 mRNA. Translation: AAH16165.1 .
BC026788 mRNA. Translation: AAH26788.1 .
BC068991 mRNA. Translation: AAH68991.1 .
BC150182 mRNA. Translation: AAI50183.1 .
BC152425 mRNA. Translation: AAI52426.1 .
BC152555 mRNA. Translation: AAI52556.1 .
AF063601 mRNA. Translation: AAG43160.1 . Sequence problems.
CCDSi CCDS1851.1. [Q9NQC3-2 ]
CCDS1852.1. [Q9NQC3-6 ]
CCDS42683.1. [Q9NQC3-5 ]
CCDS42684.1. [Q9NQC3-1 ]
CCDS42685.1. [Q9NQC3-3 ]
RefSeqi NP_008939.1. NM_007008.2. [Q9NQC3-3 ]
NP_065393.1. NM_020532.4. [Q9NQC3-1 ]
NP_722550.1. NM_153828.2. [Q9NQC3-2 ]
NP_997403.1. NM_207520.1. [Q9NQC3-5 ]
NP_997404.1. NM_207521.1. [Q9NQC3-6 ]
XP_005264491.1. XM_005264434.2. [Q9NQC3-6 ]
UniGenei Hs.637850.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2G31 NMR - A 1055-1114 [» ]
2JV5 NMR - A 1055-1108 [» ]
DisProti DP00524.
ProteinModelPortali Q9NQC3.
SMRi Q9NQC3. Positions 1055-1114.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121400. 71 interactions.
IntActi Q9NQC3. 26 interactions.
MINTi MINT-154434.

PTM databases

PhosphoSitei Q9NQC3.

Polymorphism databases

DMDMi 17369290.

Proteomic databases

MaxQBi Q9NQC3.
PaxDbi Q9NQC3.
PRIDEi Q9NQC3.

Protocols and materials databases

DNASUi 57142.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000317610 ; ENSP00000322147 ; ENSG00000115310 . [Q9NQC3-2 ]
ENST00000337526 ; ENSP00000337838 ; ENSG00000115310 . [Q9NQC3-1 ]
ENST00000357376 ; ENSP00000349944 ; ENSG00000115310 . [Q9NQC3-6 ]
ENST00000357732 ; ENSP00000350365 ; ENSG00000115310 . [Q9NQC3-5 ]
ENST00000394609 ; ENSP00000378107 ; ENSG00000115310 . [Q9NQC3-3 ]
ENST00000394611 ; ENSP00000378109 ; ENSG00000115310 . [Q9NQC3-6 ]
ENST00000404909 ; ENSP00000385650 ; ENSG00000115310 . [Q9NQC3-6 ]
ENST00000405240 ; ENSP00000384471 ; ENSG00000115310 . [Q9NQC3-6 ]
GeneIDi 57142.
KEGGi hsa:57142.
UCSCi uc002ryc.3. human. [Q9NQC3-3 ]
uc002ryd.3. human. [Q9NQC3-1 ]
uc002ryf.3. human. [Q9NQC3-5 ]
uc002ryg.3. human. [Q9NQC3-2 ]

Organism-specific databases

CTDi 57142.
GeneCardsi GC02M055199.
H-InvDB HIX0002059.
HGNCi HGNC:14085. RTN4.
HPAi CAB005388.
HPA023977.
MIMi 604475. gene.
neXtProti NX_Q9NQC3.
PharmGKBi PA34883.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG306139.
GeneTreei ENSGT00390000009934.
HOVERGENi HBG023134.
InParanoidi Q9NQC3.
OMAi NIHRVAT.
OrthoDBi EOG7CZK7J.
PhylomeDBi Q9NQC3.
TreeFami TF105431.

Enzyme and pathway databases

Reactomei REACT_13815. Axonal growth inhibition (RHOA activation).

Miscellaneous databases

ChiTaRSi RTN4. human.
EvolutionaryTracei Q9NQC3.
GeneWikii Reticulon_4.
GenomeRNAii 57142.
NextBioi 63075.
PMAP-CutDB Q9NQC3.
PROi Q9NQC3.
SOURCEi Search...

Gene expression databases

Bgeei Q9NQC3.
ExpressionAtlasi Q9NQC3. baseline and differential.
Genevestigatori Q9NQC3.

Family and domain databases

InterProi IPR003388. Reticulon.
[Graphical view ]
PANTHERi PTHR10994. PTHR10994. 1 hit.
Pfami PF02453. Reticulon. 1 hit.
[Graphical view ]
PROSITEi PS50845. RETICULON. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Assignment of the human reticulon 4 gene (RTN4) to chromosome 2p14-->2p13 by radiation hybrid mapping."
    Yang J., Yu L., Bi A.D., Zhao S.-Y.
    Cytogenet. Cell Genet. 88:101-102(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
  3. "A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity."
    Tagami S., Eguchi Y., Kinoshita M., Takeda M., Tsujimoto Y.
    Oncogene 19:5736-5746(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
    Tissue: Testis.
  5. "Genomic structure and functional characterisation of the promoters of human and mouse nogo/rtn4."
    Oertle T., Huber C., van der Putten H., Schwab M.E.
    J. Mol. Biol. 325:299-323(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 5 AND 6).
  6. "Isolation of a cell death-inducing gene."
    Yutsudo M.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Fibroblast.
  7. "Human neuroendocrine-specific protein C (NSP) homolog gene."
    Song H., Peng Y., Zhou J., Huang Q., Dai M., Mao Y.M., Yu Y., Xu X., Luo B., Hu R., Chen J.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Pituitary.
  8. "Cloning of a member of the reticulon gene family in human."
    Ito T., Schwartz S.M.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
    Tissue: Placenta and Skeletal muscle.
  9. "Developmentally-regulated alternative splicing in a novel Nogo-A."
    Jin W.-L., Ju G.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  10. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  11. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Umbilical cord blood.
  12. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  13. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  14. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  15. "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] (ISOFORMS 2; 3 AND 5).
    Tissue: Brain, Eye, Kidney, Ovary, Pancreas, Placenta and Skeletal muscle.
  16. Bienvenut W.V.
    Submitted (JAN-2010) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-24; 92-104; 1075-1090 AND 1158-1171, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  17. Mao Y.M., Xie Y., Zheng Z.H.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-1192 (ISOFORMS 1/4).
    Tissue: Fetal brain.
  18. "Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein."
    GrandPre T., Nakamura F., Vartanian T., Strittmatter S.M.
    Nature 403:439-444(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY, FUNCTION.
    Tissue: Brain.
  19. "Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration."
    Fournier A.E., GrandPre T., Strittmatter S.M.
    Nature 409:341-346(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Tissue: Brain.
  20. "Nogos and the Nogo-66 receptor: factors inhibiting CNS neuron regeneration."
    Ng C.E.L., Tang B.L.
    J. Neurosci. Res. 67:559-565(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  21. Cited for: INTERACTION WITH RTN3.
  22. "Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation."
    He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.
    Nat. Med. 10:959-965(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BACE1.
  23. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein."
    Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.
    Eur. J. Neurosci. 24:1237-1244(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BACE1 AND BACE2, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  25. "Mapping of interaction domains mediating binding between BACE1 and RTN/Nogo proteins."
    He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.
    J. Mol. Biol. 363:625-634(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RTN3.
  26. "Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells."
    Miao R.Q., Gao Y., Harrison K.D., Prendergast J., Acevedo L.M., Yu J., Hu F., Strittmatter S.M., Sessa W.C.
    Proc. Natl. Acad. Sci. U.S.A. 103:10997-11002(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NGBR.
  27. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "A class of dynamin-like GTPases involved in the generation of the tubular ER network."
    Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A., Rapoport T.A., Blackstone C.
    Cell 138:549-561(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATL1.
  31. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  33. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "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, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-429.

Entry informationi

Entry nameiRTN4_HUMAN
AccessioniPrimary (citable) accession number: Q9NQC3
Secondary accession number(s): O94962
, Q7L7Q5, Q7L7Q6, Q7L7Q8, Q8IUA4, Q96B16, Q9BXG5, Q9H212, Q9H3I3, Q9UQ42, Q9Y293, Q9Y2Y7, Q9Y5U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: October 29, 2014
This is version 151 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3