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Q99K48

- NONO_MOUSE

UniProt

Q99K48 - NONO_MOUSE

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Protein

Non-POU domain-containing octamer-binding protein

Gene
Nono
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double-stranded DNA. Also binds single-stranded DNA and RNA at a site independent of the duplex site. Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. Together with PSPC1, required for the formation of nuclear paraspeckles. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends. In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer.2 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. nucleotide binding Source: InterPro
  3. protein binding Source: IntAct
  4. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. circadian rhythm Source: UniProtKB
  2. DNA recombination Source: UniProtKB-KW
  3. DNA repair Source: UniProtKB-KW
  4. mRNA processing Source: UniProtKB-KW
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. RNA splicing Source: UniProtKB-KW
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, DNA damage, DNA recombination, DNA repair, mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-POU domain-containing octamer-binding protein
Short name:
NonO protein
Gene namesi
Name:Nono
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1855692. Nono.

Subcellular locationi

Nucleus. Nucleusnucleolus By similarity. Nucleus speckle By similarity
Note: Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles By similarity.1 Publication

GO - Cellular componenti

  1. nuclear matrix Source: Ensembl
  2. nuclear speck Source: UniProtKB-SubCell
  3. nucleolus Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB
  5. paraspeckles Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Non-POU domain-containing octamer-binding proteinPRO_0000081684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei5 – 51N6-acetyllysine1 Publication
Modified residuei11 – 111N6-acetyllysine1 Publication
Modified residuei149 – 1491Phosphoserine By similarity
Modified residuei200 – 2001N6-acetyllysine1 Publication
Modified residuei297 – 2971N6-acetyllysine1 Publication
Modified residuei373 – 3731N6-acetyllysine1 Publication
Modified residuei430 – 4301Phosphothreonine By similarity
Modified residuei442 – 4421Phosphothreonine By similarity
Modified residuei452 – 4521Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99K48.
PaxDbiQ99K48.
PRIDEiQ99K48.

PTM databases

PhosphoSiteiQ99K48.

Expressioni

Tissue specificityi

Expressed in liver and suprachiasmatic nuclei, hippocampus and neocortex (at protein level). Detected in testis and kidney.

Gene expression databases

ArrayExpressiQ99K48.
BgeeiQ99K48.
GenevestigatoriQ99K48.

Interactioni

Subunit structurei

Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. NONO is a component of spliceosome and U5.4/6 snRNP complexes. Forms heterodimers with PSPC1; this involves formation of a coiled coil domain by helices from both proteins. Interacts with PSPC1 and SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Part of a complex consisting of SFPQ, NONO and NR5A1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SPI1. Interacts with RNF43. Interacts with PER1 and PER2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Spi1P174333EBI-607499,EBI-607588

Protein-protein interaction databases

BioGridi207330. 15 interactions.
IntActiQ99K48. 5 interactions.
MINTiMINT-1751475.

Structurei

Secondary structure

1
473
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi77 – 826
Helixi89 – 957
Helixi97 – 993
Beta strandi103 – 1086
Turni109 – 1124
Beta strandi113 – 1175
Beta strandi119 – 1213
Helixi122 – 13110
Beta strandi142 – 1476

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPJNMR-A68-153[»]
2RS8NMR-A68-153[»]
ProteinModelPortaliQ99K48.
SMRiQ99K48. Positions 20-306.

Miscellaneous databases

EvolutionaryTraceiQ99K48.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 14368RRM 1Add
BLAST
Domaini150 – 23182RRM 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 375320DBHS By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili270 – 374105 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi29 – 3810Poly-Gln
Compositional biasi39 – 446Poly-Pro
Compositional biasi350 – 3534Poly-Arg

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG298586.
GeneTreeiENSGT00390000005004.
HOVERGENiHBG009801.
InParanoidiQ99K48.
KOiK13214.
OMAiNQQYHKE.
TreeFamiTF315795.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99K48-1) [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

MQSNKAFNLE KQNHTPRKHH QHHHQQHHQQ QQQQQQQQPP PPIPANGQQA    50
SSQNEGLTID LKNFRKPGEK TFTQRSRLFV GNLPPDITEE EMRKLFEKYG 100
KAGEVFIHKD KGFGFIRLET RTLAEIAKVE LDNMPLRGKQ LRVRFACHSA 150
SLTVRNLPQY VSNELLEEAF SVFGQVERAV VIVDDRGRPS GKGIVEFSGK 200
PAARKALDRC SEGSFLLTTF PRPVTVEPMD QLDDEEGLPE KLVIKNQQFH 250
KEREQPPRFA QPGSFEYEYA MRWKALIEME KQQQDQVDRN IKEAREKLEM 300
EMEAARHEHQ VMLMRQDLMR RQEELRRMEE LHNQEVQKRK QLELRQEEER 350
RRREEEMRRQ QEEMMRRQQE GFKGTFPDAR EQEIRMGQMA MGGAMGINNR 400
GAMPPAPVPP GTPAPPGPAT MMPDGTLGLT PPTTERFGQA ATMEGIGAIG 450
GTPPAFNRPA PGAEFAPNKR RRY 473
Length:473
Mass (Da):54,541
Last modified:July 5, 2005 - v3
Checksum:iF65E6AE25D471A38
GO
Isoform 2 (identifier: Q99K48-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     220-473: Missing.

Note: No experimental confirmation available.

Show »
Length:219
Mass (Da):24,969
Checksum:iCFF17042BD1E721E
GO

Sequence cautioni

The sequence BAB28857.1 differs from that shown. Reason: Frameshift at position 187.
The sequence BAB23598.1 differs from that shown. Reason: Erroneous termination at position 258. Translated as Arg.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei220 – 473254Missing in isoform 2. VSP_013981Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761S → T in BAB28857. 1 Publication
Sequence conflicti117 – 1171R → N in BAB28857. 1 Publication
Sequence conflicti127 – 1271A → V in AAB27887. 1 Publication
Sequence conflicti153 – 1531T → K in BAB28857. 1 Publication
Sequence conflicti167 – 1671E → G in BAB28857. 1 Publication
Sequence conflicti183 – 1831V → E in BAB28857. 1 Publication
Sequence conflicti188 – 1881R → W in BAB28857. 1 Publication
Sequence conflicti203 – 2042AR → VL in BAB28857. 1 Publication
Sequence conflicti222 – 2221R → W in AAB27887. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S64860 mRNA. Translation: AAB27887.1.
AK004830 mRNA. Translation: BAB23598.1. Sequence problems.
AK013444 mRNA. Translation: BAB28857.1. Sequence problems.
AK028338 mRNA. Translation: BAC25890.1.
BC005465 mRNA. Translation: AAH05465.1.
BC083074 mRNA. Translation: AAH83074.1.
CCDSiCCDS30316.1. [Q99K48-1]
RefSeqiNP_001239447.1. NM_001252518.1. [Q99K48-1]
NP_075633.2. NM_023144.2. [Q99K48-1]
UniGeneiMm.280069.
Mm.475350.

Genome annotation databases

EnsembliENSMUST00000033673; ENSMUSP00000033673; ENSMUSG00000031311. [Q99K48-1]
GeneIDi53610.
KEGGimmu:53610.
UCSCiuc009txr.2. mouse. [Q99K48-2]
uc009txs.2. mouse. [Q99K48-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S64860 mRNA. Translation: AAB27887.1 .
AK004830 mRNA. Translation: BAB23598.1 . Sequence problems.
AK013444 mRNA. Translation: BAB28857.1 . Sequence problems.
AK028338 mRNA. Translation: BAC25890.1 .
BC005465 mRNA. Translation: AAH05465.1 .
BC083074 mRNA. Translation: AAH83074.1 .
CCDSi CCDS30316.1. [Q99K48-1 ]
RefSeqi NP_001239447.1. NM_001252518.1. [Q99K48-1 ]
NP_075633.2. NM_023144.2. [Q99K48-1 ]
UniGenei Mm.280069.
Mm.475350.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CPJ NMR - A 68-153 [» ]
2RS8 NMR - A 68-153 [» ]
ProteinModelPortali Q99K48.
SMRi Q99K48. Positions 20-306.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207330. 15 interactions.
IntActi Q99K48. 5 interactions.
MINTi MINT-1751475.

PTM databases

PhosphoSitei Q99K48.

Proteomic databases

MaxQBi Q99K48.
PaxDbi Q99K48.
PRIDEi Q99K48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033673 ; ENSMUSP00000033673 ; ENSMUSG00000031311 . [Q99K48-1 ]
GeneIDi 53610.
KEGGi mmu:53610.
UCSCi uc009txr.2. mouse. [Q99K48-2 ]
uc009txs.2. mouse. [Q99K48-1 ]

Organism-specific databases

CTDi 4841.
MGIi MGI:1855692. Nono.

Phylogenomic databases

eggNOGi NOG298586.
GeneTreei ENSGT00390000005004.
HOVERGENi HBG009801.
InParanoidi Q99K48.
KOi K13214.
OMAi NQQYHKE.
TreeFami TF315795.

Miscellaneous databases

ChiTaRSi NONO. mouse.
EvolutionaryTracei Q99K48.
NextBioi 310319.
PROi Q99K48.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99K48.
Bgeei Q99K48.
Genevestigatori Q99K48.

Family and domain databases

Gene3Di 3.30.70.330. 3 hits.
InterProi IPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "NonO, a non-POU-domain-containing, octamer-binding protein, is the mammalian homolog of Drosophila nonAdiss."
    Yang Y.-S., Hanke J.H., Carayannopoulos L., Craft C.M., Capra J.D., Tucker P.W.
    Mol. Cell. Biol. 13:5593-5603(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 195-201; 260-274; 300-306; 387-400 AND 438-445, FUNCTION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Embryo and Lung.
  3. "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] (ISOFORM 1).
    Strain: C57BL/6 and FVB/N.
    Tissue: Mammary tumor and Olfactory epithelium.
  4. "The transcription factor Spi-1/PU.1 binds RNA and interferes with the RNA-binding protein p54nrb."
    Hallier M., Tavitian A., Moreau-Gachelin F.
    J. Biol. Chem. 271:11177-11181(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 298-312, INTERACTION WITH SPI1.
  5. "The intracisternal A-particle proximal enhancer-binding protein activates transcription and is identical to the RNA- and DNA-binding protein p54nrb/NonO."
    Basu A., Dong B., Krainer A.R., Howe C.C.
    Mol. Cell. Biol. 17:677-686(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, DNA-BINDING.
  6. "Expression and functional significance of mouse paraspeckle protein 1 on spermatogenesis."
    Myojin R., Kuwahara S., Yasaki T., Matsunaga T., Sakurai T., Kimura M., Uesugi S., Kurihara Y.
    Biol. Reprod. 71:926-932(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSPC1.
  7. "PERIOD1-associated proteins modulate the negative limb of the mammalian circadian oscillator."
    Brown S.A., Ripperger J., Kadener S., Fleury-Olela F., Vilbois F., Rosbash M., Schibler U.
    Science 308:693-696(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Distinct roles of DBHS family members in the circadian transcriptional feedback loop."
    Kowalska E., Ripperger J.A., Muheim C., Maier B., Kurihara Y., Fox A.H., Kramer A., Brown S.A.
    Mol. Cell. Biol. 32:4585-4594(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PER1 AND PER2.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-5; LYS-11; LYS-200; LYS-297 AND LYS-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. "Solution structure of the N-terminal RNA recognition motif of NonO."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 68-153.

Entry informationi

Entry nameiNONO_MOUSE
AccessioniPrimary (citable) accession number: Q99K48
Secondary accession number(s): Q63887, Q9CYQ4, Q9DBP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2005
Last modified: September 3, 2014
This is version 126 of the entry and version 3 of the sequence. [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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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