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P35564

- CALX_MOUSE

UniProt

P35564 - CALX_MOUSE

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Protein

Calnexin

Gene

Canx

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

Functioni

Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi75 – 751Calcium; via carbonyl oxygenBy similarity
Metal bindingi118 – 1181Calcium; via carbonyl oxygenBy similarity
Binding sitei165 – 1651CarbohydrateBy similarity
Binding sitei167 – 1671CarbohydrateBy similarity
Binding sitei186 – 1861CarbohydrateBy similarity
Binding sitei217 – 2171CarbohydrateBy similarity
Metal bindingi437 – 4371CalciumBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. carbohydrate binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. aging Source: Ensembl
  2. chaperone-mediated protein folding Source: Ensembl
  3. clathrin-mediated endocytosis Source: UniProtKB
  4. synaptic vesicle endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_198616. Calnexin/calreticulin cycle.
REACT_246972. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
Calnexin
Gene namesi
Name:Canx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:88261. Canx.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endoplasmic reticulum By similarity. Melanosome By similarity
Note: The palmitoylated form preferentially localizes to the perinuclear rough ER (By similarity). When bound to CD3 epsilon chains, calnexin's ER retention signal can be masked, permitting it to escape ER retention.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 482462LumenalSequence AnalysisAdd
BLAST
Transmembranei483 – 50321HelicalSequence AnalysisAdd
BLAST
Topological domaini504 – 59188CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon Source: Ensembl
  2. dendrite cytoplasm Source: Ensembl
  3. dendritic spine Source: Ensembl
  4. endoplasmic reticulum Source: MGI
  5. extracellular vesicular exosome Source: Ensembl
  6. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  7. integral component of membrane Source: MGI
  8. membrane Source: MGI
  9. neuronal cell body Source: Ensembl
  10. protein complex Source: Ensembl
  11. ribosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 591571CalnexinPRO_0000004199Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei138 – 1381N6-acetyllysineBy similarity
Disulfide bondi161 ↔ 195By similarity
Disulfide bondi361 ↔ 367By similarity
Lipidationi503 – 5031S-palmitoyl cysteineBy similarity
Lipidationi504 – 5041S-palmitoyl cysteineBy similarity
Modified residuei553 – 5531Phosphoserine2 Publications
Modified residuei561 – 5611PhosphothreonineBy similarity
Modified residuei563 – 5631Phosphoserine; by MAPK31 Publication
Modified residuei582 – 5821Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated at Ser-563 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes (By similarity).By similarity
Palmitoylation by DHHC6 leads to the preferential localization to the perinuclear rough ER. It mediates the association of calnexin with the ribosome-translocon complex (RTC) which is required for efficient folding of glycosylated proteins (By similarity).By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP35564.
PaxDbiP35564.
PRIDEiP35564.

PTM databases

PhosphoSiteiP35564.

Miscellaneous databases

PMAP-CutDBP35564.

Expressioni

Gene expression databases

BgeeiP35564.
CleanExiMM_CANX.
ExpressionAtlasiP35564. baseline and differential.
GenevestigatoriP35564.

Interactioni

Subunit structurei

Interacts with MAPK3/ERK1 (By similarity). Interacts with KCNH2 (By similarity). Associates with ribosomes. The palmitoylated form interacts with the ribosome-translocon complex component SSR1, promoting efficient folding of glycoproteins (By similarity). Interacts with SERPINA2P/SERPINA2 and with the S and Z variants of SERPINA1 (By similarity). Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP (By similarity). Interacts with SGIP1; involved in negative regulation of endocytosis. Interacts with PPIB.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Sgip1Q8VD373EBI-738422,EBI-776269

Protein-protein interaction databases

BioGridi198467. 8 interactions.
IntActiP35564. 17 interactions.
MINTiMINT-1862151.

Structurei

3D structure databases

ProteinModelPortaliP35564.
SMRiP35564. Positions 61-458.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati279 – 291131-1Add
BLAST
Repeati296 – 308131-2Add
BLAST
Repeati315 – 327131-3Add
BLAST
Repeati334 – 346131-4Add
BLAST
Repeati349 – 359112-1Add
BLAST
Repeati368 – 378112-2Add
BLAST
Repeati382 – 392112-3Add
BLAST
Repeati396 – 406112-4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni277 – 410134P domain (Extended arm)By similarityAdd
BLAST
Regioni279 – 346684 X approximate repeatsAdd
BLAST
Regioni327 – 36034Interaction with PPIBBy similarityAdd
BLAST
Regioni349 – 406584 X approximate repeatsAdd
BLAST
Regioni504 – 59188Sufficient to mediate interaction with SGIP1Add
BLAST

Sequence similaritiesi

Belongs to the calreticulin family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG305105.
HOGENOMiHOG000192436.
HOVERGENiHBG005407.
InParanoidiP35564.
KOiK08054.
OMAiEAHDGHD.
OrthoDBiEOG77126Z.
PhylomeDBiP35564.
TreeFamiTF300618.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 1 hit.
[Graphical view]
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P35564-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEGKWLLCLL LVLGTAAVEA HDGHDDDAID IEDDLDDVIE EVEDSKSKSD
60 70 80 90 100
ASTPPSPKVT YKAPVPTGEV YFADSFDRGS LSGWILSKAK KDDTDDEIAK
110 120 130 140 150
YDGKWEVDEM KETKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ
160 170 180 190 200
YEVNFQNGIE CGGAYVKLLS KTAELSLDQF HDKTPYTIMF GPDKCGEDYK
210 220 230 240 250
LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE
260 270 280 290 300
ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIADPDAV
310 320 330 340 350
KPDDWDEDAP SKIPDEEATK PEGWLDDEPE YIPDPDAEKP EDWDEDMDGE
360 370 380 390 400
WEAPQIANPK CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP
410 420 430 440 450
RKIPNPDFFE DLEPFKMTPF SAIGLELWSM TSDIFFDNFI ISGDRRVVDD
460 470 480 490 500
WANDGWGLKK AADGAAEPGV VLQMLEAAEE RPWLWVVYIL TVALPVFLVI
510 520 530 540 550
LFCCSGKKQS NAMEYKKTDA PQPDVKDEEG KEEEKNKRDE EEEEEKLEEK
560 570 580 590
QKSDAEEDGV TGSQDEEDSK PKAEEDEILN RSPRNRKPRR E
Length:591
Mass (Da):67,278
Last modified:June 1, 1994 - v1
Checksum:i0D9F8FE03434BADC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti416 – 4161K → R in AAA62450. (PubMed:8148318)Curated
Sequence conflicti468 – 4681P → L in AAA62450. (PubMed:8148318)Curated
Sequence conflicti472 – 4721L → G in AAA62450. (PubMed:8148318)Curated
Sequence conflicti538 – 5381R → G in AAA62450. (PubMed:8148318)Curated
Sequence conflicti560 – 5601V → G in AAA62450. (PubMed:8148318)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18888 mRNA. Translation: AAA21014.1.
BC012408 mRNA. Translation: AAH12408.1.
BC040244 mRNA. Translation: AAH40244.1.
AK084175 mRNA. Translation: BAC39133.1.
L23865 mRNA. Translation: AAA62450.1.
CCDSiCCDS24633.1.
PIRiB54354.
RefSeqiNP_001103969.1. NM_001110499.1.
NP_001103970.1. NM_001110500.1.
NP_031623.1. NM_007597.3.
UniGeneiMm.248827.

Genome annotation databases

EnsembliENSMUST00000020637; ENSMUSP00000020637; ENSMUSG00000020368.
ENSMUST00000179865; ENSMUSP00000137440; ENSMUSG00000020368.
GeneIDi12330.
KEGGimmu:12330.
UCSCiuc007isf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18888 mRNA. Translation: AAA21014.1 .
BC012408 mRNA. Translation: AAH12408.1 .
BC040244 mRNA. Translation: AAH40244.1 .
AK084175 mRNA. Translation: BAC39133.1 .
L23865 mRNA. Translation: AAA62450.1 .
CCDSi CCDS24633.1.
PIRi B54354.
RefSeqi NP_001103969.1. NM_001110499.1.
NP_001103970.1. NM_001110500.1.
NP_031623.1. NM_007597.3.
UniGenei Mm.248827.

3D structure databases

ProteinModelPortali P35564.
SMRi P35564. Positions 61-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198467. 8 interactions.
IntActi P35564. 17 interactions.
MINTi MINT-1862151.

PTM databases

PhosphoSitei P35564.

Proteomic databases

MaxQBi P35564.
PaxDbi P35564.
PRIDEi P35564.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020637 ; ENSMUSP00000020637 ; ENSMUSG00000020368 .
ENSMUST00000179865 ; ENSMUSP00000137440 ; ENSMUSG00000020368 .
GeneIDi 12330.
KEGGi mmu:12330.
UCSCi uc007isf.2. mouse.

Organism-specific databases

CTDi 821.
MGIi MGI:88261. Canx.

Phylogenomic databases

eggNOGi NOG305105.
HOGENOMi HOG000192436.
HOVERGENi HBG005407.
InParanoidi P35564.
KOi K08054.
OMAi EAHDGHD.
OrthoDBi EOG77126Z.
PhylomeDBi P35564.
TreeFami TF300618.

Enzyme and pathway databases

Reactomei REACT_196550. MHC class II antigen presentation.
REACT_198616. Calnexin/calreticulin cycle.
REACT_246972. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSi Canx. mouse.
NextBioi 280926.
PMAP-CutDB P35564.
PROi P35564.
SOURCEi Search...

Gene expression databases

Bgeei P35564.
CleanExi MM_CANX.
ExpressionAtlasi P35564. baseline and differential.
Genevestigatori P35564.

Family and domain databases

Gene3Di 2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProi IPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view ]
PANTHERi PTHR11073. PTHR11073. 1 hit.
Pfami PF00262. Calreticulin. 1 hit.
[Graphical view ]
PRINTSi PR00626. CALRETICULIN.
SUPFAMi SSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEi PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5."
    Tjoelker L.W., Seyfried C.E., Eddy R.L. Jr., Shows T.B. Jr., Calderon J., Schreiber R.B., Gray P.W.
    Biochemistry 33:3229-3236(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. "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] OF 1-155.
    Strain: C57BL/6J.
    Tissue: Eye.
  4. "Class II histocompatibility molecules associate with calnexin during assembly in the endoplasmic reticulum."
    Schreiber K.L., Bell M.P., Huntoon C.J., Rajagopalan S., Brenner M.B., McKean D.J.
    Int. Immunol. 6:101-111(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-591.
    Strain: BALB/c.
  5. "The molecular chaperone calnexin is expressed on the surface of immature thymocytes in association with clonotype-independent CD3 complexes."
    Wiest D.L., Burgess W.H., McKean D., Kearse K.P., Singer A.
    EMBO J. 14:3425-3433(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THYMOCYTE MATURATION, SUBCELLULAR LOCATION.
  6. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
    Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
    J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  7. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "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 SER-553; SER-563 AND SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. "Enhanced clathrin-dependent endocytosis in the absence of calnexin."
    Li H.D., Liu W.X., Michalak M.
    PLoS ONE 6:E21678-E21678(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SGIP1.

Entry informationi

Entry nameiCALX_MOUSE
AccessioniPrimary (citable) accession number: P35564
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 144 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3