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Q9Z0P7

- SUFU_MOUSE

UniProt

Q9Z0P7 - SUFU_MOUSE

Protein

Suppressor of fused homolog

Gene

Sufu

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Negative regulator in the hedgehog signaling pathway. Down-regulates GLI1-mediated transactivation of target genes. Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein. Negative regulator of beta-catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A). Required for the proper formation of hair follicles and the control of epidermal differentiation.5 Publications

    GO - Molecular functioni

    1. beta-catenin binding Source: MGI
    2. protein binding Source: UniProtKB
    3. transcription factor binding Source: MGI

    GO - Biological processi

    1. cytoplasmic sequestering of transcription factor Source: MGI
    2. determination of left/right symmetry Source: MGI
    3. heart looping Source: MGI
    4. negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: MGI
    5. negative regulation of smoothened signaling pathway Source: MGI
    6. negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: MGI
    7. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    8. neural tube closure Source: MGI
    9. skin development Source: MGI
    10. smoothened signaling pathway involved in spinal cord motor neuron cell fate specification Source: MGI
    11. smoothened signaling pathway involved in ventral spinal cord interneuron specification Source: MGI
    12. spinal cord dorsal/ventral patterning Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Suppressor of fused homolog
    Gene namesi
    Name:Sufu
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1345643. Sufu.

    Subcellular locationi

    GO - Cellular componenti

    1. cilium Source: MGI
    2. cytoplasm Source: UniProtKB
    3. nucleus Source: MGI
    4. primary cilium Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 484484Suppressor of fused homologPRO_0000072303Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei303 – 3031N6-acetyllysineBy similarity
    Modified residuei481 – 4811PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z0P7.
    PaxDbiQ9Z0P7.
    PRIDEiQ9Z0P7.

    PTM databases

    PhosphoSiteiQ9Z0P7.

    Expressioni

    Tissue specificityi

    Widely expressed in adult and fetal tissues.2 Publications

    Gene expression databases

    ArrayExpressiQ9Z0P7.
    BgeeiQ9Z0P7.
    CleanExiMM_SUFU.
    GenevestigatoriQ9Z0P7.

    Interactioni

    Subunit structurei

    Interacts with ULK3; inactivating the protein kinase activity of ULK3. Interacts with RAB23 By similarity. May form homodimers. Part of a DNA-bound corepressor complex containing SAP18, GLI1 and SIN3. Part of a complex containing CTNNB1. Binds BTRC, GLI2, GLI3, SAP18 and STK36. Binds both free and DNA-bound GLI1. Interacts with KIF7. Interacts with GLI3FL and this interaction regulates the formation of either repressor or activator forms of GLI3. Its association with GLI3FL is regulated by Hh signaling and dissociation of the SUFU-GLI3 interaction requires the presence of the ciliary motor KIF3A.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Lgals3P161105EBI-3508336,EBI-3508325
    Pias1O889073EBI-3508336,EBI-3508327
    Rnf19aP506363EBI-3508336,EBI-3508340
    Sap18O551286EBI-3508336,EBI-3508332

    Protein-protein interaction databases

    BioGridi204881. 21 interactions.
    IntActiQ9Z0P7. 18 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z0P7.
    SMRiQ9Z0P7. Positions 1-280, 356-481.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SUFU family.Curated

    Phylogenomic databases

    eggNOGiNOG72477.
    GeneTreeiENSGT00390000009747.
    HOGENOMiHOG000007864.
    HOVERGENiHBG061539.
    KOiK06229.
    OMAiGDTAITF.
    OrthoDBiEOG7RV9FV.
    PhylomeDBiQ9Z0P7.
    TreeFamiTF324548.

    Family and domain databases

    InterProiIPR020941. SUFU-like_domain.
    IPR024314. SUFU_C.
    IPR007768. Suppressor_of_fused.
    IPR016591. Suppressor_of_fused_euk.
    [Graphical view]
    PANTHERiPTHR10928. PTHR10928. 1 hit.
    PfamiPF05076. SUFU. 1 hit.
    PF12470. SUFU_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF011844. Suppressor_of_fused_protein. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Z0P7-1) [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

    MAELRPSVAP GPAAPPASGP SAPPAFASLF PPGLHAIYGE CRRLYPDQPN    50
    PLQVTAIVKY WLGGPDPLDY VSMYRNMGSP SANIPEHWHY ISFGLSDLYG 100
    DNRVHEFTGT DGPSGFGFEL TFRLKRETGE SAPPTWPAEL MQGLARYVFQ 150
    SENTFCSGDH VSWHSPLDNS ESRIQHMLLT EDPQMQPVRT PFGVVTFLQI 200
    VGVCTEELHS AQQWNGQGIL ELLRTVPIAG GPWLITDMRR GETIFEIDPH 250
    LQERVDKGIE TDGSNLSGVS AKCAWDDLSR PPEDEEDSRS ICLGTQPRRL 300
    SGKDTEQIRE TLRRGLEINS KPVLPPINSQ RQNGLTHDRA PSRKDSLGSD 350
    SSTAIIPHEL IRTRQLESVH LKFNQESGAL IPLCLRGRLL HGRHFTYKSI 400
    TGDMAITFVS TGVEGAFATE EHPYAAHGPW LQILLTEEFV EKMLEDLEDL 450
    TSPEEFKLPK EYSWPEKKLK VSILPDVVFD SPLH 484
    Length:484
    Mass (Da):53,957
    Last modified:May 1, 1999 - v1
    Checksum:i6ED5666BC4D4AFB5
    GO
    Isoform 2 (identifier: Q9Z0P7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         62-106: Missing.
         252-252: Q → QQ

    Note: No experimental confirmation available.

    Show »
    Length:440
    Mass (Da):48,994
    Checksum:i1C36B0D3382C1F95
    GO
    Isoform 3 (identifier: Q9Z0P7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         252-252: Q → QQ
         433-484: ILLTEEFVEK...PDVVFDSPLH → VRRSLSSFSSSSCSSLAACPPLPHHPKDRPLWLPC

    Show »
    Length:468
    Mass (Da):51,759
    Checksum:i98B0F3F09CA85B8A
    GO
    Isoform 4 (identifier: Q9Z0P7-4) [UniParc]FASTAAdd to Basket

    Also known as: SU(FU)-XL

    The sequence of this isoform differs from the canonical sequence as follows:
         252-252: Q → QQ

    Show »
    Length:485
    Mass (Da):54,085
    Checksum:iF9387714357EC8E4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 791S → C in AAF61412. (PubMed:10531011)Curated
    Sequence conflicti220 – 2201L → Q in AAF61412. (PubMed:10531011)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei62 – 10645Missing in isoform 2. 1 PublicationVSP_013281Add
    BLAST
    Alternative sequencei252 – 2521Q → QQ in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_013282
    Alternative sequencei433 – 48452ILLTE…DSPLH → VRRSLSSFSSSSCSSLAACP PLPHHPKDRPLWLPC in isoform 3. 1 PublicationVSP_013283Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF134893 mRNA. Translation: AAF61412.1.
    AJ131692 mRNA. Translation: CAB38081.1.
    AJ308625 mRNA. Translation: CAC34257.1.
    AJ308626 mRNA. Translation: CAC34258.1.
    AJ308627
    , AJ308628, AJ308629, AJ308630, AJ308632, AJ308634, AJ308635, AJ308633, AJ308631 Genomic DNA. Translation: CAC34271.1.
    AK015885 mRNA. Translation: BAB30017.1.
    AK047603 mRNA. Translation: BAC33095.1.
    BC048168 mRNA. Translation: AAH48168.1.
    BC056997 mRNA. Translation: AAH56997.1.
    CCDSiCCDS29879.1. [Q9Z0P7-1]
    CCDS38008.1. [Q9Z0P7-4]
    RefSeqiNP_001020562.1. NM_001025391.2. [Q9Z0P7-1]
    NP_056567.2. NM_015752.3. [Q9Z0P7-4]
    UniGeneiMm.41210.

    Genome annotation databases

    EnsembliENSMUST00000039922; ENSMUSP00000049109; ENSMUSG00000025231. [Q9Z0P7-1]
    ENSMUST00000111867; ENSMUSP00000107498; ENSMUSG00000025231. [Q9Z0P7-4]
    ENSMUST00000120778; ENSMUSP00000112653; ENSMUSG00000025231.
    GeneIDi24069.
    KEGGimmu:24069.
    UCSCiuc008htn.1. mouse. [Q9Z0P7-2]
    uc008hto.1. mouse. [Q9Z0P7-3]
    uc008htq.1. mouse. [Q9Z0P7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF134893 mRNA. Translation: AAF61412.1 .
    AJ131692 mRNA. Translation: CAB38081.1 .
    AJ308625 mRNA. Translation: CAC34257.1 .
    AJ308626 mRNA. Translation: CAC34258.1 .
    AJ308627
    , AJ308628 , AJ308629 , AJ308630 , AJ308632 , AJ308634 , AJ308635 , AJ308633 , AJ308631 Genomic DNA. Translation: CAC34271.1 .
    AK015885 mRNA. Translation: BAB30017.1 .
    AK047603 mRNA. Translation: BAC33095.1 .
    BC048168 mRNA. Translation: AAH48168.1 .
    BC056997 mRNA. Translation: AAH56997.1 .
    CCDSi CCDS29879.1. [Q9Z0P7-1 ]
    CCDS38008.1. [Q9Z0P7-4 ]
    RefSeqi NP_001020562.1. NM_001025391.2. [Q9Z0P7-1 ]
    NP_056567.2. NM_015752.3. [Q9Z0P7-4 ]
    UniGenei Mm.41210.

    3D structure databases

    ProteinModelPortali Q9Z0P7.
    SMRi Q9Z0P7. Positions 1-280, 356-481.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204881. 21 interactions.
    IntActi Q9Z0P7. 18 interactions.

    PTM databases

    PhosphoSitei Q9Z0P7.

    Proteomic databases

    MaxQBi Q9Z0P7.
    PaxDbi Q9Z0P7.
    PRIDEi Q9Z0P7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000039922 ; ENSMUSP00000049109 ; ENSMUSG00000025231 . [Q9Z0P7-1 ]
    ENSMUST00000111867 ; ENSMUSP00000107498 ; ENSMUSG00000025231 . [Q9Z0P7-4 ]
    ENSMUST00000120778 ; ENSMUSP00000112653 ; ENSMUSG00000025231 .
    GeneIDi 24069.
    KEGGi mmu:24069.
    UCSCi uc008htn.1. mouse. [Q9Z0P7-2 ]
    uc008hto.1. mouse. [Q9Z0P7-3 ]
    uc008htq.1. mouse. [Q9Z0P7-1 ]

    Organism-specific databases

    CTDi 51684.
    MGIi MGI:1345643. Sufu.

    Phylogenomic databases

    eggNOGi NOG72477.
    GeneTreei ENSGT00390000009747.
    HOGENOMi HOG000007864.
    HOVERGENi HBG061539.
    KOi K06229.
    OMAi GDTAITF.
    OrthoDBi EOG7RV9FV.
    PhylomeDBi Q9Z0P7.
    TreeFami TF324548.

    Miscellaneous databases

    NextBioi 304049.
    PROi Q9Z0P7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z0P7.
    Bgeei Q9Z0P7.
    CleanExi MM_SUFU.
    Genevestigatori Q9Z0P7.

    Family and domain databases

    InterProi IPR020941. SUFU-like_domain.
    IPR024314. SUFU_C.
    IPR007768. Suppressor_of_fused.
    IPR016591. Suppressor_of_fused_euk.
    [Graphical view ]
    PANTHERi PTHR10928. PTHR10928. 1 hit.
    Pfami PF05076. SUFU. 1 hit.
    PF12470. SUFU_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF011844. Suppressor_of_fused_protein. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Mouse suppressor of fused is a negative regulator of sonic hedgehog signaling and alters the subcellular distribution of Gli1."
      Ding Q., Fukami S., Meng X., Nishizaki Y., Zhang X., Sasaki H., Dlugosz A., Nakafuku M., Hui C.
      Curr. Biol. 9:1119-1122(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH GLI1; GLI2 AND GLI3, TISSUE SPECIFICITY.
    2. "Suppressor of fused gene involved in hedgehog signal transduction in Drosophila melanogaster is conserved in mammals."
      Delattre M., Briand S., Paces-Fessy M., Blanchet-Tournier M.-F.
      Dev. Genes Evol. 209:294-300(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Embryo.
    3. "Genomic organization and embryonic expression of suppressor of fused, a candidate gene for the split-hand/split-foot malformation type 3."
      Grimm T., Teglund S., Tackels D., Sangiorgi E., Gurrieri F., Schwartz C., Toftgaard R.
      FEBS Lett. 505:13-17(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Strain: 129/SvJ and C57BL/6J.
      Tissue: Mammary gland and Testis.
    4. "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 2 AND 3).
      Strain: C57BL/6J.
      Tissue: Cerebellum and Testis.
    5. "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.
      Tissue: Brain.
    6. "Suppressor of fused negatively regulates beta-catenin signaling."
      Meng X., Poon R., Zhang X., Cheah A., Ding Q., Hui C.-C., Alman B.
      J. Biol. Chem. 276:40113-40119(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH CTNNB1.
    7. "Suppressor of fused represses Gli-mediated transcription by recruiting the SAP18-mSin3 corepressor complex."
      Cheng S.Y., Bishop J.M.
      Proc. Natl. Acad. Sci. U.S.A. 99:5442-5447(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SAP18, IDENTIFICATION IN A DNA-BOUND SIN3 COREPRESSOR COMPLEX.
    8. "The mammalian Cos2 homolog Kif7 plays an essential role in modulating Hh signal transduction during development."
      Endoh-Yamagami S., Evangelista M., Wilson D., Wen X., Theunissen J.W., Phamluong K., Davis M., Scales S.J., Solloway M.J., de Sauvage F.J., Peterson A.S.
      Curr. Biol. 19:1320-1326(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIF7.
    9. "The output of Hedgehog signaling is controlled by the dynamic association between Suppressor of Fused and the Gli proteins."
      Humke E.W., Dorn K.V., Milenkovic L., Scott M.P., Rohatgi R.
      Genes Dev. 24:670-682(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GLI3.
    10. "Kif7 regulates Gli2 through Sufu-dependent and -independent functions during skin development and tumorigenesis."
      Li Z.J., Nieuwenhuis E., Nien W., Zhang X., Zhang J., Puviindran V., Wainwright B.J., Kim P.C., Hui C.C.
      Development 139:4152-4161(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EPIDERMAL DIFFERENTIATION, SUBCELLULAR LOCATION, INTERACTION WITH GLI2.

    Entry informationi

    Entry nameiSUFU_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z0P7
    Secondary accession number(s): Q8C8B4
    , Q99JG0, Q9D521, Q9JLU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 104 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