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Q91Z67

- SRGP2_MOUSE

UniProt

Q91Z67 - SRGP2_MOUSE

Protein

SLIT-ROBO Rho GTPase-activating protein 2

Gene

Srgap2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. May play a role for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia.2 Publications

    GO - Molecular functioni

    1. protein homodimerization activity Source: UniProtKB
    2. Rac GTPase activator activity Source: UniProtKB
    3. Rac GTPase binding Source: UniProtKB

    GO - Biological processi

    1. actin filament severing Source: UniProtKB
    2. dendritic spine development Source: UniProtKB
    3. extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration Source: UniProtKB
    4. filopodium assembly Source: UniProtKB
    5. negative regulation of neuron migration Source: UniProtKB
    6. neuron projection morphogenesis Source: UniProtKB
    7. positive regulation of Rac GTPase activity Source: UniProtKB
    8. signal transduction Source: InterPro

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Biological processi

    Neurogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SLIT-ROBO Rho GTPase-activating protein 2
    Short name:
    srGAP2
    Alternative name(s):
    Formin-binding protein 2
    Formin-binding protein 27
    Short name:
    FBP-27
    Gene namesi
    Name:Srgap2
    Synonyms:Fbp27, Fnbp2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:109605. Srgap2.

    Subcellular locationi

    Cell membrane By similarity. Cell projectiondendritic spine By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell junctionsynapsepostsynaptic cell membrane. Cell projectionlamellipodium By similarity. Cytoplasmic vesiclephagosome. Nucleus By similarity. Cytoplasm By similarity
    Note: Recruited to actin-rich phagosomes during phagocytosis. Translocates from nucleus to cytoplasm during development By similarity.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytosol Source: UniProtKB
    3. dendritic spine head Source: UniProtKB
    4. lamellipodium Source: UniProtKB-SubCell
    5. mitochondrial inner membrane Source: MGI
    6. nucleus Source: UniProtKB-SubCell
    7. phagocytic vesicle Source: UniProtKB
    8. plasma membrane Source: UniProtKB
    9. postsynaptic density Source: UniProtKB
    10. postsynaptic membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Disruption phenotypei

    Mice are viable and show no abnormality of cortical lamination. However, a delay in dendritic spine maturation coupled to an increase in spine neck and spine density is observed.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi527 – 5271R → L: Unable to stimulate RAC1 GTPase activity and to induce neurite branching. No effect on filopodia biogenesis and neurite outgrowth. 1 Publication
    Mutagenesisi765 – 7651W → A: Loss of the ability to induce filopodia and to initiate neurite outgrowht. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10711071SLIT-ROBO Rho GTPase-activating protein 2PRO_0000056768Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei927 – 9271Omega-N-methylated arginine; by PRMT5By similarity
    Modified residuei930 – 9301PhosphoserineBy similarity

    Post-translational modificationi

    Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions.By similarity

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ91Z67.
    PaxDbiQ91Z67.
    PRIDEiQ91Z67.

    PTM databases

    PhosphoSiteiQ91Z67.

    Expressioni

    Developmental stagei

    Expressed throughout cortical development culminating at P1. Expression is reduced but still present in the adult cortex. Expressed in the cortical wall both in neuronal progenitors in the ventricular zone and post-mitotic neurons in the cortical plate (at protein level).1 Publication

    Gene expression databases

    BgeeiQ91Z67.
    CleanExiMM_SRGAP2.
    GenevestigatoriQ91Z67.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with FASLG By similarity. Interacts with PRMT5 By similarity. Probably interacts with ROBO1 and ROBO2. Interacts with RAC1; specifically stimulates RAC1 GTPase activity. Interacts (via SH3 domain) with FMNL1 (activated by RAC1); regulates the actin filament severing activity of FMNL1. Interacts (via SH3 domain) with FMNL3. Interacts (via SH3 domain) with GPHN.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi199721. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91Z67.
    SMRiQ91Z67. Positions 723-787.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 8766FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini489 – 679191Rho-GAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini728 – 78760SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 502502F-BAR domainBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili363 – 40139Sequence AnalysisAdd
    BLAST
    Coiled coili940 – 96829Sequence AnalysisAdd
    BLAST

    Domaini

    The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions.

    Sequence similaritiesi

    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG264793.
    GeneTreeiENSGT00710000106292.
    HOGENOMiHOG000039980.
    HOVERGENiHBG051637.
    KOiK07526.
    OMAiEDYCESP.
    OrthoDBiEOG7966FQ.
    PhylomeDBiQ91Z67.
    TreeFamiTF315892.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    InterProiIPR001060. FCH_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00611. FCH. 1 hit.
    PF00620. RhoGAP. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    SMARTiSM00055. FCH. 1 hit.
    SM00324. RhoGAP. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS50238. RHOGAP. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q91Z67-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ     50
    DFFRKKAEIE MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN 100
    LLLNQVKRES RDHTTLSDIY LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ 150
    DDLMKVLNEL YSVMKTYHMY NADSISAQSK LKEAEKQEEK QIGKSVKQED 200
    RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT ENKLKAIKAR 250
    NEYLLALEAT NASVFKYYIH DLSDIIDQCC DLGYHASLNR ALRTFLSAEL 300
    NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG 350
    DMASQLCAQQ PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD 400
    IVTVEDFDVS DCFQYSNSME SVKSTVSETF MSKPSIAKRR ANQQETEQFY 450
    FTKMKEYLEG RNLITKLQAK HDLLQKTLGE SQRTDCSLAR RSSTVRKQDS 500
    SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN AFERGEDPLA 550
    GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLIACVT MDNLQERAVH 600
    IRKVLLVLPK PTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS 650
    VPEGHDQVSC QAHVNELIKT IIIQHENIFP NPRELEGPIY SRGGSMEDYC 700
    DSTHGETTSA EDSTQDVTAE HHTSDDECEP IEAIAKFDYV GRTARELSFK 750
    KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ YIVVQDTEDG VVERSSPKSE 800
    IEVMSEPPEE KVTARTGASC PSGGHVADIY LANINKQRKR PESGSIRKAF 850
    RSDSHGLGSS LTDSSSLGVG ASCRPSSQPI MSQNLPKEGP DKCSISGHGS 900
    LNSISRHSSL KNRMDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM 950
    NSALNELQEL ERQSSAKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL 1000
    LKDPEPAFQR SASTAGDIAC AFRPVKSVKM AAPVKPPATR PKPTVFPKTN 1050
    ATSPGVNSSA SPQATDKSCT V 1071
    Length:1,071
    Mass (Da):120,798
    Last modified:January 9, 2007 - v2
    Checksum:i9093C63476BA605D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti598 – 5981A → V in AAL27032. (PubMed:11672528)Curated
    Sequence conflicti612 – 6121T → S in AAL27032. (PubMed:11672528)Curated
    Sequence conflicti662 – 6621A → S in AAL27032. (PubMed:11672528)Curated
    Sequence conflicti737 – 7371F → C in AAL27032. (PubMed:11672528)Curated
    Sequence conflicti765 – 7651W → L in AAL27032. (PubMed:11672528)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC109299 Genomic DNA. No translation available.
    AC120217 Genomic DNA. No translation available.
    AC165436 Genomic DNA. No translation available.
    BC151081 mRNA. Translation: AAI51082.1.
    BC151082 mRNA. Translation: AAI51083.1.
    BC158055 mRNA. Translation: AAI58056.1.
    BC172152 mRNA. Translation: AAI72152.1.
    AY057900 mRNA. Translation: AAL27032.1.
    AK132220 mRNA. Translation: BAE21041.1.
    U40752 mRNA. Translation: AAC52480.1.
    CCDSiCCDS48355.1.
    PIRiS64712.
    RefSeqiNP_001074480.2. NM_001081011.2.
    XP_006529197.1. XM_006529134.1.
    XP_006529198.1. XM_006529135.1.
    UniGeneiMm.276259.

    Genome annotation databases

    EnsembliENSMUST00000097588; ENSMUSP00000095195; ENSMUSG00000026425.
    GeneIDi14270.
    KEGGimmu:14270.
    UCSCiuc007cng.2. mouse.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Branching out - Issue 143 of October 2012

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC109299 Genomic DNA. No translation available.
    AC120217 Genomic DNA. No translation available.
    AC165436 Genomic DNA. No translation available.
    BC151081 mRNA. Translation: AAI51082.1 .
    BC151082 mRNA. Translation: AAI51083.1 .
    BC158055 mRNA. Translation: AAI58056.1 .
    BC172152 mRNA. Translation: AAI72152.1 .
    AY057900 mRNA. Translation: AAL27032.1 .
    AK132220 mRNA. Translation: BAE21041.1 .
    U40752 mRNA. Translation: AAC52480.1 .
    CCDSi CCDS48355.1.
    PIRi S64712.
    RefSeqi NP_001074480.2. NM_001081011.2.
    XP_006529197.1. XM_006529134.1.
    XP_006529198.1. XM_006529135.1.
    UniGenei Mm.276259.

    3D structure databases

    ProteinModelPortali Q91Z67.
    SMRi Q91Z67. Positions 723-787.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199721. 1 interaction.

    PTM databases

    PhosphoSitei Q91Z67.

    Proteomic databases

    MaxQBi Q91Z67.
    PaxDbi Q91Z67.
    PRIDEi Q91Z67.

    Protocols and materials databases

    DNASUi 14270.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000097588 ; ENSMUSP00000095195 ; ENSMUSG00000026425 .
    GeneIDi 14270.
    KEGGi mmu:14270.
    UCSCi uc007cng.2. mouse.

    Organism-specific databases

    CTDi 23380.
    MGIi MGI:109605. Srgap2.

    Phylogenomic databases

    eggNOGi NOG264793.
    GeneTreei ENSGT00710000106292.
    HOGENOMi HOG000039980.
    HOVERGENi HBG051637.
    KOi K07526.
    OMAi EDYCESP.
    OrthoDBi EOG7966FQ.
    PhylomeDBi Q91Z67.
    TreeFami TF315892.

    Miscellaneous databases

    ChiTaRSi SRGAP2. mouse.
    NextBioi 285639.
    PROi Q91Z67.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q91Z67.
    CleanExi MM_SRGAP2.
    Genevestigatori Q91Z67.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    InterProi IPR001060. FCH_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00611. FCH. 1 hit.
    PF00620. RhoGAP. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    SMARTi SM00055. FCH. 1 hit.
    SM00324. RhoGAP. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF50044. SSF50044. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS50238. RHOGAP. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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].
      Tissue: Brain.
    3. "Signal transduction in neuronal migration: roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway."
      Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H., Wen L., Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.
      Cell 107:209-221(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 432-836.
    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] OF 538-1071.
      Strain: C57BL/6J.
      Tissue: Brain.
    5. "Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains."
      Chan D.C., Bedford M.T., Leder P.
      EMBO J. 15:1045-1054(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 732-782.
      Strain: FVB.
    6. "The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis."
      Guerrier S., Coutinho-Budd J., Sassa T., Gresset A., Jordan N.V., Chen K., Jin W.L., Frost A., Polleux F.
      Cell 138:990-1004(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEURON MIGRATION AND MORPHOGENESIS, DEVELOPMENTAL STAGE, SUBUNIT, INTERACTION WITH RAC1, MUTAGENESIS OF ARG-527 AND TRP-765.
    7. Cited for: INTERACTION WITH FMNL1; FMNL3 AND ROBO2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "SH3 domain-based phototrapping in living cells reveals Rho family GAP signaling complexes."
      Okada H., Uezu A., Mason F.M., Soderblom E.J., Moseley M.A. III, Soderling S.H.
      Sci. Signal. 4:RS13-RS13(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GPHN.
    9. "Inhibition of SRGAP2 function by its human-specific paralogs induces neoteny during spine maturation."
      Charrier C., Joshi K., Coutinho-Budd J., Kim J.E., Lambert N., de Marchena J., Jin W.L., Vanderhaeghen P., Ghosh A., Sassa T., Polleux F.
      Cell 149:923-935(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DENDRITIC SPINE MATURATION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiSRGP2_MOUSE
    AccessioniPrimary (citable) accession number: Q91Z67
    Secondary accession number(s): B2RY13, Q3V1V8, Q61054
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 102 of the entry and version 2 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3