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Q8R1F1

- NIBL1_MOUSE

UniProt

Q8R1F1 - NIBL1_MOUSE

Protein

Niban-like protein 1

Gene

Fam129b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (13 Aug 2002)
      Previous versions | rss
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    Functioni

    May play a role in apoptosis suppression.By similarity

    GO - Biological processi

    1. negative regulation of apoptotic process Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Niban-like protein 1
    Alternative name(s):
    Protein FAM129B
    Gene namesi
    Name:Fam129b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2442910. Fam129b.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Cell junctionadherens junction By similarity
    Note: In exponentially growing cells, exclusively cytoplasmic. Cell membrane localization is observed when cells reach confluency and during telophase By similarity. Phosphorylation may play a role in relocalization to the membrane By similarity.By similarity

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB-SubCell
    2. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 749749Niban-like protein 1PRO_0000213122Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei568 – 5681PhosphoserineBy similarity
    Modified residuei574 – 5741PhosphoserineBy similarity
    Modified residuei607 – 6071PhosphoserineBy similarity
    Modified residuei628 – 6281PhosphoserineBy similarity
    Modified residuei650 – 6501PhosphoserineBy similarity
    Modified residuei669 – 6691PhosphoserineBy similarity
    Modified residuei685 – 6851PhosphoserineBy similarity
    Modified residuei695 – 6951PhosphoserineBy similarity
    Modified residuei699 – 6991PhosphoserineBy similarity

    Post-translational modificationi

    As apoptosis proceeds, degraded via an proteasome-independent pathway, probably by caspases.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8R1F1.
    PaxDbiQ8R1F1.
    PRIDEiQ8R1F1.

    PTM databases

    PhosphoSiteiQ8R1F1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8R1F1.
    BgeeiQ8R1F1.
    GenevestigatoriQ8R1F1.

    Interactioni

    Protein-protein interaction databases

    BioGridi230679. 2 interactions.
    IntActiQ8R1F1. 2 interactions.
    MINTiMINT-1849821.
    STRINGi10090.ENSMUSP00000028135.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R1F1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini68 – 192125PHPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Niban family.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG46977.
    GeneTreeiENSGT00530000063284.
    HOVERGENiHBG026217.
    InParanoidiQ3UDW4.
    OMAiRFYEDQY.
    OrthoDBiEOG7GN2MC.
    PhylomeDBiQ8R1F1.
    TreeFamiTF333351.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR026088. Niban_like.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PANTHERiPTHR14392. PTHR14392. 1 hit.
    SMARTiSM00233. PH. 1 hit.
    [Graphical view]
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8R1F1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDVLSTHLD DARRQHIAEK TEKILTEFLR FYEDQYGVSL FNSMRHEIEG    50
    TGPPQAQLLW RKVPLDERII FSGNLFQYQE DNKKWRNRFS LVPHNYGLVL 100
    YENKVAYERQ IPPRAVINSA GYKVLTSVDQ YLELVGNSLP GTTSKSGSTP 150
    ILKCPTQFPL ILWHPYARHY YFCMMTEAEQ DKWQAVLQDC VRHCNNGIPE 200
    NSKVEGPAFT DAIRMYRQSK EQYGTWEMLC GNEVQILSNL VMEELGPALK 250
    AELGPRLKGK PQERQRQWIQ ISDAVYRLVF EQAKVHFEDV LCKLQRARPA 300
    MEAVIRTDMD QIITSKEHLA SKIRAFILPK AEVCVRNHVQ PYIPSILEAL 350
    MVPTSQGFTE VRDVFFKEVT DMNLNVINEG GIDKLGEYME KLSQLAYHPL 400
    KMQSCYEKME PLRLDGLQQR FDVSSTSVFK QRAQIHMREQ MDNAVYTFET 450
    LLHQELGKGP TKEELCKSIQ RILERVLKKY DYDSSSVRKR FFREALLQIT 500
    IPFLLKKLAP TCKSELPRFQ ELIFEDFARF ILVENTYEEV VLQTVMKDIL 550
    QAVKEAAVQR KHNLYRDSMV LHNSDPNLHL LAEGTPIDWG EQYGDSGDSG 600
    GGDSGGSPCP SEAATLTEKR RRAKQVMSVV QDEESGLPFE AGVEPPSPAS 650
    PDSVTELRGL LAQDLQAESS PPASPLLNGA PVQESSQPVA VPEASPPASP 700
    LRHLPPGKAV DLEPPKPSDQ ETGEQVSSPG SRPPIHTTTE DSAGVQTEF 749
    Length:749
    Mass (Da):84,819
    Last modified:August 13, 2002 - v2
    Checksum:iDB578DEA188492C8
    GO

    Sequence cautioni

    The sequence BAC28456.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti81 – 811D → G in BAE31035. (PubMed:16141072)Curated
    Sequence conflicti140 – 1401P → A in BAC28456. (PubMed:16141072)Curated
    Sequence conflicti193 – 1931H → L in BAE29147. (PubMed:16141072)Curated
    Sequence conflicti333 – 3331V → E in BAC34625. (PubMed:16141072)Curated
    Sequence conflicti344 – 3441P → Q in BAE27562. (PubMed:16141072)Curated
    Sequence conflicti503 – 5031F → S in BAE41849. (PubMed:16141072)Curated
    Sequence conflicti655 – 6551T → A in BAE29147. (PubMed:16141072)Curated
    Sequence conflicti662 – 6621A → G in BAE27562. (PubMed:16141072)Curated
    Sequence conflicti711 – 7111D → V in BAE29730. (PubMed:16141072)Curated
    Sequence conflicti724 – 7241E → K in BAE41849. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK033735 mRNA. Translation: BAC28456.1. Different initiation.
    AK046583 mRNA. Translation: BAC32795.1.
    AK051396 mRNA. Translation: BAC34625.1.
    AK146953 mRNA. Translation: BAE27562.1.
    AK149888 mRNA. Translation: BAE29147.1.
    AK150642 mRNA. Translation: BAE29730.1.
    AK152207 mRNA. Translation: BAE31035.1.
    AK153489 mRNA. Translation: BAE32037.1.
    AK170512 mRNA. Translation: BAE41849.1.
    AL845471, AL929154 Genomic DNA. Translation: CAM20729.1.
    AL929154, AL845471 Genomic DNA. Translation: CAM27398.1.
    CH466542 Genomic DNA. Translation: EDL08584.1.
    BC024639 mRNA. Translation: AAH24639.1.
    BC027843 mRNA. Translation: AAH27843.1.
    CCDSiCCDS15934.1.
    RefSeqiNP_666231.1. NM_146119.2.
    UniGeneiMm.301646.

    Genome annotation databases

    EnsembliENSMUST00000028135; ENSMUSP00000028135; ENSMUSG00000026796.
    GeneIDi227737.
    KEGGimmu:227737.
    UCSCiuc008jhc.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK033735 mRNA. Translation: BAC28456.1 . Different initiation.
    AK046583 mRNA. Translation: BAC32795.1 .
    AK051396 mRNA. Translation: BAC34625.1 .
    AK146953 mRNA. Translation: BAE27562.1 .
    AK149888 mRNA. Translation: BAE29147.1 .
    AK150642 mRNA. Translation: BAE29730.1 .
    AK152207 mRNA. Translation: BAE31035.1 .
    AK153489 mRNA. Translation: BAE32037.1 .
    AK170512 mRNA. Translation: BAE41849.1 .
    AL845471 , AL929154 Genomic DNA. Translation: CAM20729.1 .
    AL929154 , AL845471 Genomic DNA. Translation: CAM27398.1 .
    CH466542 Genomic DNA. Translation: EDL08584.1 .
    BC024639 mRNA. Translation: AAH24639.1 .
    BC027843 mRNA. Translation: AAH27843.1 .
    CCDSi CCDS15934.1.
    RefSeqi NP_666231.1. NM_146119.2.
    UniGenei Mm.301646.

    3D structure databases

    ProteinModelPortali Q8R1F1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230679. 2 interactions.
    IntActi Q8R1F1. 2 interactions.
    MINTi MINT-1849821.
    STRINGi 10090.ENSMUSP00000028135.

    PTM databases

    PhosphoSitei Q8R1F1.

    Proteomic databases

    MaxQBi Q8R1F1.
    PaxDbi Q8R1F1.
    PRIDEi Q8R1F1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028135 ; ENSMUSP00000028135 ; ENSMUSG00000026796 .
    GeneIDi 227737.
    KEGGi mmu:227737.
    UCSCi uc008jhc.2. mouse.

    Organism-specific databases

    CTDi 64855.
    MGIi MGI:2442910. Fam129b.

    Phylogenomic databases

    eggNOGi NOG46977.
    GeneTreei ENSGT00530000063284.
    HOVERGENi HBG026217.
    InParanoidi Q3UDW4.
    OMAi RFYEDQY.
    OrthoDBi EOG7GN2MC.
    PhylomeDBi Q8R1F1.
    TreeFami TF333351.

    Miscellaneous databases

    ChiTaRSi FAM129B. mouse.
    NextBioi 378808.
    PROi Q8R1F1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8R1F1.
    Bgeei Q8R1F1.
    Genevestigatori Q8R1F1.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR026088. Niban_like.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    PANTHERi PTHR14392. PTHR14392. 1 hit.
    SMARTi SM00233. PH. 1 hit.
    [Graphical view ]
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Strain: C57BL/6J and NOD.
      Tissue: Adipose tissue, Cecum, Dendritic cell, Embryonic heart, Embryonic spinal ganglion and Macrophage.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "FAM129B/MINERVA, a novel adherens junction-associated protein, suppresses apoptosis in HeLa cells."
      Chen S., Evans H.G., Evans D.R.
      J. Biol. Chem. 286:10201-10209(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiNIBL1_MOUSE
    AccessioniPrimary (citable) accession number: Q8R1F1
    Secondary accession number(s): Q3TCV6
    , Q3U8I3, Q3UC84, Q3UDW4, Q3UIE4, Q543S7, Q8BQ71, Q8CC78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: August 13, 2002
    Last modified: October 1, 2014
    This is version 94 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3