Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8R1F1

- NIBL1_MOUSE

UniProt

Q8R1F1 - NIBL1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Niban-like protein 1

Gene

Fam129b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

May play a role in apoptosis suppression.By similarity

GO - Biological processi

  1. negative regulation of apoptotic process Source: Ensembl
Complete GO annotation...

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. actin cytoskeleton Source: Ensembl
  2. adherens junction Source: Ensembl
  3. cytosol Source: UniProtKB
  4. extracellular vesicular exosome Source: Ensembl
  5. plasma membrane Source: Ensembl
Complete GO annotation...

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

BgeeiQ8R1F1.
ExpressionAtlasiQ8R1F1. baseline and differential.
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.
InParanoidiQ8R1F1.
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

        10         20         30         40         50
MGDVLSTHLD DARRQHIAEK TEKILTEFLR FYEDQYGVSL FNSMRHEIEG
60 70 80 90 100
TGPPQAQLLW RKVPLDERII FSGNLFQYQE DNKKWRNRFS LVPHNYGLVL
110 120 130 140 150
YENKVAYERQ IPPRAVINSA GYKVLTSVDQ YLELVGNSLP GTTSKSGSTP
160 170 180 190 200
ILKCPTQFPL ILWHPYARHY YFCMMTEAEQ DKWQAVLQDC VRHCNNGIPE
210 220 230 240 250
NSKVEGPAFT DAIRMYRQSK EQYGTWEMLC GNEVQILSNL VMEELGPALK
260 270 280 290 300
AELGPRLKGK PQERQRQWIQ ISDAVYRLVF EQAKVHFEDV LCKLQRARPA
310 320 330 340 350
MEAVIRTDMD QIITSKEHLA SKIRAFILPK AEVCVRNHVQ PYIPSILEAL
360 370 380 390 400
MVPTSQGFTE VRDVFFKEVT DMNLNVINEG GIDKLGEYME KLSQLAYHPL
410 420 430 440 450
KMQSCYEKME PLRLDGLQQR FDVSSTSVFK QRAQIHMREQ MDNAVYTFET
460 470 480 490 500
LLHQELGKGP TKEELCKSIQ RILERVLKKY DYDSSSVRKR FFREALLQIT
510 520 530 540 550
IPFLLKKLAP TCKSELPRFQ ELIFEDFARF ILVENTYEEV VLQTVMKDIL
560 570 580 590 600
QAVKEAAVQR KHNLYRDSMV LHNSDPNLHL LAEGTPIDWG EQYGDSGDSG
610 620 630 640 650
GGDSGGSPCP SEAATLTEKR RRAKQVMSVV QDEESGLPFE AGVEPPSPAS
660 670 680 690 700
PDSVTELRGL LAQDLQAESS PPASPLLNGA PVQESSQPVA VPEASPPASP
710 720 730 740
LRHLPPGKAV DLEPPKPSDQ ETGEQVSSPG SRPPIHTTTE DSAGVQTEF
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 Q8R1F1.
OMAi RFYEDQY.
OrthoDBi EOG7GN2MC.
PhylomeDBi Q8R1F1.
TreeFami TF333351.

Miscellaneous databases

ChiTaRSi Fam129b. mouse.
NextBioi 378808.
PROi Q8R1F1.
SOURCEi Search...

Gene expression databases

Bgeei Q8R1F1.
ExpressionAtlasi Q8R1F1. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 96 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