Skip Header

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

Smad nuclear-interacting protein 1

Gene

Snip1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Down-regulates NF-kappa-B signaling by competing with RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis. biogenesis. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

RNA-mediated gene silencing

Names & Taxonomyi

Protein namesi
Recommended name:
Smad nuclear-interacting protein 1
Gene namesi
Name:Snip1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2156003. Snip1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 383383Smad nuclear-interacting protein 1PRO_0000072010Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphoserineCombined sources
Cross-linki28 – 28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki28 – 28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki28 – 28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei33 – 331PhosphoserineBy similarity
Modified residuei48 – 481PhosphoserineCombined sources
Modified residuei50 – 501PhosphoserineCombined sources
Modified residuei91 – 911PhosphoserineBy similarity
Cross-linki100 – 100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei145 – 1451PhosphoserineBy similarity
Modified residuei381 – 3811PhosphoserineBy similarity

Post-translational modificationi

Degraded by the proteasome upon binding to the SMAD1/OAZ1/PSMB4 complex.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8BIZ6.
MaxQBiQ8BIZ6.
PaxDbiQ8BIZ6.
PeptideAtlasiQ8BIZ6.
PRIDEiQ8BIZ6.

PTM databases

iPTMnetiQ8BIZ6.
PhosphoSiteiQ8BIZ6.

Expressioni

Gene expression databases

BgeeiQ8BIZ6.
CleanExiMM_SNIP1.
GenevisibleiQ8BIZ6. MM.

Interactioni

Subunit structurei

Binds SMAD4 and CREBBP/EP300. Binds the SMAD1/OAZ1/PSMB4 complex. Interacts with DROSHA and SMARCA4. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN (By similarity).By similarity

Protein-protein interaction databases

IntActiQ8BIZ6. 1 interaction.
STRINGi10090.ENSMUSP00000060721.

Structurei

3D structure databases

ProteinModelPortaliQ8BIZ6.
SMRiQ8BIZ6. Positions 233-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini268 – 33164FHAPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili153 – 19442Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi62 – 180119Arg-richAdd
BLAST
Compositional biasi374 – 3774Poly-Glu

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1882. Eukaryota.
ENOG4111F4H. LUCA.
GeneTreeiENSGT00730000110659.
HOGENOMiHOG000264922.
HOVERGENiHBG056615.
InParanoidiQ8BIZ6.
KOiK13108.
OMAiKNDEFLP.
OrthoDBiEOG7P02K5.
PhylomeDBiQ8BIZ6.
TreeFamiTF312797.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BIZ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAGKSERER SGRRRHRSGD ALTTVVVKQE RLSPEPVAHR RPDAPAASLS
60 70 80 90 100
PPAAEPGHSG HRGSRARSPA KKKSKSSGRR SKSPRTKRSQ SPHYPMVKVK
110 120 130 140 150
QEREDHPRRG REDRQHREPS EQEHRRARNS ERDRHRGHSR QGRSSDERPV
160 170 180 190 200
SGQDRDRDSQ NLQAQEEERD FHNARRREHR QQNESAGSEA QEVIPRPAGN
210 220 230 240 250
RSKEVPVKEK PSFELSGALL EDTNTFRGVV IKYSEPPEAR IPKKRWRLYP
260 270 280 290 300
FKNDEVLPVM YIHRQSAYLL GRHRRIADIP IDHPSCSKQH AVFQYRLVEY
310 320 330 340 350
TRADGTVGRR VKPYIIDLGS GNGTFLNNKR IEPQRYYELK EKDVLKFGFS
360 370 380
SREYVLLHES SDTSELDRKE DEDDEEEEMV SDS
Length:383
Mass (Da):44,415
Last modified:March 1, 2003 - v1
Checksum:i0ADD646D4CB952BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2231T → P in BAC33680 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040571 mRNA. Translation: BAE20582.1.
AK049254 mRNA. Translation: BAC33638.1.
AK049318 mRNA. Translation: BAC33680.1.
AK132768 mRNA. Translation: BAE21347.1.
AK143801 mRNA. Translation: BAE25543.1.
BC064067 mRNA. Translation: AAH64067.1.
CCDSiCCDS18636.1.
RefSeqiNP_780455.2. NM_175246.4.
UniGeneiMm.22548.

Genome annotation databases

EnsembliENSMUST00000052183; ENSMUSP00000060721; ENSMUSG00000050213.
GeneIDi76793.
KEGGimmu:76793.
UCSCiuc008urq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040571 mRNA. Translation: BAE20582.1.
AK049254 mRNA. Translation: BAC33638.1.
AK049318 mRNA. Translation: BAC33680.1.
AK132768 mRNA. Translation: BAE21347.1.
AK143801 mRNA. Translation: BAE25543.1.
BC064067 mRNA. Translation: AAH64067.1.
CCDSiCCDS18636.1.
RefSeqiNP_780455.2. NM_175246.4.
UniGeneiMm.22548.

3D structure databases

ProteinModelPortaliQ8BIZ6.
SMRiQ8BIZ6. Positions 233-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BIZ6. 1 interaction.
STRINGi10090.ENSMUSP00000060721.

PTM databases

iPTMnetiQ8BIZ6.
PhosphoSiteiQ8BIZ6.

Proteomic databases

EPDiQ8BIZ6.
MaxQBiQ8BIZ6.
PaxDbiQ8BIZ6.
PeptideAtlasiQ8BIZ6.
PRIDEiQ8BIZ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052183; ENSMUSP00000060721; ENSMUSG00000050213.
GeneIDi76793.
KEGGimmu:76793.
UCSCiuc008urq.2. mouse.

Organism-specific databases

CTDi79753.
MGIiMGI:2156003. Snip1.

Phylogenomic databases

eggNOGiKOG1882. Eukaryota.
ENOG4111F4H. LUCA.
GeneTreeiENSGT00730000110659.
HOGENOMiHOG000264922.
HOVERGENiHBG056615.
InParanoidiQ8BIZ6.
KOiK13108.
OMAiKNDEFLP.
OrthoDBiEOG7P02K5.
PhylomeDBiQ8BIZ6.
TreeFamiTF312797.

Miscellaneous databases

PROiQ8BIZ6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BIZ6.
CleanExiMM_SNIP1.
GenevisibleiQ8BIZ6. MM.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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.
    Tissue: Embryonic stem cell, Spleen, Testis and Thymus.
  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: C57BL/6J.
    Tissue: Mammary gland.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "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-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-48 AND SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiSNIP1_MOUSE
AccessioniPrimary (citable) accession number: Q8BIZ6
Secondary accession number(s): Q3V106, Q8BIZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 110 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.