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Protein

Smad nuclear interacting protein 1

Gene

Snip1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 2 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 - 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componentsi: Chromosome 15, Chromosome 5

Organism-specific databases

RGDi1359268. Snip1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 389389Smad nuclear interacting protein 1PRO_0000391412Add
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 SUMO2); alternateBy similarity
Modified residuei33 – 331PhosphoserineBy similarity
Modified residuei48 – 481PhosphoserineCombined sources
Modified residuei95 – 951PhosphoserineCombined sources
Cross-linki104 – 104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei149 – 1491PhosphoserineCombined sources
Modified residuei386 – 3861PhosphoserineBy 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

PaxDbiQ5M9G6.

PTM databases

iPTMnetiQ5M9G6.

Expressioni

Gene expression databases

GenevisibleiQ5M9G6. RN.

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

STRINGi10116.ENSRNOP00000064732.

Structurei

3D structure databases

ProteinModelPortaliQ5M9G6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini272 – 33564FHAPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili166 – 19732Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 524Poly-Pro
Compositional biasi62 – 184123Arg-richAdd
BLAST
Compositional biasi374 – 38310Poly-Glu

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1882. Eukaryota.
ENOG4111F4H. LUCA.
GeneTreeiENSGT00730000110659.
HOGENOMiHOG000264922.
HOVERGENiHBG056615.
InParanoidiQ5M9G6.
KOiK13108.
OMAiKNDEFLP.
OrthoDBiEOG7P02K5.
PhylomeDBiQ5M9G6.
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.

Q5M9G6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAGKSERER SSRRRHRSGD ALATVVVKQE RLSPEPVAHR RPDAPAASPP
60 70 80 90 100
PPAAESGSAG HRGSRARGAS RSPAKKKSKS SGRRSKSPRT KRSRSPHYST
110 120 130 140 150
VKVKQEREDH PRRGREDRQH RELSEQEHRR ARNSERDRHR GHARQRRSSD
160 170 180 190 200
ERPVSGQGRD RDSQILQAQE EERDFNNARR REHRQQNESA GAEAQEVIPR
210 220 230 240 250
PAGNKNKEVP VKEKPSFELS GALLEDTNTF RGVVIKYSEP PEARIPKKRW
260 270 280 290 300
RLYPFKNDEV LPVMYIHRQS AYLLGRHRRI ADIPIDHPSC SKQHAVFQYR
310 320 330 340 350
LVEYTRADGT VGRRVKPYII DLGSGNGTFL NNKRIEPQRY YELKEKDVLK
360 370 380
FGFSSREYVL LHESSDTSEL DRKEDEDEEE EEEMVSDSS
Length:389
Mass (Da):44,923
Last modified:February 1, 2005 - v1
Checksum:i6FFD73E2CA7BBAC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087118 mRNA. Translation: AAH87118.1.
RefSeqiNP_001014091.1. NM_001014069.1.
XP_003751496.1. XM_003751448.2.
UniGeneiRn.8811.

Genome annotation databases

EnsembliENSRNOT00000037510; ENSRNOP00000030728; ENSRNOG00000024889.
ENSRNOT00000075184; ENSRNOP00000064732; ENSRNOG00000046920.
GeneIDi100912429.
313588.
KEGGirno:100912429.
rno:313588.
UCSCiRGD:1359268. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087118 mRNA. Translation: AAH87118.1.
RefSeqiNP_001014091.1. NM_001014069.1.
XP_003751496.1. XM_003751448.2.
UniGeneiRn.8811.

3D structure databases

ProteinModelPortaliQ5M9G6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064732.

PTM databases

iPTMnetiQ5M9G6.

Proteomic databases

PaxDbiQ5M9G6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000037510; ENSRNOP00000030728; ENSRNOG00000024889.
ENSRNOT00000075184; ENSRNOP00000064732; ENSRNOG00000046920.
GeneIDi100912429.
313588.
KEGGirno:100912429.
rno:313588.
UCSCiRGD:1359268. rat.

Organism-specific databases

CTDi79753.
RGDi1359268. Snip1.

Phylogenomic databases

eggNOGiKOG1882. Eukaryota.
ENOG4111F4H. LUCA.
GeneTreeiENSGT00730000110659.
HOGENOMiHOG000264922.
HOVERGENiHBG056615.
InParanoidiQ5M9G6.
KOiK13108.
OMAiKNDEFLP.
OrthoDBiEOG7P02K5.
PhylomeDBiQ5M9G6.
TreeFamiTF312797.

Miscellaneous databases

PROiQ5M9G6.

Gene expression databases

GenevisibleiQ5M9G6. RN.

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 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: Lung.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-48; SER-95 AND SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSNIP1_RAT
AccessioniPrimary (citable) accession number: Q5M9G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: February 1, 2005
Last modified: June 8, 2016
This is version 82 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. 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.