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Q8TAD8

- SNIP1_HUMAN

UniProt

Q8TAD8 - SNIP1_HUMAN

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Protein
Smad nuclear-interacting protein 1
Gene
SNIP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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. 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.4 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: IntAct

GO - Biological processi

  1. I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  2. production of miRNAs involved in gene silencing by miRNA Source: UniProtKB
  3. regulation of transcription, DNA-templated Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

RNA-mediated gene silencing

Enzyme and pathway databases

SignaLinkiQ8TAD8.

Names & Taxonomyi

Protein namesi
Recommended name:
Smad nuclear-interacting protein 1
Alternative name(s):
FHA domain-containing protein SNIP1
Gene namesi
Name:SNIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:30587. SNIP1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Psychomotor retardation, epilepsy, and craniofacial dysmorphism (PMRED) [MIM:614501]: A disease characterized by severe psychomotor retardation, intractable seizures, dysmorphic features, and a lumpy skull surface. Patients are hypotonic and have poor feeding in the neonatal period.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti366 – 3661E → G in PMRED. 1 Publication
VAR_067542

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301K → R: Abolishes sumoylation. 1 Publication

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

MIMi614501. phenotype.
PharmGKBiPA142670893.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Smad nuclear-interacting protein 1
PRO_0000072009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki30 – 30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei35 – 351Phosphoserine3 Publications
Modified residuei49 – 491Phosphoserine1 Publication
Modified residuei52 – 521Phosphoserine2 Publications
Modified residuei54 – 541Phosphoserine2 Publications
Modified residuei394 – 3941Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8TAD8.
PaxDbiQ8TAD8.
PRIDEiQ8TAD8.

PTM databases

PhosphoSiteiQ8TAD8.

Expressioni

Tissue specificityi

Ubiquitous, with highest expression in heart and skeletal muscle.1 Publication

Gene expression databases

ArrayExpressiQ8TAD8.
BgeeiQ8TAD8.
CleanExiHS_SNIP1.
GenevestigatoriQ8TAD8.

Organism-specific databases

HPAiHPA036896.

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IKQ131232EBI-749336,EBI-713456
MYCP011069EBI-749336,EBI-447544
SNW1Q135737EBI-749336,EBI-632715

Protein-protein interaction databases

BioGridi122864. 27 interactions.
DIPiDIP-38956N.
IntActiQ8TAD8. 41 interactions.
MINTiMINT-1181692.
STRINGi9606.ENSP00000296215.

Structurei

3D structure databases

ProteinModelPortaliQ8TAD8.
SMRiQ8TAD8. Positions 246-374.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini281 – 34464FHA
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili165 – 19632 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi62 – 192131Arg-rich
Add
BLAST
Compositional biasi385 – 3928Poly-Glu

Sequence similaritiesi

Contains 1 FHA domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG271234.
HOGENOMiHOG000264922.
HOVERGENiHBG056615.
InParanoidiQ8TAD8.
KOiK13108.
OMAiGQEHRRA.
OrthoDBiEOG7P02K5.
PhylomeDBiQ8TAD8.
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.

Q8TAD8-1 [UniParc]FASTAAdd to Basket

« Hide

MKAVKSERER GSRRRHRDGD VVLPAGVVVK QERLSPEVAP PAHRRPDHSG    50
GSPSPPTSEP ARSGHRGNRA RGVSRSPPKK KNKASGRRSK SPRSKRNRSP 100
HHSTVKVKQE REDHPRRGRE DRQHREPSEQ EHRRARNSDR DRHRGHSHQR 150
RTSNERPGSG QGQGRDRDTQ NLQAQEEERE FYNARRREHR QRNDVGGGGS 200
ESQELVPRPG GNNKEKEVPA KEKPSFELSG ALLEDTNTFR GVVIKYSEPP 250
EARIPKKRWR LYPFKNDEVL PVMYIHRQSA YLLGRHRRIA DIPIDHPSCS 300
KQHAVFQYRL VEYTRADGTV GRRVKPYIID LGSGNGTFLN NKRIEPQRYY 350
ELKEKDVLKF GFSSREYVLL HESSDTSEID RKDDEDEEEE EEVSDS 396
Length:396
Mass (Da):45,778
Last modified:June 1, 2002 - v1
Checksum:iB183F83EC3184676
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti366 – 3661E → G in PMRED. 1 Publication
VAR_067542

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811F → S in BAB55241. 1 Publication
Sequence conflicti364 – 3641S → I in BAB14134. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY081909 mRNA. Translation: AAL91140.1.
AK022615 mRNA. Translation: BAB14134.1.
AK027622 mRNA. Translation: BAB55241.1.
BC027040 mRNA. Translation: AAH27040.1.
CCDSiCCDS419.1.
RefSeqiNP_078976.2. NM_024700.3.
UniGeneiHs.47232.

Genome annotation databases

EnsembliENST00000296215; ENSP00000296215; ENSG00000163877.
GeneIDi79753.
KEGGihsa:79753.
UCSCiuc001cbi.4. human.

Polymorphism databases

DMDMi48428655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY081909 mRNA. Translation: AAL91140.1 .
AK022615 mRNA. Translation: BAB14134.1 .
AK027622 mRNA. Translation: BAB55241.1 .
BC027040 mRNA. Translation: AAH27040.1 .
CCDSi CCDS419.1.
RefSeqi NP_078976.2. NM_024700.3.
UniGenei Hs.47232.

3D structure databases

ProteinModelPortali Q8TAD8.
SMRi Q8TAD8. Positions 246-374.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122864. 27 interactions.
DIPi DIP-38956N.
IntActi Q8TAD8. 41 interactions.
MINTi MINT-1181692.
STRINGi 9606.ENSP00000296215.

PTM databases

PhosphoSitei Q8TAD8.

Polymorphism databases

DMDMi 48428655.

Proteomic databases

MaxQBi Q8TAD8.
PaxDbi Q8TAD8.
PRIDEi Q8TAD8.

Protocols and materials databases

DNASUi 79753.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296215 ; ENSP00000296215 ; ENSG00000163877 .
GeneIDi 79753.
KEGGi hsa:79753.
UCSCi uc001cbi.4. human.

Organism-specific databases

CTDi 79753.
GeneCardsi GC01M038002.
HGNCi HGNC:30587. SNIP1.
HPAi HPA036896.
MIMi 608241. gene.
614501. phenotype.
neXtProti NX_Q8TAD8.
PharmGKBi PA142670893.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271234.
HOGENOMi HOG000264922.
HOVERGENi HBG056615.
InParanoidi Q8TAD8.
KOi K13108.
OMAi GQEHRRA.
OrthoDBi EOG7P02K5.
PhylomeDBi Q8TAD8.
TreeFami TF312797.

Enzyme and pathway databases

SignaLinki Q8TAD8.

Miscellaneous databases

ChiTaRSi SNIP1. human.
GeneWikii SNIP1.
GenomeRNAii 79753.
NextBioi 69203.
PROi Q8TAD8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8TAD8.
Bgeei Q8TAD8.
CleanExi HS_SNIP1.
Genevestigatori Q8TAD8.

Family and domain databases

Gene3Di 2.60.200.20. 1 hit.
InterProi IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view ]
Pfami PF00498. FHA. 1 hit.
[Graphical view ]
SMARTi SM00240. FHA. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
PROSITEi PS50006. FHA_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel Smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction."
    Kim R.H., Wang D., Tsang M., Martin J., Huff C., de Caestecker M.P., Parks T.W., Meng X., Lechleider R.J., Wang T., Roberts A.B.
    Genes Dev. 14:1605-1616(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SMAD4 AND CREBBP/EP300, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Embryonic kidney.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Teratocarcinoma.
  3. "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: Testis.
  4. "SNIP1 inhibits NF-kappa B signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators."
    Kim R.H., Flanders K.C., Birkey Reffey S., Anderson L.A., Duckett C.S., Perkins N.D., Roberts A.B.
    J. Biol. Chem. 276:46297-46304(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CREBBP AND EP300.
  5. "A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs)."
    Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y., Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T.
    BMC Cell Biol. 3:15-15(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE SMAD1/OAZ1/PSMB4 COMPLEX, DEGRADATION BY THE PROTEASOME.
  6. "The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression."
    Roche K.C., Wiechens N., Owen-Hughes T., Perkins N.D.
    Oncogene 23:8185-8195(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SMARCA4.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: SUMOYLATION AT LYS-30, MUTAGENESIS OF LYS-30.
  9. Cited for: FUNCTION, IDENTIFICATION IN THE SNARP COMPLEX.
  10. "The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in small RNA biogenesis."
    Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M., Ramachandran V., Li W., Lagrange T., Walker J.C., Chen X.
    Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DROSHA.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-52 AND SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: VARIANT PMRED GLY-366.

Entry informationi

Entry nameiSNIP1_HUMAN
AccessioniPrimary (citable) accession number: Q8TAD8
Secondary accession number(s): Q96SP9, Q9H9T7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2002
Last modified: September 3, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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