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Q8TAD8 (SNIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Smad nuclear-interacting protein 1
Alternative name(s):
FHA domain-containing protein SNIP1
Gene names
Name:SNIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6 Ref.9 Ref.10

Subunit structure

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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.9 Ref.10

Subcellular location

Nucleus Ref.1.

Tissue specificity

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

Post-translational modification

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

Involvement in disease

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. Ref.16

Sequence similarities

Contains 1 FHA domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396Smad nuclear-interacting protein 1
PRO_0000072009

Regions

Domain281 – 34464FHA
Coiled coil165 – 19632 Potential
Compositional bias62 – 192131Arg-rich
Compositional bias385 – 3928Poly-Glu

Amino acid modifications

Modified residue351Phosphoserine Ref.7 Ref.13 Ref.14
Modified residue491Phosphoserine Ref.11
Modified residue521Phosphoserine Ref.11 Ref.12
Modified residue541Phosphoserine Ref.11 Ref.14
Modified residue3941Phosphoserine Ref.13
Cross-link30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8

Natural variations

Natural variant3661E → G in PMRED. Ref.16
VAR_067542

Experimental info

Mutagenesis301K → R: Abolishes sumoylation. Ref.8
Sequence conflict1811F → S in BAB55241. Ref.2
Sequence conflict3641S → I in BAB14134. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8TAD8 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B183F83EC3184676

FASTA39645,778
        10         20         30         40         50         60 
MKAVKSERER GSRRRHRDGD VVLPAGVVVK QERLSPEVAP PAHRRPDHSG GSPSPPTSEP 

        70         80         90        100        110        120 
ARSGHRGNRA RGVSRSPPKK KNKASGRRSK SPRSKRNRSP HHSTVKVKQE REDHPRRGRE 

       130        140        150        160        170        180 
DRQHREPSEQ EHRRARNSDR DRHRGHSHQR RTSNERPGSG QGQGRDRDTQ NLQAQEEERE 

       190        200        210        220        230        240 
FYNARRREHR QRNDVGGGGS ESQELVPRPG GNNKEKEVPA KEKPSFELSG ALLEDTNTFR 

       250        260        270        280        290        300 
GVVIKYSEPP EARIPKKRWR LYPFKNDEVL PVMYIHRQSA YLLGRHRRIA DIPIDHPSCS 

       310        320        330        340        350        360 
KQHAVFQYRL VEYTRADGTV GRRVKPYIID LGSGNGTFLN NKRIEPQRYY ELKEKDVLKF 

       370        380        390 
GFSSREYVLL HESSDTSEID RKDDEDEEEE EEVSDS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"PDSM, a motif for phosphorylation-dependent SUMO modification."
Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J., Nakai A., Sistonen L.
Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-30, MUTAGENESIS OF LYS-30.
[9]"Regulation of cyclin D1 RNA stability by SNIP1."
Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M., Perkins N.D.
Cancer Res. 68:7621-7628(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Genetic mapping and exome sequencing identify variants associated with five novel diseases."
Puffenberger E.G., Jinks R.N., Sougnez C., Cibulskis K., Willert R.A., Achilly N.P., Cassidy R.P., Fiorentini C.J., Heiken K.F., Lawrence J.J., Mahoney M.H., Miller C.J., Nair D.T., Politi K.A., Worcester K.N., Setton R.A., Dipiazza R., Sherman E.A. expand/collapse author list , Eastman J.T., Francklyn C., Robey-Bond S., Rider N.L., Gabriel S., Morton D.H., Strauss K.A.
PLoS ONE 7:E28936-E28936(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PMRED GLY-366.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY081909 mRNA. Translation: AAL91140.1.
AK022615 mRNA. Translation: BAB14134.1.
AK027622 mRNA. Translation: BAB55241.1.
BC027040 mRNA. Translation: AAH27040.1.
RefSeqNP_078976.2. NM_024700.3.
UniGeneHs.47232.

3D structure databases

ProteinModelPortalQ8TAD8.
SMRQ8TAD8. Positions 246-374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122864. 26 interactions.
DIPDIP-38956N.
IntActQ8TAD8. 41 interactions.
MINTMINT-1181692.
STRING9606.ENSP00000296215.

PTM databases

PhosphoSiteQ8TAD8.

Polymorphism databases

DMDM48428655.

Proteomic databases

PaxDbQ8TAD8.
PRIDEQ8TAD8.

Protocols and materials databases

DNASU79753.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296215; ENSP00000296215; ENSG00000163877.
GeneID79753.
KEGGhsa:79753.
UCSCuc001cbi.4. human.

Organism-specific databases

CTD79753.
GeneCardsGC01M038002.
HGNCHGNC:30587. SNIP1.
HPAHPA036896.
MIM608241. gene.
614501. phenotype.
neXtProtNX_Q8TAD8.
PharmGKBPA142670893.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271234.
HOGENOMHOG000264922.
HOVERGENHBG056615.
InParanoidQ8TAD8.
KOK13108.
OMAGQEHRRA.
OrthoDBEOG7P02K5.
PhylomeDBQ8TAD8.
TreeFamTF312797.

Enzyme and pathway databases

SignaLinkQ8TAD8.

Gene expression databases

ArrayExpressQ8TAD8.
BgeeQ8TAD8.
CleanExHS_SNIP1.
GenevestigatorQ8TAD8.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
InterProIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamPF00498. FHA. 1 hit.
[Graphical view]
SMARTSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
PROSITEPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNIP1. human.
GeneWikiSNIP1.
GenomeRNAi79753.
NextBio69203.
PROQ8TAD8.
SOURCESearch...

Entry information

Entry nameSNIP1_HUMAN
AccessionPrimary (citable) accession number: Q8TAD8
Secondary accession number(s): Q96SP9, Q9H9T7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM