Reviewed, UniProtKB/Swiss-Prot Q8TAD8 (SNIP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Smad nuclear-interacting protein 1

Gene names

Name:

SNIP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Down-regulates NF-kappa-B signaling by competing with RELA for CREBBP/EP300 binding. Ref.4
Subunit structure	Binds SMAD4 and CREBBP/EP300. Binds the SMAD1/OAZ1/PSMB4 complex.
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. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Sequence similarities	Contains 1 FHA domain.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Coiled coil
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAX	P61244	1	EBI-749336,EBI-878388
MYC	P01106	5	EBI-749336,EBI-447544
RNASEN	Q9NRR4	1	EBI-749336,EBI-528367

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 396	396	Smad nuclear-interacting protein 1		PRO_0000072009
Regions
	Domain	281 – 344	64	FHA
	Coiled coil	165 – 196	32	Potential
	Compositional bias	62 – 192	131	Arg-rich
	Compositional bias	385 – 392	8	Poly-Glu
Amino acid modifications
	Modified residue	35	1	Phosphoserine Ref.6 Ref.9 Ref.10 Ref.12
	Modified residue	49	1	Phosphoserine Ref.12
	Modified residue	52	1	Phosphoserine Ref.12 Ref.13
	Modified residue	54	1	Phosphoserine Ref.12 Ref.13
	Modified residue	89	1	Phosphoserine Ref.6
	Modified residue	91	1	Phosphoserine Ref.6
	Modified residue	153	1	Phosphoserine Ref.6
	Modified residue	169	1	Phosphothreonine Ref.8
	Modified residue	202	1	Phosphoserine Ref.8
	Modified residue	394	1	Phosphoserine Ref.11
	Cross-link	30		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7
Experimental info
	Mutagenesis	30	1	K → R: Abolishes sumoylation. Ref.7
	Sequence conflict	181	1	F → S in BAB55241. Ref.2
	Sequence conflict	364	1	S → I in BAB14134. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8TAD8-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: B183F83EC3184676	FASTA	396	45,778
	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

References

	« Hide 'large scale' referencesShow '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: 10887155] [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: 14702039] [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: 15489334] [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: 11567019] [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: 12097147] [Abstract] Cited for: INTERACTION WITH THE SMAD1/OAZ1/PSMB4 COMPLEX, DEGRADATION BY THE PROTEASOME.
[6]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-89; SER-91 AND SER-153, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"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: 16371476] [Abstract] Cited for: SUMOYLATION AT LYS-30, MUTAGENESIS OF LYS-30.
[8]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169 AND SER-202, MASS SPECTROMETRY.
[9]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY.
[10]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY.
[11]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, MASS SPECTROMETRY. Tissue: T-cell.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-49; SER-52 AND SER-54, MASS SPECTROMETRY.
[13]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-54, MASS SPECTROMETRY. Tissue: T-cell.

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.
IPI	IPI00154515.
RefSeq	NP_078976.2.
UniGene	Hs.471951
3D structure databases
SMR	Q8TAD8. Positions 236-370.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38956N.
IntAct	Q8TAD8. 6 interactions.
STRING	Q8TAD8.
PTM databases
PhosphoSite	Q8TAD8.
Proteomic databases
PRIDE	Q8TAD8.
Genome annotation databases
Ensembl	ENST00000296215; ENSP00000296215; ENSG00000163877; Homo sapiens. [Genome view]
GeneID	79753.
KEGG	hsa:79753.
UCSC	uc001cbi.1. human.
Organism-specific databases
CTD	79753.
GeneCards	GC01M037774.
H-InvDB	HIX0000434.
HGNC	HGNC:30587. SNIP1.
MIM	608241. gene.
PharmGKB	PA142670893.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08408.
HOGENOM	HBG717219.
HOVERGEN	Q8TAD8.
InParanoid	Q8TAD8.
OMA	KQEREDH.
OrthoDB	EOG9B2WH7.
PhylomeDB	Q8TAD8.
Enzyme and pathway databases
Pathway_Interaction_DB	smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
Gene expression databases
ArrayExpress	Q8TAD8.
Bgee	Q8TAD8.
CleanEx	HS_SNIP1.
Genevestigator	Q8TAD8.
GermOnline	ENSG00000163877. Homo sapiens.
Family and domain databases
InterPro	IPR000253. FHA. IPR008984. SMAD_FHA_domain. [Graphical view]
Gene3D	G3DSA:2.60.200.20. FHA. 1 hit.
Pfam	PF00498. FHA. 1 hit. [Graphical view]
SMART	SM00240. FHA. 1 hit. [Graphical view]
PROSITE	PS50006. FHA_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	69203.
SOURCE	Search...

Entry information

Entry name

SNIP1_HUMAN

Accession

Primary (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:	February 9, 2010
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.