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Q9NQ55 (SSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Suppressor of SWI4 1 homolog

Short name=Ssf-1
Alternative name(s):
Brix domain-containing protein 3
Peter Pan homolog
Gene names
Name:PPAN
Synonyms:BXDC3, SSF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May have a role in cell growth.

Subcellular location

Nucleusnucleolus Ref.5.

Tissue specificity

Widely expressed. Ref.1 Ref.4

Miscellaneous

A chimeric transcript, characterized by the first third of PPAN exon 12 joined to P2RY11 exon 2, has been detected. It is possibly produced by trans-splicing. The chimeric transcript is widely expressed and can be induced by retinoic acid during the granulocytic differentiation of the HL-60 cell line. The resulting chimeric protein shows a much lower activity than the non-chimeric P2RY11 gene product, but qualitatively indistinguishable (Ref.4).

Sequence similarities

Contains 1 Brix domain.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 15302935. Source: MGI

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NQ55-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NQ55-2)

The sequence of this isoform differs from the canonical sequence as follows:
     444-456: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9NQ55-3)

The sequence of this isoform differs from the canonical sequence as follows:
     448-473: ARRGPRGASRDGGRGRGRGRPGKRVA → VPSPALPTSW...SWQSATCSAP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Suppressor of SWI4 1 homolog
PRO_0000120257

Regions

Domain29 – 292264Brix

Amino acid modifications

Modified residue2381Phosphoserine Ref.10 Ref.13 Ref.14 Ref.16
Modified residue2401Phosphoserine Ref.10 Ref.13 Ref.14 Ref.16
Modified residue3591Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.16
Modified residue4381N6-acetyllysine By similarity

Natural variations

Alternative sequence444 – 45613Missing in isoform 2.
VSP_003973
Alternative sequence448 – 47326ARRGP…GKRVA → VPSPALPTSWQLPTTNSVGS RGTSCGPYWWLSSWWPWPAM AWPCTASASGSSAHGTPPWS SLSSWQSATCSAP in isoform 3.
VSP_046377
Natural variant3581G → V.
Corresponds to variant rs2305793 [ dbSNP | Ensembl ].
VAR_022157
Natural variant4081Q → R.
Corresponds to variant rs11559188 [ dbSNP | Ensembl ].
VAR_048422

Experimental info

Isoform 3:
Sequence conflict5201P → L in BC171852. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9FF7B7201BD37BEC

FASTA47353,194
        10         20         30         40         50         60 
MGQSGRSRHQ KRARAQAQLR NLEAYAANPH SFVFTRGCTG RNIRQLSLDV RRVMEPLTAS 

        70         80         90        100        110        120 
RLQVRKKNSL KDCVAVAGPL GVTHFLILSK TETNVYFKLM RLPGGPTLTF QVKKYSLVRD 

       130        140        150        160        170        180 
VVSSLRRHRM HEQQFAHPPL LVLNSFGPHG MHVKLMATMF QNLFPSINVH KVNLNTIKRC 

       190        200        210        220        230        240 
LLIDYNPDSQ ELDFRHYSIK VVPVGASRGM KKLLQEKFPN MSRLQDISEL LATGAGLSES 

       250        260        270        280        290        300 
EAEPDGDHNI TELPQAVAGR GNMRAQQSAV RLTEIGPRMT LQLIKVQEGV GEGKVMFHSF 

       310        320        330        340        350        360 
VSKTEEELQA ILEAKEKKLR LKAQRQAQQA QNVQRKQEQR EAHRKKSLEG MKKARVGGSD 

       370        380        390        400        410        420 
EEASGIPSRT ASLELGEDDD EQEDDDIEYF CQAVGEAPSE DLFPEAKQKR LAKSPGRKRK 

       430        440        450        460        470 
RWEMDRGRGR LCDQKFPKTK DKSQGAQARR GPRGASRDGG RGRGRGRPGK RVA 

« Hide

Isoform 2 [UniParc].

Checksum: DEDA8FEF86C6575D
Show »

FASTA46051,900
Isoform 3 [UniParc].

Checksum: B5EE1A65E9E13B5E
Show »

FASTA52058,199

References

« Hide 'large scale' references
[1]"Cloning, genomic organization, and tissue distribution of human Ssf-1."
Suarez-Huerta N., Boeynaems J.-M., Communi D.
Biochem. Biophys. Res. Commun. 275:37-42(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Placenta.
[2]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1; 2 AND 3).
Tissue: Brain, Placenta and Skin.
[4]"Cotranscription and intergenic splicing of human P2Y11 and SSF1 genes."
Communi D., Suarez-Huerta N., Dussossoy D., Savi P., Boeynaems J.-M.
J. Biol. Chem. 276:16561-16566(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-427, TISSUE SPECIFICITY, TRANS-SPLICING.
Tissue: Placenta.
[5]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-238; SER-240 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238; SER-240 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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-238; SER-240 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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-238; SER-240 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ292529 mRNA. Translation: CAB99252.1.
AC020931 Genomic DNA. No translation available.
BC000535 mRNA. Translation: AAH00535.2.
BC009833 mRNA. Translation: AAH09833.1.
BC033202 mRNA. Translation: AAH33202.1.
BC171852 mRNA. No translation available.
AJ300588 mRNA. Translation: CAC18877.1. Different termination.
PIRJC7359.
RefSeqNP_001035754.1. NM_001040664.2.
NP_001185619.1. NM_001198690.1.
NP_064615.3. NM_020230.5.
UniGeneHs.14468.

3D structure databases

ProteinModelPortalQ9NQ55.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121141. 12 interactions.
593098. 1 interaction.
IntActQ9NQ55. 7 interactions.
MINTMINT-3072003.
STRING9606.ENSP00000253107.

PTM databases

PhosphoSiteQ9NQ55.

Polymorphism databases

DMDM21264056.

2D gel databases

SWISS-2DPAGEQ9NQ55.

Proteomic databases

PaxDbQ9NQ55.
PRIDEQ9NQ55.

Protocols and materials databases

DNASU56342.
692312.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253107; ENSP00000253107; ENSG00000130810. [Q9NQ55-1]
GeneID56342.
692312.
KEGGhsa:56342.
hsa:692312.
UCSCuc002mmz.2. human. [Q9NQ55-1]

Organism-specific databases

CTD56342.
692312.
GeneCardsGC19P010216.
GC19P010217.
HGNCHGNC:9227. PPAN.
HPAHPA043265.
MIM607793. gene.
neXtProtNX_Q9NQ55.
PharmGKBPA162399971.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG272199.
HOGENOMHOG000210038.
HOVERGENHBG026954.
InParanoidQ9NQ55.
KOK14859.
OMALGVTHLM.
PhylomeDBQ9NQ55.
TreeFamTF318923.

Gene expression databases

ArrayExpressQ9NQ55.
BgeeQ9NQ55.
CleanExHS_PPAN.
GenevestigatorQ9NQ55.

Family and domain databases

InterProIPR007109. Brix.
[Graphical view]
PfamPF04427. Brix. 1 hit.
[Graphical view]
SMARTSM00879. Brix. 1 hit.
[Graphical view]
PROSITEPS50833. BRIX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPAN. human.
GeneWikiPPAN.
NextBio124574.
PROQ9NQ55.
SOURCESearch...

Entry information

Entry nameSSF1_HUMAN
AccessionPrimary (citable) accession number: Q9NQ55
Secondary accession number(s): C9J3F9, Q9BW97, Q9H170
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 120 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 19

Human chromosome 19: entries, gene names and cross-references to MIM