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Q9NQ55

- SSF1_HUMAN

UniProt

Q9NQ55 - SSF1_HUMAN

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Protein

Suppressor of SWI4 1 homolog

Gene

PPAN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

May have a role in cell growth.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. RNA splicing Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of SWI4 1 homolog
Short name:
Ssf-1
Alternative name(s):
Brix domain-containing protein 3
Peter Pan homolog
Gene namesi
Name:PPAN
Synonyms:BXDC3, SSF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9227. PPAN.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162399971.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Suppressor of SWI4 1 homologPRO_0000120257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei238 – 2381Phosphoserine4 Publications
Modified residuei240 – 2401Phosphoserine4 Publications
Modified residuei359 – 3591Phosphoserine8 Publications
Modified residuei438 – 4381N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NQ55.
PaxDbiQ9NQ55.
PRIDEiQ9NQ55.

2D gel databases

SWISS-2DPAGEQ9NQ55.

PTM databases

PhosphoSiteiQ9NQ55.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiQ9NQ55.
CleanExiHS_PPAN.
ExpressionAtlasiQ9NQ55. baseline and differential.
GenevestigatoriQ9NQ55.

Organism-specific databases

HPAiHPA043265.

Interactioni

Protein-protein interaction databases

BioGridi121141. 14 interactions.
593098. 11 interactions.
IntActiQ9NQ55. 7 interactions.
MINTiMINT-3072003.
STRINGi9606.ENSP00000253107.

Structurei

3D structure databases

ProteinModelPortaliQ9NQ55.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 292264BrixPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Brix domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG272199.
GeneTreeiENSGT00530000064158.
HOGENOMiHOG000210038.
HOVERGENiHBG026954.
InParanoidiQ9NQ55.
KOiK14859.
OMAiLGVTHLM.
PhylomeDBiQ9NQ55.
TreeFamiTF318923.

Family and domain databases

InterProiIPR007109. Brix.
[Graphical view]
PfamiPF04427. Brix. 1 hit.
[Graphical view]
SMARTiSM00879. Brix. 1 hit.
[Graphical view]
PROSITEiPS50833. BRIX. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NQ55-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGQSGRSRHQ KRARAQAQLR NLEAYAANPH SFVFTRGCTG RNIRQLSLDV
60 70 80 90 100
RRVMEPLTAS RLQVRKKNSL KDCVAVAGPL GVTHFLILSK TETNVYFKLM
110 120 130 140 150
RLPGGPTLTF QVKKYSLVRD VVSSLRRHRM HEQQFAHPPL LVLNSFGPHG
160 170 180 190 200
MHVKLMATMF QNLFPSINVH KVNLNTIKRC LLIDYNPDSQ ELDFRHYSIK
210 220 230 240 250
VVPVGASRGM KKLLQEKFPN MSRLQDISEL LATGAGLSES EAEPDGDHNI
260 270 280 290 300
TELPQAVAGR GNMRAQQSAV RLTEIGPRMT LQLIKVQEGV GEGKVMFHSF
310 320 330 340 350
VSKTEEELQA ILEAKEKKLR LKAQRQAQQA QNVQRKQEQR EAHRKKSLEG
360 370 380 390 400
MKKARVGGSD EEASGIPSRT ASLELGEDDD EQEDDDIEYF CQAVGEAPSE
410 420 430 440 450
DLFPEAKQKR LAKSPGRKRK RWEMDRGRGR LCDQKFPKTK DKSQGAQARR
460 470
GPRGASRDGG RGRGRGRPGK RVA
Length:473
Mass (Da):53,194
Last modified:October 1, 2000 - v1
Checksum:i9FF7B7201BD37BEC
GO
Isoform 2 (identifier: Q9NQ55-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     444-456: Missing.

Note: No experimental confirmation available.

Show »
Length:460
Mass (Da):51,900
Checksum:iDEDA8FEF86C6575D
GO
Isoform 3 (identifier: Q9NQ55-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     448-473: ARRGPRGASRDGGRGRGRGRPGKRVA → VPSPALPTSW...SWQSATCSAP

Note: No experimental confirmation available.Curated

Show »
Length:520
Mass (Da):58,199
Checksum:iB5EE1A65E9E13B5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 3 (identifier: Q9NQ55-3)
Sequence conflicti520 – 5201P → L in BC171852. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti358 – 3581G → V.
Corresponds to variant rs2305793 [ dbSNP | Ensembl ].
VAR_022157
Natural varianti408 – 4081Q → R.
Corresponds to variant rs11559188 [ dbSNP | Ensembl ].
VAR_048422

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei444 – 45613Missing in isoform 2. 1 PublicationVSP_003973Add
BLAST
Alternative sequencei448 – 47326ARRGP…GKRVA → VPSPALPTSWQLPTTNSVGS RGTSCGPYWWLSSWWPWPAM AWPCTASASGSSAHGTPPWS SLSSWQSATCSAP in isoform 3. 1 PublicationVSP_046377Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12225.1. [Q9NQ55-1]
PIRiJC7359.
RefSeqiNP_001035754.1. NM_001040664.2.
NP_001185619.1. NM_001198690.1. [Q9NQ55-3]
NP_064615.3. NM_020230.5. [Q9NQ55-1]
UniGeneiHs.14468.

Genome annotation databases

EnsembliENST00000253107; ENSP00000253107; ENSG00000130810. [Q9NQ55-1]
GeneIDi56342.
692312.
KEGGihsa:56342.
hsa:692312.
UCSCiuc002mmz.2. human. [Q9NQ55-1]

Polymorphism databases

DMDMi21264056.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS12225.1. [Q9NQ55-1 ]
PIRi JC7359.
RefSeqi NP_001035754.1. NM_001040664.2.
NP_001185619.1. NM_001198690.1. [Q9NQ55-3 ]
NP_064615.3. NM_020230.5. [Q9NQ55-1 ]
UniGenei Hs.14468.

3D structure databases

ProteinModelPortali Q9NQ55.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121141. 14 interactions.
593098. 11 interactions.
IntActi Q9NQ55. 7 interactions.
MINTi MINT-3072003.
STRINGi 9606.ENSP00000253107.

PTM databases

PhosphoSitei Q9NQ55.

Polymorphism databases

DMDMi 21264056.

2D gel databases

SWISS-2DPAGE Q9NQ55.

Proteomic databases

MaxQBi Q9NQ55.
PaxDbi Q9NQ55.
PRIDEi Q9NQ55.

Protocols and materials databases

DNASUi 56342.
692312.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253107 ; ENSP00000253107 ; ENSG00000130810 . [Q9NQ55-1 ]
GeneIDi 56342.
692312.
KEGGi hsa:56342.
hsa:692312.
UCSCi uc002mmz.2. human. [Q9NQ55-1 ]

Organism-specific databases

CTDi 56342.
692312.
GeneCardsi GC19P010216.
HGNCi HGNC:9227. PPAN.
HPAi HPA043265.
MIMi 607793. gene.
neXtProti NX_Q9NQ55.
PharmGKBi PA162399971.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG272199.
GeneTreei ENSGT00530000064158.
HOGENOMi HOG000210038.
HOVERGENi HBG026954.
InParanoidi Q9NQ55.
KOi K14859.
OMAi LGVTHLM.
PhylomeDBi Q9NQ55.
TreeFami TF318923.

Miscellaneous databases

ChiTaRSi PPAN. human.
GeneWikii PPAN.
NextBioi 124574.
PROi Q9NQ55.
SOURCEi Search...

Gene expression databases

Bgeei Q9NQ55.
CleanExi HS_PPAN.
ExpressionAtlasi Q9NQ55. baseline and differential.
Genevestigatori Q9NQ55.

Family and domain databases

InterProi IPR007109. Brix.
[Graphical view ]
Pfami PF04427. Brix. 1 hit.
[Graphical view ]
SMARTi SM00879. Brix. 1 hit.
[Graphical view ]
PROSITEi PS50833. BRIX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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].

Entry informationi

Entry nameiSSF1_HUMAN
AccessioniPrimary (citable) accession number: Q9NQ55
Secondary accession number(s): C9J3F9, Q9BW97, Q9H170
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 126 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

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 (PubMed:11278528).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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