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Protein

Paraspeckle component 1

Gene

PSPC1

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

Functioni

Regulates, cooperatively with NONO and SFPQ, androgen receptor-mediated gene transcription activity in Sertoli cell line (By similarity). Binds to poly(A), poly(G) and poly(U) RNA homopolymers. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer (By similarity). Together with NONO, required for the formation of nuclear paraspeckles.By similarity1 Publication

GO - Molecular functioni

  • core promoter binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Paraspeckle component 1
Alternative name(s):
Paraspeckle protein 1
Gene namesi
Name:PSPC1
Synonyms:PSP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:20320. PSPC1.

Subcellular locationi

  • Nucleusnucleolus
  • Nucleus matrix By similarity
  • Cytoplasm By similarity
  • Nucleus speckle

  • Note: In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Colocalizes with NONO and SFPQ in paraspeckles and perinucleolar caps in an RNA-dependent manner. May cycles between paraspeckles and nucleolus. In telophase, when daughter nuclei form, localizes to perinucleolar caps.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi119 – 1191F → A: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-121; A-198 and A-200. 1 Publication
Mutagenesisi121 – 1211F → A: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-198 and A-200. 1 Publication
Mutagenesisi198 – 1981K → A: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-121 and A-200. 1 Publication
Mutagenesisi200 – 2001F → A: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-121 and A-198. 1 Publication
Mutagenesisi275 – 2751Y → A: Abolishes interaction with NONO and localization in nuclear paraspeckles; when associated with A-279. 1 Publication
Mutagenesisi279 – 2791W → A: Abolishes interaction with NONO and localization in nuclear paraspeckles; when associated with A-275. 1 Publication

Organism-specific databases

PharmGKBiPA134968603.

Polymorphism and mutation databases

BioMutaiPSPC1.
DMDMi74762636.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 523523Paraspeckle component 1PRO_0000297540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei409 – 4091Phosphoserine1 Publication
Modified residuei473 – 4731Phosphoserine1 Publication
Modified residuei477 – 4771Phosphoserine1 Publication
Modified residuei509 – 5091Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8WXF1.
PaxDbiQ8WXF1.
PRIDEiQ8WXF1.

PTM databases

PhosphoSiteiQ8WXF1.

Expressioni

Tissue specificityi

Expressed in pancreas, kidney, skeletal muscle, liver, lung, placenta, brain and heart.1 Publication

Gene expression databases

BgeeiQ8WXF1.
CleanExiHS_PSPC1.
ExpressionAtlasiQ8WXF1. baseline and differential.
GenevisibleiQ8WXF1. HS.

Organism-specific databases

HPAiHPA038904.

Interactioni

Subunit structurei

Forms heterodimers with NONO; this involves formation of a coiled coil domain by helices from both proteins. Found in a RNP complex with CAT2 transcribed nuclear RNA (CTN-RNA). Interaction with NONO is required for its targeting to paraspeckles and perinucleolar caps. Interacts with SFPQ (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT31Q153233EBI-1392258,EBI-948001
NONOQ1523311EBI-1392258,EBI-350527
NONOQ15233-23EBI-1392258,EBI-10203843

Protein-protein interaction databases

BioGridi120558. 28 interactions.
DIPiDIP-39028N.
IntActiQ8WXF1. 10 interactions.
MINTiMINT-1395719.
STRINGi9606.ENSP00000343966.

Structurei

Secondary structure

1
523
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi80 – 823Combined sources
Beta strandi83 – 886Combined sources
Helixi95 – 1017Combined sources
Helixi102 – 1054Combined sources
Beta strandi109 – 1146Combined sources
Turni115 – 1184Combined sources
Beta strandi119 – 1235Combined sources
Helixi127 – 13711Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi155 – 1628Combined sources
Helixi169 – 1768Combined sources
Helixi177 – 1793Combined sources
Beta strandi182 – 1909Combined sources
Beta strandi195 – 20511Combined sources
Helixi206 – 21813Combined sources
Beta strandi221 – 2266Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi238 – 2425Combined sources
Helixi246 – 2483Combined sources
Helixi253 – 2597Combined sources
Beta strandi263 – 2653Combined sources
Helixi271 – 31848Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SDEX-ray1.90A61-320[»]
ProteinModelPortaliQ8WXF1.
SMRiQ8WXF1. Positions 66-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 15473RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini156 – 23782RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 358234Sufficient for paraspeckles localizationAdd
BLAST
Regioni231 – 358128Sufficient for perinucleolar caps localization and interaction with NONOAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili283 – 37795Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi394 – 516123Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the PSPC family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG298586.
GeneTreeiENSGT00390000005004.
HOGENOMiHOG000231095.
HOVERGENiHBG009801.
InParanoidiQ8WXF1.
OMAiMDNREQE.
OrthoDBiEOG7327P0.
PhylomeDBiQ8WXF1.
TreeFamiTF315795.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WXF1-1) [UniParc]FASTAAdd to basket

Also known as: PSP1-alpha

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
MMLRGNLKQV RIEKNPARLR ALESAVGESE PAAAAAMALA LAGEPAPPAP
60 70 80 90 100
APPEDHPDEE MGFTIDIKSF LKPGEKTYTQ RCRLFVGNLP TDITEEDFKR
110 120 130 140 150
LFERYGEPSE VFINRDRGFG FIRLESRTLA EIAKAELDGT ILKSRPLRIR
160 170 180 190 200
FATHGAALTV KNLSPVVSNE LLEQAFSQFG PVEKAVVVVD DRGRATGKGF
210 220 230 240 250
VEFAAKPPAR KALERCGDGA FLLTTTPRPV IVEPMEQFDD EDGLPEKLMQ
260 270 280 290 300
KTQQYHKERE QPPRFAQPGT FEFEYASRWK ALDEMEKQQR EQVDRNIREA
310 320 330 340 350
KEKLEAEMEA ARHEHQLMLM RQDLMRRQEE LRRLEELRNQ ELQKRKQIQL
360 370 380 390 400
RHEEEHRRRE EEMIRHREQE ELRRQQEGFK PNYMENREQE MRMGDMGPRG
410 420 430 440 450
AINMGDAFSP APAGNQGPPP MMGMNMNNRA TIPGPPMGPG PAMGPEGAAN
460 470 480 490 500
MGTPMMPDNG AVHNDRFPQG PPSQMGSPMG SRTGSETPQA PMSGVGPVSG
510 520
GPGGFGRGSQ GGNFEGPNKR RRY
Length:523
Mass (Da):58,744
Last modified:March 1, 2002 - v1
Checksum:i3A8C44079D64BBF0
GO
Isoform 2 (identifier: Q8WXF1-2) [UniParc]FASTAAdd to basket

Also known as: PSP1-beta

The sequence of this isoform differs from the canonical sequence as follows:
     387-393: REQEMRM → GDKRKCG
     394-523: Missing.

Show »
Length:393
Mass (Da):45,571
Checksum:i67F1A7EBF93050B2
GO

Sequence cautioni

The sequence BAA91924.1 differs from that shown. Reason: Erroneous termination at position 14. Translated as Lys.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei387 – 3937REQEMRM → GDKRKCG in isoform 2. 5 PublicationsVSP_027274
Alternative sequencei394 – 523130Missing in isoform 2. 5 PublicationsVSP_027275Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF448795 mRNA. Translation: AAL59601.1.
AF449627 mRNA. Translation: AAL59602.1.
AK001817 mRNA. Translation: BAA91924.1. Sequence problems.
AL354808 Genomic DNA. Translation: CAI41004.1.
AL354808 Genomic DNA. Translation: CAI41005.1.
CH471075 Genomic DNA. Translation: EAX08232.1.
BC014184 mRNA. Translation: AAH14184.2.
CR457272 mRNA. Translation: CAG33553.1.
AL834505 mRNA. Translation: CAD39162.1.
CCDSiCCDS41870.1. [Q8WXF1-1]
RefSeqiNP_001035879.1. NM_001042414.2. [Q8WXF1-1]
XP_006719907.1. XM_006719844.2. [Q8WXF1-1]
UniGeneiHs.213198.

Genome annotation databases

EnsembliENST00000338910; ENSP00000343966; ENSG00000121390. [Q8WXF1-1]
ENST00000471658; ENSP00000436038; ENSG00000121390. [Q8WXF1-2]
ENST00000492741; ENSP00000435921; ENSG00000121390. [Q8WXF1-2]
ENST00000619300; ENSP00000481916; ENSG00000121390. [Q8WXF1-1]
GeneIDi55269.
KEGGihsa:55269.
UCSCiuc021rgx.1. human. [Q8WXF1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF448795 mRNA. Translation: AAL59601.1.
AF449627 mRNA. Translation: AAL59602.1.
AK001817 mRNA. Translation: BAA91924.1. Sequence problems.
AL354808 Genomic DNA. Translation: CAI41004.1.
AL354808 Genomic DNA. Translation: CAI41005.1.
CH471075 Genomic DNA. Translation: EAX08232.1.
BC014184 mRNA. Translation: AAH14184.2.
CR457272 mRNA. Translation: CAG33553.1.
AL834505 mRNA. Translation: CAD39162.1.
CCDSiCCDS41870.1. [Q8WXF1-1]
RefSeqiNP_001035879.1. NM_001042414.2. [Q8WXF1-1]
XP_006719907.1. XM_006719844.2. [Q8WXF1-1]
UniGeneiHs.213198.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SDEX-ray1.90A61-320[»]
ProteinModelPortaliQ8WXF1.
SMRiQ8WXF1. Positions 66-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120558. 28 interactions.
DIPiDIP-39028N.
IntActiQ8WXF1. 10 interactions.
MINTiMINT-1395719.
STRINGi9606.ENSP00000343966.

PTM databases

PhosphoSiteiQ8WXF1.

Polymorphism and mutation databases

BioMutaiPSPC1.
DMDMi74762636.

Proteomic databases

MaxQBiQ8WXF1.
PaxDbiQ8WXF1.
PRIDEiQ8WXF1.

Protocols and materials databases

DNASUi55269.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338910; ENSP00000343966; ENSG00000121390. [Q8WXF1-1]
ENST00000471658; ENSP00000436038; ENSG00000121390. [Q8WXF1-2]
ENST00000492741; ENSP00000435921; ENSG00000121390. [Q8WXF1-2]
ENST00000619300; ENSP00000481916; ENSG00000121390. [Q8WXF1-1]
GeneIDi55269.
KEGGihsa:55269.
UCSCiuc021rgx.1. human. [Q8WXF1-1]

Organism-specific databases

CTDi55269.
GeneCardsiGC13M020249.
H-InvDBHIX0011177.
HGNCiHGNC:20320. PSPC1.
HPAiHPA038904.
MIMi612408. gene.
neXtProtiNX_Q8WXF1.
PharmGKBiPA134968603.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG298586.
GeneTreeiENSGT00390000005004.
HOGENOMiHOG000231095.
HOVERGENiHBG009801.
InParanoidiQ8WXF1.
OMAiMDNREQE.
OrthoDBiEOG7327P0.
PhylomeDBiQ8WXF1.
TreeFamiTF315795.

Miscellaneous databases

ChiTaRSiPSPC1. human.
GenomeRNAii55269.
NextBioi59380.
PROiQ8WXF1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WXF1.
CleanExiHS_PSPC1.
ExpressionAtlasiQ8WXF1. baseline and differential.
GenevisibleiQ8WXF1. HS.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 21-83; 105-124; 135-143; 185-194; 199-210; 252-259; 265-289; 327-345; 352-357; 366-374 AND 483-507, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  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] (ISOFORM 2).
    Tissue: Placenta.
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Skin.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-523 (ISOFORM 2).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-523 (ISOFORM 2).
    Tissue: Kidney.
  8. "P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner."
    Fox A.H., Bond C.S., Lamond A.I.
    Mol. Biol. Cell 16:5304-5315(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH NONO, MUTAGENESIS OF PHE-119; PHE-121; LYS-198 AND PHE-200, SUBCELLULAR LOCATION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-409; SER-473 AND SER-477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation."
    Passon D.M., Lee M., Rackham O., Stanley W.A., Sadowska A., Filipovska A., Fox A.H., Bond C.S.
    Proc. Natl. Acad. Sci. U.S.A. 109:4846-4850(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 61-320 IN COMPLEX WITH NONO, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-275 AND TRP-279.

Entry informationi

Entry nameiPSPC1_HUMAN
AccessioniPrimary (citable) accession number: Q8WXF1
Secondary accession number(s): Q5JTQ3
, Q8NCZ9, Q8WXE8, Q9NV36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: March 1, 2002
Last modified: June 24, 2015
This is version 127 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.