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Protein

Plasminogen activator inhibitor 1 RNA-binding protein

Gene

SERBP1

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

Functioni

May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay.

GO - Molecular functioni

  • mRNA 3'-UTR binding Source: HGNC
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • regulation of apoptotic process Source: Ensembl
  • regulation of mRNA stability Source: HGNC
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Plasminogen activator inhibitor 1 RNA-binding protein
Alternative name(s):
PAI1 RNA-binding protein 1
Short name:
PAI-RBP1
SERPINE1 mRNA-binding protein 1
Gene namesi
Name:SERBP1
Synonyms:PAIRBP1
ORF Names:CGI-55
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17860. SERBP1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication
  • Cytoplasmperinuclear region 1 Publication

  • Note: Also found in perinuclear regions.

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA413.

Polymorphism and mutation databases

BioMutaiSERBP1.
DMDMi52783206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 408407Plasminogen activator inhibitor 1 RNA-binding proteinPRO_0000058182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphoserine2 Publications
Modified residuei52 – 521N6-acetyllysineBy similarity
Modified residuei68 – 681N6-acetyllysine1 Publication
Modified residuei122 – 1221N6-acetyllysine1 Publication
Modified residuei140 – 1401N6-acetyllysine1 Publication
Modified residuei211 – 2111N6-acetyllysine1 Publication
Modified residuei234 – 2341Phosphoserine2 Publications
Modified residuei329 – 3291N6-acetyllysineBy similarity
Modified residuei330 – 3301Phosphoserine2 Publications
Modified residuei392 – 3921Phosphoserine1 Publication
Modified residuei394 – 3941Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8NC51.
PaxDbiQ8NC51.
PRIDEiQ8NC51.

PTM databases

PhosphoSiteiQ8NC51.

Expressioni

Tissue specificityi

Expressed at high level in the heart, skeletal muscle and kidney, and at low levels in placenta, liver and brain.1 Publication

Gene expression databases

BgeeiQ8NC51.
CleanExiHS_SERBP1.
ExpressionAtlasiQ8NC51. baseline and differential.
GenevisibleiQ8NC51. HS.

Organism-specific databases

HPAiCAB026297.
HPA020559.

Interactioni

Subunit structurei

Interacts with SPIN1 (By similarity). Interacts with CHD3 and TDRD3.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHD3Q128735EBI-523558,EBI-523590

Protein-protein interaction databases

BioGridi117571. 75 interactions.
DIPiDIP-33819N.
IntActiQ8NC51. 33 interactions.
MINTiMINT-1373976.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Ah1-408[»]
ProteinModelPortaliQ8NC51.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiNOG321910.
GeneTreeiENSGT00520000055591.
HOVERGENiHBG056357.
InParanoidiQ8NC51.
KOiK13199.
OMAiANRTREF.
OrthoDBiEOG71P2BG.
PhylomeDBiQ8NC51.
TreeFamiTF318374.

Family and domain databases

InterProiIPR006861. HABP4_PAIRBP1-bd.
IPR027205. SERBP1.
[Graphical view]
PANTHERiPTHR12299:SF22. PTHR12299:SF22. 1 hit.
PfamiPF04774. HABP4_PAI-RBP1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NC51-1) [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
MPGHLQEGFG CVVTNRFDQL FDDESDPFEV LKAAENKKKE AGGGGVGGPG
60 70 80 90 100
AKSAAQAAAQ TNSNAAGKQL RKESQKDRKN PLPPSVGVVD KKEETQPPVA
110 120 130 140 150
LKKEGIRRVG RRPDQQLQGE GKIIDRRPER RPPRERRFEK PLEEKGEGGE
160 170 180 190 200
FSVDRPIIDR PIRGRGGLGR GRGGRGRGMG RGDGFDSRGK REFDRHSGSD
210 220 230 240 250
RSSFSHYSGL KHEDKRGGSG SHNWGTVKDE LTESPKYIQK QISYNYSDLD
260 270 280 290 300
QSNVTEETPE GEEHHPVADT ENKENEVEEV KEEGPKEMTL DEWKAIQNKD
310 320 330 340 350
RAKVEFNIRK PNEGADGQWK KGFVLHKSKS EEAHAEDSVM DHHFRKPAND
360 370 380 390 400
ITSQLEINFG DLGRPGRGGR GGRGGRGRGG RPNRGSRTDK SSASAPDVDD

PEAFPALA
Length:408
Mass (Da):44,965
Last modified:September 27, 2004 - v2
Checksum:i2289992374FA6A96
GO
Isoform 2 (identifier: Q8NC51-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     203-208: Missing.

Note: May be due to a competing acceptor splice site.
Show »
Length:402
Mass (Da):44,257
Checksum:iB5DBDE629FC4EC7A
GO
Isoform 3 (identifier: Q8NC51-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     233-247: Missing.

Note: May be due to a competing acceptor splice site. Contains a phosphoserine at position 237. Contains a phosphothreonine at position 240.2 Publications
Show »
Length:393
Mass (Da):43,135
Checksum:iABE09AC75FE95CBC
GO
Isoform 4 (identifier: Q8NC51-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     203-208: Missing.
     233-247: Missing.

Note: Contains a phosphoserine at position 231. Contains a phosphothreonine at position 234.2 Publications
Show »
Length:387
Mass (Da):42,427
Checksum:i8C47134D22C1CCFA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551A → T in AAD34050 (PubMed:10810093).Curated
Sequence conflicti101 – 1011L → F in AAD34050 (PubMed:10810093).Curated
Sequence conflicti312 – 3121N → S in BAC11324 (PubMed:14702039).Curated
Sequence conflicti376 – 3761R → C in AAH02488 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei203 – 2086Missing in isoform 2 and isoform 4. 3 PublicationsVSP_011630
Alternative sequencei233 – 24715Missing in isoform 3 and isoform 4. 5 PublicationsVSP_011631Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151813 mRNA. Translation: AAD34050.1.
AL080119 mRNA. Translation: CAB45718.1.
AK074970 mRNA. Translation: BAC11324.1.
CR457383 mRNA. Translation: CAG33664.1.
AL590559 Genomic DNA. Translation: CAH73323.1.
AL590559 Genomic DNA. Translation: CAH73324.1.
AL590559 Genomic DNA. Translation: CAH73326.1.
BC003049 mRNA. Translation: AAH03049.1.
BC008045 mRNA. Translation: AAH08045.1.
BC017449 mRNA. Translation: AAH17449.1.
BC019273 mRNA. Translation: AAH19273.1.
BC020555 mRNA. Translation: AAH20555.1.
BC002488 mRNA. Translation: AAH02488.1.
BC026916 mRNA. Translation: AAH26916.1.
AY032853 mRNA. Translation: AAK51130.1.
CCDSiCCDS30746.1. [Q8NC51-1]
CCDS30747.1. [Q8NC51-3]
CCDS30748.1. [Q8NC51-2]
CCDS639.1. [Q8NC51-4]
PIRiT12456.
RefSeqiNP_001018077.1. NM_001018067.1. [Q8NC51-1]
NP_001018078.1. NM_001018068.1. [Q8NC51-2]
NP_001018079.1. NM_001018069.1. [Q8NC51-3]
NP_056455.3. NM_015640.3. [Q8NC51-4]
UniGeneiHs.530412.

Genome annotation databases

EnsembliENST00000361219; ENSP00000354591; ENSG00000142864. [Q8NC51-3]
ENST00000370990; ENSP00000360029; ENSG00000142864. [Q8NC51-2]
ENST00000370994; ENSP00000360033; ENSG00000142864. [Q8NC51-4]
ENST00000370995; ENSP00000360034; ENSG00000142864. [Q8NC51-1]
GeneIDi26135.
KEGGihsa:26135.
UCSCiuc001ddv.3. human. [Q8NC51-1]
uc001ddw.3. human. [Q8NC51-3]
uc001ddx.3. human. [Q8NC51-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151813 mRNA. Translation: AAD34050.1.
AL080119 mRNA. Translation: CAB45718.1.
AK074970 mRNA. Translation: BAC11324.1.
CR457383 mRNA. Translation: CAG33664.1.
AL590559 Genomic DNA. Translation: CAH73323.1.
AL590559 Genomic DNA. Translation: CAH73324.1.
AL590559 Genomic DNA. Translation: CAH73326.1.
BC003049 mRNA. Translation: AAH03049.1.
BC008045 mRNA. Translation: AAH08045.1.
BC017449 mRNA. Translation: AAH17449.1.
BC019273 mRNA. Translation: AAH19273.1.
BC020555 mRNA. Translation: AAH20555.1.
BC002488 mRNA. Translation: AAH02488.1.
BC026916 mRNA. Translation: AAH26916.1.
AY032853 mRNA. Translation: AAK51130.1.
CCDSiCCDS30746.1. [Q8NC51-1]
CCDS30747.1. [Q8NC51-3]
CCDS30748.1. [Q8NC51-2]
CCDS639.1. [Q8NC51-4]
PIRiT12456.
RefSeqiNP_001018077.1. NM_001018067.1. [Q8NC51-1]
NP_001018078.1. NM_001018068.1. [Q8NC51-2]
NP_001018079.1. NM_001018069.1. [Q8NC51-3]
NP_056455.3. NM_015640.3. [Q8NC51-4]
UniGeneiHs.530412.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00Ah1-408[»]
ProteinModelPortaliQ8NC51.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117571. 75 interactions.
DIPiDIP-33819N.
IntActiQ8NC51. 33 interactions.
MINTiMINT-1373976.

PTM databases

PhosphoSiteiQ8NC51.

Polymorphism and mutation databases

BioMutaiSERBP1.
DMDMi52783206.

Proteomic databases

MaxQBiQ8NC51.
PaxDbiQ8NC51.
PRIDEiQ8NC51.

Protocols and materials databases

DNASUi26135.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361219; ENSP00000354591; ENSG00000142864. [Q8NC51-3]
ENST00000370990; ENSP00000360029; ENSG00000142864. [Q8NC51-2]
ENST00000370994; ENSP00000360033; ENSG00000142864. [Q8NC51-4]
ENST00000370995; ENSP00000360034; ENSG00000142864. [Q8NC51-1]
GeneIDi26135.
KEGGihsa:26135.
UCSCiuc001ddv.3. human. [Q8NC51-1]
uc001ddw.3. human. [Q8NC51-3]
uc001ddx.3. human. [Q8NC51-2]

Organism-specific databases

CTDi26135.
GeneCardsiGC01M067873.
HGNCiHGNC:17860. SERBP1.
HPAiCAB026297.
HPA020559.
MIMi607378. gene.
neXtProtiNX_Q8NC51.
PharmGKBiPA413.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG321910.
GeneTreeiENSGT00520000055591.
HOVERGENiHBG056357.
InParanoidiQ8NC51.
KOiK13199.
OMAiANRTREF.
OrthoDBiEOG71P2BG.
PhylomeDBiQ8NC51.
TreeFamiTF318374.

Miscellaneous databases

ChiTaRSiSERBP1. human.
GeneWikiiSERBP1.
GenomeRNAii26135.
NextBioi48165.
PROiQ8NC51.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NC51.
CleanExiHS_SERBP1.
ExpressionAtlasiQ8NC51. baseline and differential.
GenevisibleiQ8NC51. HS.

Family and domain databases

InterProiIPR006861. HABP4_PAIRBP1-bd.
IPR027205. SERBP1.
[Graphical view]
PANTHERiPTHR12299:SF22. PTHR12299:SF22. 1 hit.
PfamiPF04774. HABP4_PAI-RBP1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Brain.
  3. "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 1).
    Tissue: Teratocarcinoma.
  4. "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] (ISOFORM 4).
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 4).
    Tissue: Colon, Lung, Placenta, Prostate and Skin.
  7. Bienvenut W.V.
    Submitted (JAN-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 40-52; 137-145; 287-294 AND 304-309, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  8. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-32; 93-103; 146-160; 217-236; 274-286; 304-309 AND 328-364, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  9. "Homo sapiens CGI-55 protein mRNA."
    Spiridonov N.A., Wong L., Johnson G.R.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-408 (ISOFORM 3).
  10. "Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3."
    Lemos T.A., Passos D.O., Nery F.C., Kobarg J.
    FEBS Lett. 533:14-20(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH CHD3.
  11. "Identification and cDNA cloning of a novel RNA-binding protein that interacts with the cyclic nucleotide-responsive sequence in the type-1 plasminogen activator inhibitor mRNA."
    Heaton J.H., Dlakic W.M., Dlakic M., Gelehrter T.D.
    J. Biol. Chem. 276:3341-3347(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SERPINE1 MRNA.
  12. "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-237 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules."
    Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.
    Hum. Mol. Genet. 17:3055-3074(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TDRD3.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234; SER-330 AND SER-394, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND THR-240 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND THR-234 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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].
  17. "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-25; SER-234; SER-392 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-122; LYS-140 AND LYS-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-330 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPAIRB_HUMAN
AccessioniPrimary (citable) accession number: Q8NC51
Secondary accession number(s): Q5VU19
, Q5VU20, Q5VU22, Q8WUH0, Q96SE2, Q9BTY3, Q9BUM4, Q9Y367, Q9Y4S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: June 24, 2015
This is version 131 of the entry and version 2 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 1
    Human chromosome 1: 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

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.