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Q9H307

- PININ_HUMAN

UniProt

Q9H307 - PININ_HUMAN

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Protein
Pinin
Gene
PNN, DRS, MEMA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell-cell adhesion. Potential tumor suppressor for renal cell carcinoma.7 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB
  3. structural molecule activity Source: ProtInc

GO - Biological processi

  1. cell adhesion Source: ProtInc
  2. mRNA splicing, via spliceosome Source: UniProtKB
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Pinin
Alternative name(s):
140 kDa nuclear and cell adhesion-related phosphoprotein
Desmosome-associated protein
Domain-rich serine protein
Short name:
DRS protein
Short name:
DRSP
Melanoma metastasis clone A protein
Nuclear protein SDK3
SR-like protein
Gene namesi
Name:PNN
Synonyms:DRS, MEMA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:9162. PNN.

Subcellular locationi

Nucleus speckle. Cell junctiondesmosome
Note: Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein.8 Publications

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cell-cell junction Source: ProtInc
  3. cytoplasm Source: Ensembl
  4. desmosome Source: UniProtKB-SubCell
  5. intermediate filament Source: ProtInc
  6. nuclear speck Source: UniProtKB-SubCell
  7. nucleus Source: HPA
  8. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81L → P: Abolishes interaction with KRT18. 2 Publications
Mutagenesisi19 – 191L → P: Abolishes interaction with KRT18. 2 Publications
Mutagenesisi502 – 5032PE → AA: Abolishes interaction with CTBP1 and shows moderate relief of CTBP1-mediated repression. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA33484.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 717716Pinin
PRO_0000190242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei66 – 661Phosphoserine4 Publications
Modified residuei96 – 961Phosphoserine1 Publication
Modified residuei100 – 1001Phosphoserine4 Publications
Modified residuei114 – 1141Phosphoserine1 Publication
Modified residuei115 – 1151Phosphoserine1 Publication
Modified residuei124 – 1241Phosphothreonine1 Publication
Modified residuei238 – 2381N6-acetyllysine; alternate1 Publication
Modified residuei238 – 2381N6-succinyllysine; alternate By similarity
Modified residuei347 – 3471Phosphoserine3 Publications
Modified residuei375 – 3751Phosphoserine1 Publication
Modified residuei381 – 3811Phosphoserine4 Publications
Modified residuei443 – 4431Phosphoserine3 Publications
Modified residuei450 – 4501Phosphoserine3 Publications
Modified residuei552 – 5521Phosphoserine2 Publications
Modified residuei658 – 6581Phosphoserine1 Publication
Modified residuei692 – 6921Phosphoserine1 Publication
Modified residuei695 – 6951Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H307.
PaxDbiQ9H307.
PRIDEiQ9H307.

PTM databases

PhosphoSiteiQ9H307.

Expressioni

Tissue specificityi

Expressed in placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon, heart, epidermis, esophagus, brain and smooth and skeletal muscle. Expressed strongly in melanoma metastasis lesions and advanced primary tumors.3 Publications

Gene expression databases

ArrayExpressiQ9H307.
BgeeiQ9H307.
CleanExiHS_PNN.
GenevestigatoriQ9H307.

Organism-specific databases

HPAiHPA001378.

Interactioni

Subunit structurei

Found in a mRNA splicing-dependent exon junction complex (EJC). Found in a complex with SR proteins. Found in a mRNP complex with RNPS1. Component of the PSAP complex consisting of RNPS1, SAP18 and PNN. Interacts with PNISR, CTBP1, CTBP2, KRT8, KRT18, KRT19, PS1D/PNO40, PPIG, RNPS1, SFRS4 and SRRM2. Identified in the spliceosome C complex.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NFKBIL1Q9UBC11EBI-681904,EBI-1043728
RNPS1Q152871EBI-681904,EBI-395959

Protein-protein interaction databases

BioGridi111412. 35 interactions.
DIPiDIP-32950N.
IntActiQ9H307. 25 interactions.
MINTiMINT-1683388.

Structurei

3D structure databases

ProteinModelPortaliQ9H307.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 284283Necessary for interaction with RNPS1
Add
BLAST
Regioni2 – 167166Necessary for mediating alternative 5' splicing
Add
BLAST
Regioni2 – 9897Necessary for interactions with KRT8, KRT18 and KRT19
Add
BLAST
Regioni221 – 28464Sufficient for PSAP complex assembly
Add
BLAST
Regioni606 – 717112Necessary for interaction with PPIG
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2 – 3231 Reviewed prediction
Add
BLAST
Coiled coili163 – 23472 Reviewed prediction
Add
BLAST
Coiled coili287 – 37993 Reviewed prediction
Add
BLAST
Coiled coili446 – 46722 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi172 – 471300Glu-rich
Add
BLAST
Compositional biasi469 – 52052Gln-rich
Add
BLAST
Compositional biasi552 – 704153Ser-rich
Add
BLAST
Compositional biasi632 – 71786Arg-rich
Add
BLAST

Sequence similaritiesi

Belongs to the pinin family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG249368.
HOVERGENiHBG053104.
InParanoidiQ9H307.
KOiK13114.
OrthoDBiEOG7DC25H.
PhylomeDBiQ9H307.
TreeFamiTF331859.

Family and domain databases

InterProiIPR006786. Pinin_SDK_MemA.
IPR006787. Pinin_SDK_N.
[Graphical view]
PfamiPF04696. Pinin_SDK_memA. 1 hit.
PF04697. Pinin_SDK_N. 1 hit.
[Graphical view]
ProDomiPD011048. Pinin_SDK_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H307-1) [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

MAVAVRTLQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP    50
GGGRGRGSLL LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES 100
DPEDDDVKKP ALQSSVVATS KERTRRDLIQ DQNMDEKGKQ RNRRIFGLLM 150
GTLQKFKQES TVATERQKRR QEIEQKLEVQ AEEERKQVEN ERRELFEERR 200
AKQTELRLLE QKVELAQLQE EWNEHNAKII KYIRTKTKPH LFYIPGRMCP 250
ATQKLIEESQ RKMNALFEGR RIEFAEQINK MEARPRRQSM KEKEHQVVRN 300
EEQKAEQEEG KVAQREEELE ETGNQHNDVE IEEAGEEEEK EIAIVHSDAE 350
KEQEEEEQKQ EMEVKMEEET EVRESEKQQD SQPEEVMDVL EMVENVKHVI 400
ADQEVMETNR VESVEPSENE ASKELEPEME FEIEPDKECK SLSPGKENVS 450
ALDMEKESEE KEEKESEPQP EPVAQPQPQS QPQLQLQSQS QPVLQSQPPS 500
QPEDLSLAVL QPTPQVTQEQ GHLLPERKDF PVESVKLTEV PVEPVLTVHP 550
ESKSKTKTRS RSRGRARNKT SKSRSRSSSS SSSSSSSTSS SSGSSSSSGS 600
SSSRSSSSSS SSTSGSSSRD SSSSTSSSSE SRSRSRGRGH NRDRKHRRSV 650
DRKRRDTSGL ERSHKSSKGG SSRDTKGSKD KNSRSDRKRS ISESSRSGKR 700
SSRSERDRKS DRKDKRR 717
Length:717
Mass (Da):81,614
Last modified:January 23, 2007 - v4
Checksum:i1C05E1E12F54299F
GO
Isoform 2 (identifier: Q9H307-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Show »
Length:584
Mass (Da):67,005
Checksum:i7D96168629D5C4DA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti441 – 4411S → T.
Corresponds to variant rs2180792 [ dbSNP | Ensembl ].
VAR_050540
Natural varianti671 – 6711S → G.2 Publications
Corresponds to variant rs13021 [ dbSNP | Ensembl ].
VAR_023368

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 133133Missing in isoform 2.
VSP_015307Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691Missing in AAB48304. 1 Publication
Sequence conflicti168 – 1681K → N in AAB48304. 1 Publication
Sequence conflicti268 – 2681E → D in AAB48304. 1 Publication
Sequence conflicti303 – 3031Q → H in AAB48304. 1 Publication
Sequence conflicti320 – 3201E → V in AAB48304. 1 Publication
Sequence conflicti343 – 3431A → G in AAB48304. 1 Publication
Sequence conflicti402 – 4032DQ → EE in AAG33941. 1 Publication
Sequence conflicti459 – 4591E → D in AAB48304. 1 Publication
Sequence conflicti478 – 4781P → A in AAB48304. 1 Publication
Sequence conflicti491 – 4922QP → EPQPQLQPEPAQPQLQSQPQ LQLQSQCHA AA sequence 1 Publication
Sequence conflicti497 – 4971Q → H in AAB48304. 1 Publication
Sequence conflicti520 – 5201Q → H in AAB48304. 1 Publication
Sequence conflicti523 – 5231L → F in AAB48304. 1 Publication
Sequence conflicti541 – 5411P → T AA sequence 1 Publication
Sequence conflicti543 – 5431E → D in AAB48304. 1 Publication
Sequence conflicti547 – 5471T → I AA sequence 1 Publication
Sequence conflicti550 – 5501P → S AA sequence 1 Publication
Sequence conflicti551 – 5511E → D AA sequence 1 Publication
Sequence conflicti553 – 5575KSKTK → ESETN in AAB48304. 1 Publication
Sequence conflicti566 – 5661A → T in AAB48304. 1 Publication
Sequence conflicti569 – 5713KTS → RTT in AAB48304. 1 Publication
Sequence conflicti618 – 6181S → G in AAF17209. 1 Publication
Sequence conflicti618 – 6181S → G in CAA71377. 1 Publication
Sequence conflicti626 – 6261S → STS in CAA70874. 1 Publication
Sequence conflicti664 – 6641H → P in AAG33941. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U77718 mRNA. Translation: AAB48304.1.
Y09703 mRNA. Translation: CAA70874.1.
AF195139 Genomic DNA. Translation: AAG33941.1.
AF112222 mRNA. Translation: AAF17209.1.
AK303136 mRNA. Translation: BAG64240.1.
AK223612 mRNA. Translation: BAD97332.1.
BC062602 mRNA. Translation: AAH62602.1.
Y10351 mRNA. Translation: CAA71377.1.
CCDSiCCDS9671.1. [Q9H307-1]
RefSeqiNP_002678.2. NM_002687.3. [Q9H307-1]
UniGeneiHs.409965.

Genome annotation databases

EnsembliENST00000216832; ENSP00000216832; ENSG00000100941.
GeneIDi5411.
KEGGihsa:5411.
UCSCiuc001wuw.4. human. [Q9H307-1]

Polymorphism databases

DMDMi73921750.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U77718 mRNA. Translation: AAB48304.1 .
Y09703 mRNA. Translation: CAA70874.1 .
AF195139 Genomic DNA. Translation: AAG33941.1 .
AF112222 mRNA. Translation: AAF17209.1 .
AK303136 mRNA. Translation: BAG64240.1 .
AK223612 mRNA. Translation: BAD97332.1 .
BC062602 mRNA. Translation: AAH62602.1 .
Y10351 mRNA. Translation: CAA71377.1 .
CCDSi CCDS9671.1. [Q9H307-1 ]
RefSeqi NP_002678.2. NM_002687.3. [Q9H307-1 ]
UniGenei Hs.409965.

3D structure databases

ProteinModelPortali Q9H307.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111412. 35 interactions.
DIPi DIP-32950N.
IntActi Q9H307. 25 interactions.
MINTi MINT-1683388.

Protein family/group databases

TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSitei Q9H307.

Polymorphism databases

DMDMi 73921750.

Proteomic databases

MaxQBi Q9H307.
PaxDbi Q9H307.
PRIDEi Q9H307.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216832 ; ENSP00000216832 ; ENSG00000100941 .
GeneIDi 5411.
KEGGi hsa:5411.
UCSCi uc001wuw.4. human. [Q9H307-1 ]

Organism-specific databases

CTDi 5411.
GeneCardsi GC14P039644.
H-InvDB HIX0037750.
HGNCi HGNC:9162. PNN.
HPAi HPA001378.
MIMi 603154. gene.
neXtProti NX_Q9H307.
PharmGKBi PA33484.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249368.
HOVERGENi HBG053104.
InParanoidi Q9H307.
KOi K13114.
OrthoDBi EOG7DC25H.
PhylomeDBi Q9H307.
TreeFami TF331859.

Miscellaneous databases

ChiTaRSi PNN. human.
GeneWikii Pinin.
GenomeRNAii 5411.
NextBioi 20949.
PROi Q9H307.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H307.
Bgeei Q9H307.
CleanExi HS_PNN.
Genevestigatori Q9H307.

Family and domain databases

InterProi IPR006786. Pinin_SDK_MemA.
IPR006787. Pinin_SDK_N.
[Graphical view ]
Pfami PF04696. Pinin_SDK_memA. 1 hit.
PF04697. Pinin_SDK_N. 1 hit.
[Graphical view ]
ProDomi PD011048. Pinin_SDK_N. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of pinin, a novel protein associated with the desmosome-intermediate filament complex."
    Ouyang P., Sugrue S.P.
    J. Cell Biol. 135:1027-1042(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 44-50; 213-228 AND 537-553, PUTATIVE FUNCTION IN EPITHELIA MAINTENANCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Placenta.
  2. "memA/DRS, a putative mediator of multiprotein complexes, is overexpressed in the metastasizing human melanoma cell lines BLM and MV3."
    Degen W.G.J., Agterbos M.A., Muyrers J.P.P., Bloemers H.P.J., Swart G.W.M.
    Biochim. Biophys. Acta 1444:384-394(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLY-671, TISSUE SPECIFICITY.
    Tissue: Melanoma.
  3. "Characterization of the gene encoding pinin/DRS/memA and evidence for its potential tumor suppressor function."
    Shi Y., Ouyang P., Sugrue S.P.
    Oncogene 19:289-297(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PUTATIVE FUNCTION.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland.
  5. "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: Thymus.
  6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLY-671.
    Tissue: Brain.
  7. "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 1).
    Tissue: Eye.
  8. "Evidence that 'pinin', reportedly a differentiation-specific desmosomal protein, is actually a widespread nuclear protein."
    Brandner J., Reidenbach S., Franke W.W.
    Differentiation 62:119-127(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-717 (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Keratinocyte.
  9. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
    Submitted (MAY-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: T-cell.
  10. "Antibodies differentiate desmosome-form and nucleus-form pinin: evidence that pinin is a moonlighting protein with dual location at the desmosome and within the nucleus."
    Ouyang P.
    Biochem. Biophys. Res. Commun. 263:192-200(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus."
    Shi J., Sugrue S.P.
    J. Biol. Chem. 275:14910-14915(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KRT8; KRT18 AND KRT19, MUTAGENESIS OF LEU-8 AND LEU-19.
  12. "Modulation of alternative pre-mRNA splicing in vivo by pinin."
    Wang P., Lou P.-J., Leu S., Ouyang P.
    Biochem. Biophys. Res. Commun. 294:448-455(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PRE-MRNA SPLICING, SUBCELLULAR LOCATION.
  13. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  14. "Molecular characterization of a novel nucleolar protein, pNO40."
    Chang W.-L., Lee D.-C., Leu S., Huang Y.-M., Lu M.-C., Ouyang P.
    Biochem. Biophys. Res. Commun. 307:569-577(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PS1D/PNO40.
  15. "Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal epithelial cells."
    Zimowska G., Shi J., Munguba G., Jackson M.R., Alpatov R., Simmons M.N., Shi Y., Sugrue S.P.
    Invest. Ophthalmol. Vis. Sci. 44:4715-4723(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH SR PROTEINS, INTERACTION WITH PNISR; SFRS4 AND SRRM2, SUBCELLULAR LOCATION.
  16. "Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1."
    Li C., Lin R.-I., Lai M.-C., Ouyang P., Tarn W.-Y.
    Mol. Cell. Biol. 23:7363-7376(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PRE-MRNA SPLICING, IDENTIFICATION IN A MRNP COMPLEX WITH RNPS1, INTERACTION WITH RNPS1, SUBCELLULAR LOCATION.
  17. "Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles."
    Lin C.L., Leu S., Lu M.C., Ouyang P.
    Biochem. Biophys. Res. Commun. 321:638-647(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPIG, SUBCELLULAR LOCATION.
  18. "Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo."
    Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A.
    Mol. Cell. Biol. 24:1174-1187(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNPS1.
  19. "Nuclear speckle-associated protein Pnn/DRS binds to the transcriptional corepressor CtBP and relieves CtBP-mediated repression of the E-cadherin gene."
    Alpatov R., Munguba G.C., Caton P., Joo J.H., Shi Y., Shi Y., Hunt M.E., Sugrue S.P.
    Mol. Cell. Biol. 24:10223-10235(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTIONAL ACTIVATION, DNA-BINDING, INTERACTION WITH CTBP1 AND CTBP2, MUTAGENESIS OF 502-PRO-GLU-503.
  20. "Reduction of Pnn by RNAi induces loss of cell-cell adhesion between human corneal epithelial cells."
    Joo J.-H., Alpatov R., Munguba G.C., Jackson M.R., Hunt M.E., Sugrue S.P.
    Mol. Vis. 11:133-142(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL-CELL ADHESION, SUBCELLULAR LOCATION.
  21. "Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
    Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
    RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  22. "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-100; SER-347 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100; SER-375; SER-443; SER-450 AND SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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-381 AND SER-443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  28. "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-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "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-66; SER-96; SER-100; SER-114; SER-115; THR-124; SER-347; SER-381; SER-443; SER-450 AND SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "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-58; SER-66; SER-100; SER-347; SER-381; SER-450; SER-658; SER-692 AND SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex."
    Murachelli A.G., Ebert J., Basquin C., Le Hir H., Conti E.
    Nat. Struct. Mol. Biol. 19:378-386(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PSAP COMPLEX, FUNCTION OIF THE PSAP COMPLEX.

Entry informationi

Entry nameiPININ_HUMAN
AccessioniPrimary (citable) accession number: Q9H307
Secondary accession number(s): B4DZX8
, O60899, Q53EM7, Q6P5X4, Q7KYL1, Q99738, Q9UHZ9, Q9UQR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

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