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Q9H307

- PININ_HUMAN

UniProt

Q9H307 - PININ_HUMAN

Protein

Pinin

Gene

PNN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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.5 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

    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.

    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. membrane Source: UniProtKB
    7. nuclear speck Source: UniProtKB-SubCell
    8. nucleus Source: HPA
    9. plasma membrane Source: ProtInc

    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 – 11Removed2 Publications
    Chaini2 – 717716PininPRO_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; alternateBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 284283Necessary for interaction with RNPS1Add
    BLAST
    Regioni2 – 167166Necessary for mediating alternative 5' splicingAdd
    BLAST
    Regioni2 – 9897Necessary for interactions with KRT8, KRT18 and KRT19Add
    BLAST
    Regioni221 – 28464Sufficient for PSAP complex assemblyAdd
    BLAST
    Regioni606 – 717112Necessary for interaction with PPIGAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2 – 3231Sequence AnalysisAdd
    BLAST
    Coiled coili163 – 23472Sequence AnalysisAdd
    BLAST
    Coiled coili287 – 37993Sequence AnalysisAdd
    BLAST
    Coiled coili446 – 46722Sequence AnalysisAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the pinin family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691Missing in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti168 – 1681K → N in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti268 – 2681E → D in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti303 – 3031Q → H in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti320 – 3201E → V in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti343 – 3431A → G in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti402 – 4032DQ → EE in AAG33941. (PubMed:10645008)Curated
    Sequence conflicti459 – 4591E → D in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti478 – 4781P → A in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti491 – 4922QP → EPQPQLQPEPAQPQLQSQPQ LQLQSQCHA AA sequence (PubMed:8922384)Curated
    Sequence conflicti497 – 4971Q → H in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti520 – 5201Q → H in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti523 – 5231L → F in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti541 – 5411P → T AA sequence (PubMed:8922384)Curated
    Sequence conflicti543 – 5431E → D in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti547 – 5471T → I AA sequence (PubMed:8922384)Curated
    Sequence conflicti550 – 5501P → S AA sequence (PubMed:8922384)Curated
    Sequence conflicti551 – 5511E → D AA sequence (PubMed:8922384)Curated
    Sequence conflicti553 – 5575KSKTK → ESETN in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti566 – 5661A → T in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti569 – 5713KTS → RTT in AAB48304. (PubMed:8922384)Curated
    Sequence conflicti618 – 6181S → G in AAF17209. (PubMed:10931946)Curated
    Sequence conflicti618 – 6181S → G in CAA71377. (PubMed:9447706)Curated
    Sequence conflicti626 – 6261S → STS in CAA70874. (PubMed:10095061)Curated
    Sequence conflicti664 – 6641H → P in AAG33941. (PubMed:10645008)Curated

    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. 2 PublicationsVSP_015307Add
    BLAST

    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

    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: October 1, 2014
    This is version 113 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