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Q9H307 (PININ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PNN
Synonyms:DRS, MEMA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length717 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.3 Ref.12 Ref.16 Ref.19 Ref.20 Ref.32

Subunit structure

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. Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.32

Subcellular location

Nucleus speckle. Cell junctiondesmosome. Note: Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein. Ref.1 Ref.8 Ref.10 Ref.12 Ref.15 Ref.16 Ref.17 Ref.20

Tissue specificity

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. Ref.1 Ref.2 Ref.8

Sequence similarities

Belongs to the pinin family.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentCell junction
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainCoiled coil
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Traceable author statement Ref.1. Source: ProtInc

mRNA splicing, via spliceosome

Inferred by curator Ref.13. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.13. Source: UniProtKB

cell-cell junction

Traceable author statement Ref.1. Source: ProtInc

cytoplasm

Inferred from electronic annotation. Source: Ensembl

desmosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

intermediate filament

Traceable author statement Ref.11. Source: ProtInc

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

structural molecule activity

Non-traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NFKBIL1Q9UBC11EBI-681904,EBI-1043728
RNPS1Q152871EBI-681904,EBI-395959

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H307-1)

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.
Isoform 2 (identifier: Q9H307-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 717716Pinin
PRO_0000190242

Regions

Region2 – 284283Necessary for interaction with RNPS1
Region2 – 167166Necessary for mediating alternative 5' splicing
Region2 – 9897Necessary for interactions with KRT8, KRT18 and KRT19
Region221 – 28464Sufficient for PSAP complex assembly
Region606 – 717112Necessary for interaction with PPIG
Coiled coil2 – 3231 Potential
Coiled coil163 – 23472 Potential
Coiled coil287 – 37993 Potential
Coiled coil446 – 46722 Potential
Compositional bias172 – 471300Glu-rich
Compositional bias469 – 52052Gln-rich
Compositional bias552 – 704153Ser-rich
Compositional bias632 – 71786Arg-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.26
Modified residue581Phosphoserine Ref.31
Modified residue661Phosphoserine Ref.23 Ref.25 Ref.29 Ref.31
Modified residue961Phosphoserine Ref.29
Modified residue1001Phosphoserine Ref.22 Ref.25 Ref.29 Ref.31
Modified residue1141Phosphoserine Ref.29
Modified residue1151Phosphoserine Ref.29
Modified residue1241Phosphothreonine Ref.29
Modified residue2381N6-acetyllysine; alternate Ref.28
Modified residue2381N6-succinyllysine; alternate By similarity
Modified residue3471Phosphoserine Ref.22 Ref.29 Ref.31
Modified residue3751Phosphoserine Ref.25
Modified residue3811Phosphoserine Ref.22 Ref.27 Ref.29 Ref.31
Modified residue4431Phosphoserine Ref.25 Ref.27 Ref.29
Modified residue4501Phosphoserine Ref.25 Ref.29 Ref.31
Modified residue5521Phosphoserine Ref.25 Ref.29
Modified residue6581Phosphoserine Ref.31
Modified residue6921Phosphoserine Ref.31
Modified residue6951Phosphoserine Ref.31

Natural variations

Alternative sequence1 – 133133Missing in isoform 2.
VSP_015307
Natural variant4411S → T.
Corresponds to variant rs2180792 [ dbSNP | Ensembl ].
VAR_050540
Natural variant6711S → G. Ref.2 Ref.6
Corresponds to variant rs13021 [ dbSNP | Ensembl ].
VAR_023368

Experimental info

Mutagenesis81L → P: Abolishes interaction with KRT18. Ref.11 Ref.19
Mutagenesis191L → P: Abolishes interaction with KRT18. Ref.11 Ref.19
Mutagenesis502 – 5032PE → AA: Abolishes interaction with CTBP1 and shows moderate relief of CTBP1-mediated repression. Ref.19
Sequence conflict691Missing in AAB48304. Ref.1
Sequence conflict1681K → N in AAB48304. Ref.1
Sequence conflict2681E → D in AAB48304. Ref.1
Sequence conflict3031Q → H in AAB48304. Ref.1
Sequence conflict3201E → V in AAB48304. Ref.1
Sequence conflict3431A → G in AAB48304. Ref.1
Sequence conflict402 – 4032DQ → EE in AAG33941. Ref.3
Sequence conflict4591E → D in AAB48304. Ref.1
Sequence conflict4781P → A in AAB48304. Ref.1
Sequence conflict491 – 4922QP → EPQPQLQPEPAQPQLQSQPQ LQLQSQCHA AA sequence Ref.1
Sequence conflict4971Q → H in AAB48304. Ref.1
Sequence conflict5201Q → H in AAB48304. Ref.1
Sequence conflict5231L → F in AAB48304. Ref.1
Sequence conflict5411P → T AA sequence Ref.1
Sequence conflict5431E → D in AAB48304. Ref.1
Sequence conflict5471T → I AA sequence Ref.1
Sequence conflict5501P → S AA sequence Ref.1
Sequence conflict5511E → D AA sequence Ref.1
Sequence conflict553 – 5575KSKTK → ESETN in AAB48304. Ref.1
Sequence conflict5661A → T in AAB48304. Ref.1
Sequence conflict569 – 5713KTS → RTT in AAB48304. Ref.1
Sequence conflict6181S → G in AAF17209. Ref.4
Sequence conflict6181S → G in CAA71377. Ref.8
Sequence conflict6261S → STS in CAA70874. Ref.2
Sequence conflict6641H → P in AAG33941. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 1C05E1E12F54299F

FASTA71781,614
        10         20         30         40         50         60 
MAVAVRTLQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP GGGRGRGSLL 

        70         80         90        100        110        120 
LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES DPEDDDVKKP ALQSSVVATS 

       130        140        150        160        170        180 
KERTRRDLIQ DQNMDEKGKQ RNRRIFGLLM GTLQKFKQES TVATERQKRR QEIEQKLEVQ 

       190        200        210        220        230        240 
AEEERKQVEN ERRELFEERR AKQTELRLLE QKVELAQLQE EWNEHNAKII KYIRTKTKPH 

       250        260        270        280        290        300 
LFYIPGRMCP ATQKLIEESQ RKMNALFEGR RIEFAEQINK MEARPRRQSM KEKEHQVVRN 

       310        320        330        340        350        360 
EEQKAEQEEG KVAQREEELE ETGNQHNDVE IEEAGEEEEK EIAIVHSDAE KEQEEEEQKQ 

       370        380        390        400        410        420 
EMEVKMEEET EVRESEKQQD SQPEEVMDVL EMVENVKHVI ADQEVMETNR VESVEPSENE 

       430        440        450        460        470        480 
ASKELEPEME FEIEPDKECK SLSPGKENVS ALDMEKESEE KEEKESEPQP EPVAQPQPQS 

       490        500        510        520        530        540 
QPQLQLQSQS QPVLQSQPPS QPEDLSLAVL QPTPQVTQEQ GHLLPERKDF PVESVKLTEV 

       550        560        570        580        590        600 
PVEPVLTVHP ESKSKTKTRS RSRGRARNKT SKSRSRSSSS SSSSSSSTSS SSGSSSSSGS 

       610        620        630        640        650        660 
SSSRSSSSSS SSTSGSSSRD SSSSTSSSSE SRSRSRGRGH NRDRKHRRSV DRKRRDTSGL 

       670        680        690        700        710 
ERSHKSSKGG SSRDTKGSKD KNSRSDRKRS ISESSRSGKR SSRSERDRKS DRKDKRR 

« Hide

Isoform 2 [UniParc].

Checksum: 7D96168629D5C4DA
Show »

FASTA58467,005

References

« Hide 'large scale' references
[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]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[25]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_002678.2. NM_002687.3.
UniGeneHs.409965.

3D structure databases

ProteinModelPortalQ9H307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111412. 35 interactions.
DIPDIP-32950N.
IntActQ9H307. 25 interactions.
MINTMINT-1683388.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteQ9H307.

Polymorphism databases

DMDM73921750.

Proteomic databases

PaxDbQ9H307.
PRIDEQ9H307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216832; ENSP00000216832; ENSG00000100941.
GeneID5411.
KEGGhsa:5411.
UCSCuc001wuw.4. human. [Q9H307-1]

Organism-specific databases

CTD5411.
GeneCardsGC14P039644.
H-InvDBHIX0037750.
HGNCHGNC:9162. PNN.
HPAHPA001378.
MIM603154. gene.
neXtProtNX_Q9H307.
PharmGKBPA33484.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249368.
HOVERGENHBG053104.
InParanoidQ9H307.
KOK13114.
OrthoDBEOG7DC25H.
PhylomeDBQ9H307.
TreeFamTF331859.

Gene expression databases

ArrayExpressQ9H307.
BgeeQ9H307.
CleanExHS_PNN.
GenevestigatorQ9H307.

Family and domain databases

InterProIPR006786. Pinin_SDK_MemA.
IPR006787. Pinin_SDK_N.
[Graphical view]
PfamPF04696. Pinin_SDK_memA. 1 hit.
PF04697. Pinin_SDK_N. 1 hit.
[Graphical view]
ProDomPD011048. Pinin_SDK_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

ChiTaRSPNN. human.
GeneWikiPinin.
GenomeRNAi5411.
NextBio20949.
PROQ9H307.
SOURCESearch...

Entry information

Entry namePININ_HUMAN
AccessionPrimary (citable) accession number: Q9H307
Secondary accession number(s): B4DZX8 expand/collapse secondary AC list , O60899, Q53EM7, Q6P5X4, Q7KYL1, Q99738, Q9UHZ9, Q9UQR9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 109 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM