Q9H307 (PININ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PNN
Synonyms:	DRS, MEMA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	717 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more 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. 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
Subunit structure	Found in a mRNA splicing-dependent exon junction complex (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, PNN, RBM8A, RNPS1, SAP18 and ALYREF/THOC4. Found in a complex with SR proteins. Found in a mRNP complex with RNPS1. 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
Subcellular location	Nucleus speckle. Cell junction › desmosome. 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 process	Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Cell junction Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Domain	Coiled coil
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Traceable author statement Ref.1. Source: ProtInc mRNA splicing, via spliceosome Inferred by curator Ref.13. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	catalytic 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: Compara 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 plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Non-traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NFKBIL1	Q9UBC1	1	EBI-681904,EBI-1043728
RNPS1	Q15287	1	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.9
	Chain	2 – 717	716	Pinin		PRO_0000190242
Regions
	Region	2 – 284	283	Necessary for interaction with RNPS1
	Region	2 – 167	166	Necessary for mediating alternative 5' splicing
	Region	2 – 98	97	Necessary for interactions with KRT8, KRT18 and KRT19
	Region	606 – 717	112	Necessary for interaction with PPIG
	Coiled coil	2 – 32	31	Potential
	Coiled coil	163 – 234	72	Potential
	Coiled coil	287 – 379	93	Potential
	Coiled coil	446 – 467	22	Potential
	Compositional bias	172 – 471	300	Glu-rich
	Compositional bias	469 – 520	52	Gln-rich
	Compositional bias	552 – 704	153	Ser-rich
	Compositional bias	632 – 717	86	Arg-rich
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.9
	Modified residue	58	1	Phosphoserine Ref.30
	Modified residue	66	1	Phosphoserine Ref.23 Ref.25 Ref.28 Ref.30
	Modified residue	96	1	Phosphoserine Ref.28
	Modified residue	100	1	Phosphoserine Ref.22 Ref.25 Ref.28 Ref.30
	Modified residue	114	1	Phosphoserine Ref.28
	Modified residue	115	1	Phosphoserine Ref.28
	Modified residue	124	1	Phosphothreonine Ref.28
	Modified residue	238	1	N6-acetyllysine Ref.27
	Modified residue	347	1	Phosphoserine Ref.22 Ref.28 Ref.30
	Modified residue	375	1	Phosphoserine Ref.25
	Modified residue	381	1	Phosphoserine Ref.22 Ref.26 Ref.28 Ref.30
	Modified residue	441	1	Phosphoserine By similarity
	Modified residue	443	1	Phosphoserine Ref.25 Ref.26 Ref.28
	Modified residue	450	1	Phosphoserine Ref.25 Ref.28 Ref.30
	Modified residue	552	1	Phosphoserine Ref.25 Ref.28
	Modified residue	658	1	Phosphoserine Ref.30
	Modified residue	671	1	Phosphoserine By similarity
	Modified residue	692	1	Phosphoserine Ref.30
	Modified residue	695	1	Phosphoserine Ref.30
Natural variations
	Alternative sequence	1 – 133	133	Missing in isoform 2.		VSP_015307
	Natural variant	441	1	S → T. Corresponds to variant rs2180792 [ dbSNP | Ensembl ].		VAR_050540
	Natural variant	671	1	S → G. Ref.2 Ref.6 Corresponds to variant rs13021 [ dbSNP | Ensembl ].		VAR_023368
Experimental info
	Mutagenesis	8	1	L → P: Abolishes interaction with KRT18. Ref.11 Ref.19
	Mutagenesis	19	1	L → P: Abolishes interaction with KRT18. Ref.11 Ref.19
	Mutagenesis	502 – 503	2	PE → AA: Abolishes interaction with CTBP1 and shows moderate relief of CTBP1-mediated repression. Ref.19
	Sequence conflict	69	1	Missing in AAB48304. Ref.1
	Sequence conflict	168	1	K → N in AAB48304. Ref.1
	Sequence conflict	268	1	E → D in AAB48304. Ref.1
	Sequence conflict	303	1	Q → H in AAB48304. Ref.1
	Sequence conflict	320	1	E → V in AAB48304. Ref.1
	Sequence conflict	343	1	A → G in AAB48304. Ref.1
	Sequence conflict	402 – 403	2	DQ → EE in AAG33941. Ref.3
	Sequence conflict	459	1	E → D in AAB48304. Ref.1
	Sequence conflict	478	1	P → A in AAB48304. Ref.1
	Sequence conflict	491 – 492	2	QP → EPQPQLQPEPAQPQLQSQPQ LQLQSQCHA AA sequence Ref.1
	Sequence conflict	497	1	Q → H in AAB48304. Ref.1
	Sequence conflict	520	1	Q → H in AAB48304. Ref.1
	Sequence conflict	523	1	L → F in AAB48304. Ref.1
	Sequence conflict	541	1	P → T AA sequence Ref.1
	Sequence conflict	543	1	E → D in AAB48304. Ref.1
	Sequence conflict	547	1	T → I AA sequence Ref.1
	Sequence conflict	550	1	P → S AA sequence Ref.1
	Sequence conflict	551	1	E → D AA sequence Ref.1
	Sequence conflict	553 – 557	5	KSKTK → ESETN in AAB48304. Ref.1
	Sequence conflict	566	1	A → T in AAB48304. Ref.1
	Sequence conflict	569 – 571	3	KTS → RTT in AAB48304. Ref.1
	Sequence conflict	618	1	S → G in AAF17209. Ref.4
	Sequence conflict	618	1	S → G in CAA71377. Ref.8
	Sequence conflict	626	1	S → STS in CAA70874. Ref.2
	Sequence conflict	664	1	H → P in AAG33941. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 1C05E1E12F54299F	FASTA	717	81,614
	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
	Isoform 2 [UniParc]. Checksum: 7D96168629D5C4DA	FASTA	584	67,005
	10 20 30 40 50 60 MDEKGKQRNR RIFGLLMGTL QKFKQESTVA TERQKRRQEI EQKLEVQAEE ERKQVENERR 70 80 90 100 110 120 ELFEERRAKQ TELRLLEQKV ELAQLQEEWN EHNAKIIKYI RTKTKPHLFY IPGRMCPATQ 130 140 150 160 170 180 KLIEESQRKM NALFEGRRIE FAEQINKMEA RPRRQSMKEK EHQVVRNEEQ KAEQEEGKVA 190 200 210 220 230 240 QREEELEETG NQHNDVEIEE AGEEEEKEIA IVHSDAEKEQ EEEEQKQEME VKMEEETEVR 250 260 270 280 290 300 ESEKQQDSQP EEVMDVLEMV ENVKHVIADQ EVMETNRVES VEPSENEASK ELEPEMEFEI 310 320 330 340 350 360 EPDKECKSLS PGKENVSALD MEKESEEKEE KESEPQPEPV AQPQPQSQPQ LQLQSQSQPV 370 380 390 400 410 420 LQSQPPSQPE DLSLAVLQPT PQVTQEQGHL LPERKDFPVE SVKLTEVPVE PVLTVHPESK 430 440 450 460 470 480 SKTKTRSRSR GRARNKTSKS RSRSSSSSSS SSSSTSSSSG SSSSSGSSSS RSSSSSSSST 490 500 510 520 530 540 SGSSSRDSSS STSSSSESRS RSRGRGHNRD RKHRRSVDRK RRDTSGLERS HKSSKGGSSR 550 560 570 580 DTKGSKDKNS RSDRKRSISE SSRSGKRSSR SERDRKSDRK DKRR

References

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[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. , 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. , 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, 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, HETERODIMERIZATION, IDENTIFICATION IN A HETEROTRIMERIC COMPLEX, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[27]	"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, MASS SPECTROMETRY.
[28]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"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].
[30]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00002649. IPI00789041.
RefSeq	NP_002678.2. NM_002687.3.
UniGene	Hs.409965.
3D structure databases
ProteinModelPortal	Q9H307.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32950N.
IntAct	Q9H307. 15 interactions.
MINT	MINT-1683388.
Protein family/group databases
TCDB	3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.
PTM databases
PhosphoSite	Q9H307.
Polymorphism databases
DMDM	73921750.
Proteomic databases
PaxDb	Q9H307.
PRIDE	Q9H307.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000216832; ENSP00000216832; ENSG00000100941.
GeneID	5411.
KEGG	hsa:5411.
UCSC	uc001wuw.4. human.
Organism-specific databases
CTD	5411.
GeneCards	GC14P039644.
H-InvDB	HIX0037750.
HGNC	HGNC:9162. PNN.
HPA	HPA001378.
MIM	603154. gene.
neXtProt	NX_Q9H307.
PharmGKB	PA33484.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG249368.
HOVERGEN	HBG053104.
InParanoid	Q9H307.
KO	K13114.
OrthoDB	EOG4K0QNP.
Gene expression databases
ArrayExpress	Q9H307.
Bgee	Q9H307.
CleanEx	HS_PNN.
Genevestigator	Q9H307.
GermOnline	ENSG00000100941. Homo sapiens.
Family and domain databases
InterPro	IPR006786. Pinin_SDK_MemA. IPR006787. Pinin_SDK_N. [Graphical view]
Pfam	PF04696. Pinin_SDK_memA. 1 hit. PF04697. Pinin_SDK_N. 1 hit. [Graphical view]
ProDom	PD011048. Pinin_SDK_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other
ChiTaRS	PNN. human.
GenomeRNAi	5411.
NextBio	20949.
SOURCE	Search...

Entry information

Entry name

PININ_HUMAN

Accession

Primary (citable) accession number: Q9H307
Secondary accession number(s): B4DZX8 , 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:	May 1, 2013
This is version 99 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.