Reviewed, UniProtKB/Swiss-Prot Q14978 (NOLC1_HUMAN)

Names and origin

Protein names

Recommended name:
    Nucleolar and coiled-body phosphoprotein 1
Alternative name(s):
    Nucleolar phosphoprotein p130
    Nucleolar 130 kDa protein
    140 kDa nucleolar phosphoprotein
      Short name=Nopp140
    HCV NS5A trans-regulated protein 13
      Short name=NS5ATP13

Gene names

Name:	NOLC1
Synonyms:	KIAA0035

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	699 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Related to nucleologenesis, may play a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities. May play an important role in transcription catalyzed by RNA polymerase I.
Subunit structure	Interacts with RNA polymerase I 194 kDa subunit (RPA194) and with casein kinase-II.
Subcellular location	Nucleus › nucleolus. Cytoplasm. Note: Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase.
Post-translational modification	Undergoes rapid and massive phosphorylation/dephosphorylation cycles on CK2 and PKC sites. There is evidence suggesting that CDC2 kinase phosphorylates p130 at the M-phase.
Sequence similarities	Contains 1 LisH domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mitosis Ref.1 Traceable author statement. Source: ProtInc rRNA processing Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Ref.1 Traceable author statement. Source: ProtInc nucleolus Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	2	EBI-396155,EBI-743313
ARRB2	P32121	2	EBI-396155,EBI-714559
YWHAZ	P63104	1	EBI-396155,EBI-347088

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha (identifier: Q14978-1)

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 Beta (identifier: Q14978-2)

The sequence of this isoform differs from the canonical sequence as follows:
     241-241: K → KVWTITSVRAE

Isoform 3 (identifier: Q14978-3)

The sequence of this isoform differs from the canonical sequence as follows:
     58-59: LK → LNR

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 699	699	Nucleolar and coiled-body phosphoprotein 1		PRO_0000096942
Regions
	Domain	10 – 42	33	LisH
	Repeat	84 – 95	12	Acidic serine cluster 1
	Repeat	125 – 136	12	Acidic serine cluster 2
	Repeat	167 – 178	12	Acidic serine cluster 3
	Repeat	221 – 232	12	Acidic serine cluster 4
	Repeat	264 – 275	12	Acidic serine cluster 5
	Repeat	325 – 336	12	Acidic serine cluster 6
	Repeat	363 – 375	13	Acidic serine cluster 7
	Repeat	425 – 436	12	Acidic serine cluster 8
	Repeat	470 – 481	12	Acidic serine cluster 9
	Repeat	519 – 529	11	Acidic serine cluster 10
	Repeat	555 – 566	12	Acidic serine cluster 11
	Region	84 – 566	483	11 X 12 AA approximate repeats of an acidic serine cluster
	Region	204 – 382	179	Interacts with RPA194
	Motif	68 – 82	15	Nuclear localization signal Potential
	Motif	384 – 587	204	Nuclear localization signal Potential
	Motif	601 – 617	17	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	33	1	N6-acetyllysine Ref.24
	Modified residue	83	1	Phosphoserine Ref.12 Ref.19
	Modified residue	84	1	Phosphoserine Ref.12
	Modified residue	85	1	Phosphoserine Ref.12 Ref.19
	Modified residue	87	1	Phosphoserine Ref.12 Ref.19
	Modified residue	90	1	Phosphoserine Ref.12 Ref.19
	Modified residue	91	1	Phosphoserine Ref.12 Ref.19
	Modified residue	188	1	Phosphothreonine Ref.22
	Modified residue	366	1	Phosphoserine Ref.19
	Modified residue	397	1	Phosphoserine Ref.19 Ref.14 Ref.17
	Modified residue	415	1	N6-acetyllysine Ref.24
	Modified residue	508	1	Phosphoserine Ref.19 Ref.14 Ref.17
	Modified residue	538	1	Phosphoserine Ref.12 Ref.14 Ref.17 Ref.16
	Modified residue	563	1	Phosphoserine Ref.12 Ref.20
	Modified residue	580	1	Phosphoserine Ref.19
	Modified residue	582	1	Phosphoserine Ref.19
	Modified residue	607	1	Phosphothreonine Ref.12 Ref.19 Ref.22 Ref.14 Ref.10 Ref.13 Ref.23
	Modified residue	610	1	Phosphothreonine Ref.12 Ref.19 Ref.22 Ref.14 Ref.10 Ref.13 Ref.23
	Modified residue	622	1	Phosphoserine Ref.19
	Modified residue	623	1	Phosphoserine Ref.19 Ref.22
	Modified residue	643	1	Phosphoserine Ref.19 Ref.14 Ref.17 Ref.13 Ref.23
	Modified residue	663	1	N6-acetyllysine Ref.24
	Modified residue	686	1	Phosphoserine Ref.19
	Modified residue	698	1	Phosphoserine Ref.12 Ref.19 Ref.22 Ref.13 Ref.23 Ref.11 Ref.15 Ref.18
Natural variations
	Alternative sequence	58 – 59	2	LK → LNR in isoform 3.		VSP_035415
	Alternative sequence	241	1	K → KVWTITSVRAE in isoform Beta.		VSP_004338
	Natural variant	412	1	G → V: dbSNP rs11191224.		VAR_031677
	Natural variant	456	1	S → P: dbSNP rs1049455. Ref.6		VAR_031678
Experimental info
	Sequence conflict	3	1	D → A in BAA04803. Ref.6
	Sequence conflict	133	1	S → R in CAA84063. Ref.1
	Sequence conflict	291 – 292	2	SV → YA in CAA84063. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified April 17, 2007. Version 2. Checksum: 7C5C4F25677E2E61	FASTA	699	73,603
	10 20 30 40 50 60 MADAGIRRVV PSDLYPLVLG FLRDNQLSEV ANKFAKATGA TQQDANASSL LDIYSFWLKS 70 80 90 100 110 120 AKVPERKLQA NGPVAKKAKK KASSSDSEDS SEEEEEVQGP PAKKAAVPAK RVGLPPGKAA 130 140 150 160 170 180 AKASESSSSE ESSDDDDEED QKKQPVQKGV KPQAKAAKAP PKKAKSSDSD SDSSSEDEPP 190 200 210 220 230 240 KNQKPKITPV TVKAQTKAPP KPARAAPKIA NGKAASSSSS SSSSSSSDDS EEEKAAATPK 250 260 270 280 290 300 KTVPKKQVVA KAPVKAATTP TRKSSSSEDS SSDEEEEQKK PMKNKPGPYS SVPPPSAPPP 310 320 330 340 350 360 KKSLGTQPPK KAVEKQQPVE SSEDSSDESD SSSEEEKKPP TKAVVSKATT KPPPAKKAAE 370 380 390 400 410 420 SSSDSSDSDS SEDDEAPSKP AGTTKNSSNK PAVTTKSPAV KPAAAPKQPV GGGQKLLTRK 430 440 450 460 470 480 ADSSSSEEES SSSEEEKTKK MVATTKPKAT AKAALSLPAK QAPQGSRDSS SDSDSSSSEE 490 500 510 520 530 540 EEEKTSKSAV KKKPQKVAGG AAPSKPASAK KGKAESSNSS SSDDSSEEEE EKLKGKGSPR 550 560 570 580 590 600 PQAPKANGTS ALTAQNGKAA KNSEEEEEEK KKAAVVVSKS GSLKKRKQNE AAKEAETPQA 610 620 630 640 650 660 KKIKLQTPNT FPKRKKGEKR ASSPFRRVRE EEIEVDSRVA DNSFDAKRGA AGDWGERANQ 670 680 690 VLKFTKGKSF RHEKTKKKRG SYRGGSISVQ VNSIKFDSE
	Isoform Beta. Checksum: 5A02742A231255AB	FASTA	709	74,747
	10 20 30 40 50 60 MADAGIRRVV PSDLYPLVLG FLRDNQLSEV ANKFAKATGA TQQDANASSL LDIYSFWLKS 70 80 90 100 110 120 AKVPERKLQA NGPVAKKAKK KASSSDSEDS SEEEEEVQGP PAKKAAVPAK RVGLPPGKAA 130 140 150 160 170 180 AKASESSSSE ESSDDDDEED QKKQPVQKGV KPQAKAAKAP PKKAKSSDSD SDSSSEDEPP 190 200 210 220 230 240 KNQKPKITPV TVKAQTKAPP KPARAAPKIA NGKAASSSSS SSSSSSSDDS EEEKAAATPK 250 260 270 280 290 300 KVWTITSVRA ETVPKKQVVA KAPVKAATTP TRKSSSSEDS SSDEEEEQKK PMKNKPGPYS 310 320 330 340 350 360 SVPPPSAPPP KKSLGTQPPK KAVEKQQPVE SSEDSSDESD SSSEEEKKPP TKAVVSKATT 370 380 390 400 410 420 KPPPAKKAAE SSSDSSDSDS SEDDEAPSKP AGTTKNSSNK PAVTTKSPAV KPAAAPKQPV 430 440 450 460 470 480 GGGQKLLTRK ADSSSSEEES SSSEEEKTKK MVATTKPKAT AKAALSLPAK QAPQGSRDSS 490 500 510 520 530 540 SDSDSSSSEE EEEKTSKSAV KKKPQKVAGG AAPSKPASAK KGKAESSNSS SSDDSSEEEE 550 560 570 580 590 600 EKLKGKGSPR PQAPKANGTS ALTAQNGKAA KNSEEEEEEK KKAAVVVSKS GSLKKRKQNE 610 620 630 640 650 660 AAKEAETPQA KKIKLQTPNT FPKRKKGEKR ASSPFRRVRE EEIEVDSRVA DNSFDAKRGA 670 680 690 700 AGDWGERANQ VLKFTKGKSF RHEKTKKKRG SYRGGSISVQ VNSIKFDSE
	Isoform 3. Checksum: 5F8699563FBA24A9	FASTA	700	73,745
	10 20 30 40 50 60 MADAGIRRVV PSDLYPLVLG FLRDNQLSEV ANKFAKATGA TQQDANASSL LDIYSFWLNR 70 80 90 100 110 120 SAKVPERKLQ ANGPVAKKAK KKASSSDSED SSEEEEEVQG PPAKKAAVPA KRVGLPPGKA 130 140 150 160 170 180 AAKASESSSS EESSDDDDEE DQKKQPVQKG VKPQAKAAKA PPKKAKSSDS DSDSSSEDEP 190 200 210 220 230 240 PKNQKPKITP VTVKAQTKAP PKPARAAPKI ANGKAASSSS SSSSSSSSDD SEEEKAAATP 250 260 270 280 290 300 KKTVPKKQVV AKAPVKAATT PTRKSSSSED SSSDEEEEQK KPMKNKPGPY SSVPPPSAPP 310 320 330 340 350 360 PKKSLGTQPP KKAVEKQQPV ESSEDSSDES DSSSEEEKKP PTKAVVSKAT TKPPPAKKAA 370 380 390 400 410 420 ESSSDSSDSD SSEDDEAPSK PAGTTKNSSN KPAVTTKSPA VKPAAAPKQP VGGGQKLLTR 430 440 450 460 470 480 KADSSSSEEE SSSSEEEKTK KMVATTKPKA TAKAALSLPA KQAPQGSRDS SSDSDSSSSE 490 500 510 520 530 540 EEEEKTSKSA VKKKPQKVAG GAAPSKPASA KKGKAESSNS SSSDDSSEEE EEKLKGKGSP 550 560 570 580 590 600 RPQAPKANGT SALTAQNGKA AKNSEEEEEE KKKAAVVVSK SGSLKKRKQN EAAKEAETPQ 610 620 630 640 650 660 AKKIKLQTPN TFPKRKKGEK RASSPFRRVR EEEIEVDSRV ADNSFDAKRG AAGDWGERAN 670 680 690 700 QVLKFTKGKS FRHEKTKKKR GSYRGGSISV QVNSIKFDSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cell-cycle-dependent alterations of a highly phosphorylated nucleolar protein p130 are associated with nucleologenesis." Pai C.-Y., Chen H.-K., Sheu H.-L., Yeh N.-H. J. Cell Sci. 108:1911-1920(1995) [PubMed: 7657714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). Tissue: Leukemia.
[2]	Ying Z.L., Hong D., Jun C. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Lung.
[6]	"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1." Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S. DNA Res. 1:27-35(1994) [PubMed: 7584026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-699 (ISOFORM BETA), VARIANT PRO-456. Tissue: Bone marrow.
[7]	"Cell proliferation-dependent expression of two isoforms of the nucleolar phosphoprotein p130." Pai C.-Y., Yeh N.-H. Biochem. Biophys. Res. Commun. 221:581-587(1996) [PubMed: 8630004] [Abstract] Cited for: ALTERNATIVE SPLICING.
[8]	"The nucleolar phosphoprotein P130 is a GTPase/ATPase with intrinsic property to form large complexes triggered by F- and Mg2+." Chen H.-K., Yeh N.-H. Biochem. Biophys. Res. Commun. 230:370-375(1997) [PubMed: 9016786] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Human Nopp140, which interacts with RNA polymerase I: implications for rRNA gene transcription and nucleolar structural organization." Chen H.-K., Pai C.-Y., Huang J.-Y., Yeh N.-H. Mol. Cell. Biol. 19:8536-8546(1999) [PubMed: 10567578] [Abstract] Cited for: CHARACTERIZATION.
[10]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607 AND THR-610, MASS SPECTROMETRY. Tissue: T-cell.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-84; SER-85; SER-87; SER-90; SER-91; SER-538; SER-563; THR-607; THR-610 AND SER-698, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607; THR-610; SER-643 AND SER-698, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-508; SER-538; THR-607; THR-610 AND SER-643, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698, MASS SPECTROMETRY.
[16]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, MASS SPECTROMETRY.
[17]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-508; SER-538 AND SER-643, MASS SPECTROMETRY.
[18]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698, MASS SPECTROMETRY.
[19]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85; SER-87; SER-90; SER-91; SER-366; SER-397; SER-508; SER-580; SER-582; THR-607; THR-610; SER-622; SER-623; SER-643; SER-686 AND SER-698, MASS SPECTROMETRY.
[20]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, MASS SPECTROMETRY. Tissue: Liver.
[21]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[22]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188; THR-607; THR-610; SER-623 AND SER-698, MASS SPECTROMETRY.
[23]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607; THR-610; SER-643 AND SER-698, MASS SPECTROMETRY. Tissue: T-cell.
[24]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-415 AND LYS-663, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z34289 mRNA. Translation: CAA84063.1. AY820769 mRNA. Translation: AAV67777.1. AL500527 Genomic DNA. Translation: CAH72220.1. CH471066 Genomic DNA. Translation: EAW49714.1. CH471066 Genomic DNA. Translation: EAW49715.1. BC001883 mRNA. Translation: AAH01883.1. D21262 mRNA. Translation: BAA04803.1.
IPI	IPI00216654. IPI00292387. IPI00908873.
PIR	I38073.
RefSeq	NP_004732.2.
UniGene	Hs.523238
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14978. 6 interactions.
STRING	Q14978.
PTM databases
PhosphoSite	Q14978.
Proteomic databases
PRIDE	Q14978.
Genome annotation databases
Ensembl	ENST00000370007; ENSP00000359024; ENSG00000166197; Homo sapiens. [Genome view]
GeneID	9221.
KEGG	hsa:9221.
UCSC	uc001kuo.2. human.
Organism-specific databases
CTD	9221.
GeneCards	GC10P103902.
H-InvDB	HIX0009150.
HGNC	HGNC:15608. NOLC1.
MIM	602394. gene.
PharmGKB	PA31679.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14398.
HOVERGEN	Q14978.
OMA	PIKKKPG.
OrthoDB	EOG90044V.
PhylomeDB	Q14978.
Gene expression databases
ArrayExpress	Q14978.
Bgee	Q14978.
CleanEx	HS_NOLC1.
Genevestigator	Q14978.
GermOnline	ENSG00000166197. Homo sapiens.
Family and domain databases
InterPro	IPR006594. LisH_dimerisation. IPR007718. SRP40_C. [Graphical view]
Pfam	PF05022. SRP40_C. 1 hit. [Graphical view]
SMART	SM00667. LisH. 1 hit. [Graphical view]
PROSITE	PS50896. LISH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	34571.
SOURCE	Search...

Entry information

Entry name

NOLC1_HUMAN

Accession

Primary (citable) accession number: Q14978
Secondary accession number(s): Q15030, Q5VV70, Q9BUV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	April 17, 2007
Last modified:	February 9, 2010
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.