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Protein

Nascent polypeptide-associated complex subunit alpha, muscle-specific form

Gene

NACA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cardiac- and muscle-specific transcription factor. May act to regulate the expression of genes involved in the development of myotubes. Plays a critical role in ventricular cardiomyocyte expansion and regulates postnatal skeletal muscle growth and regeneration. Involved in the organized assembly of thick and thin filaments of myofibril sarcomeres (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nascent polypeptide-associated complex subunit alpha, muscle-specific form
Alternative name(s):
Alpha-NAC, muscle-specific form
Short name:
skNAC
Gene namesi
Name:NACA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7629. NACA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20782078Nascent polypeptide-associated complex subunit alpha, muscle-specific formPRO_0000425571Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei917 – 9171PhosphoserineBy similarity
Modified residuei1181 – 11811PhosphoserineBy similarity
Modified residuei1397 – 13971PhosphoserineBy similarity
Modified residuei1474 – 14741PhosphoserineBy similarity
Modified residuei1906 – 19061Phosphoserine; by ILK1By similarity
Modified residuei2005 – 20051N6-acetyllysineCombined sources
Modified residuei2022 – 20221Phosphothreonine; by GSK3-betaBy similarity
Modified residuei2024 – 20241PhosphothreonineCombined sources
Modified residuei2029 – 20291PhosphoserineCombined sources
Modified residuei2049 – 20491PhosphoserineCombined sources
Modified residuei2054 – 20541PhosphoserineCombined sources
Modified residuei2066 – 20661PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiE9PAV3.
PaxDbiE9PAV3.
PRIDEiE9PAV3.

PTM databases

iPTMnetiE9PAV3.

Expressioni

Gene expression databases

BgeeiE9PAV3.
ExpressionAtlasiE9PAV3. baseline and differential.
GenevisibleiE9PAV3. HS.

Interactioni

Subunit structurei

Interacts (via PXLXP motif) with the muscle-restricted histone methyltransferase SMYD1 (via MYND-type zinc finger).By similarity

Protein-protein interaction databases

BioGridi110748. 48 interactions.
IntActiE9PAV3. 2 interactions.
STRINGi9606.ENSP00000448035.

Structurei

3D structure databases

ProteinModelPortaliE9PAV3.
SMRiE9PAV3. Positions 1942-1995.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1933 – 199866NAC-A/BPROSITE-ProRule annotationAdd
BLAST
Domaini2039 – 207840UBAAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1932 – 194312Required for DNA-bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1841 – 18455PXLXPBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 18801840Pro-richAdd
BLAST

Domaini

The proline-rich muscle-specific exon 3 contains eighteen approximate 23-AA repeats.

Sequence similaritiesi

Contains 1 NAC-A/B (NAC-alpha/beta) domain.PROSITE-ProRule annotation
Contains 1 UBA domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2239. Eukaryota.
COG1308. LUCA.
GeneTreeiENSGT00440000033468.
OMAiECPATQS.
PhylomeDBiE9PAV3.

Family and domain databases

InterProiIPR016641. EGD2/NACA.
IPR002715. Nas_poly-pep-assoc_cplx_dom.
[Graphical view]
PANTHERiPTHR21713. PTHR21713. 9 hits.
PfamiPF01849. NAC. 1 hit.
[Graphical view]
SMARTiSM01407. NAC. 1 hit.
[Graphical view]
PROSITEiPS51151. NAC_AB. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform skNAC (identifier: E9PAV3-1) [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

        10         20         30         40         50
MPGEATETVP ATEQELPQPQ AETAVLPMSS ALSVTAALGQ PGPTLPPPCS
60 70 80 90 100
PAPQQCPLSA ANQASPFPSP STIASTPLEV PFPQSSSGTA LPLGTAPEAP
110 120 130 140 150
TFLPNLIGPP ISPAALALAS PMIAPTLKGT PSSSAPLALV ALAPHSVQKS
160 170 180 190 200
SAFPPNLLTS PPSVAVAESG SVITLSAPIA PSEPKTNLNK VPSEVVPNPK
210 220 230 240 250
GTPSPPCIVS TVPYHCVTPM ASIQSGVASL PQTTPTTTLA IASPQVKDTT
260 270 280 290 300
ISSVLISPQN PGSLSLKGPV SPPAALSLST QSLPVVTSSQ KTAGPNTPPD
310 320 330 340 350
FPISLGSHLA PLHQSSFGSV QLLGQTGPSA LSDPTVKTIS VDHSSTGASY
360 370 380 390 400
PSQRSVIPPL PSRNEVVPAT VAAFPVVAPS VDKGPSTISS ITCSPSGSLN
410 420 430 440 450
VATSFSLSPT TSLILKSSPN ATYHYPLVAQ MPVSSVGTTP LVVTNPCTIA
460 470 480 490 500
AAPTTTFEVA TCVSPPMSSG PISNIEPTSP AALVMAPVAP KEPSTQVATT
510 520 530 540 550
LRIPVSPPLP DPEDLKNLPS SVLVKFPTQK DLQTVPASLE GAPFSPAQAG
560 570 580 590 600
LTTKKDPTVL PLVQAAPKNS PSFQSTSSSP EIPLSPEATL AKKSLGEPLP
610 620 630 640 650
IGKPASSMTS PLGVNSSASV IKTDSYAGPD SAGPLLKSSL ITPTVAAFPL
660 670 680 690 700
ESADPAGVAP TTAKGTSTYT TTASPFLEGT VSLAPKNHPV KEGTLTTLPL
710 720 730 740 750
VPTASENCPV APSPQNTCAP LATLVLAPEI PKSVPSPSLP PAGTPPGTKK
760 770 780 790 800
VDGISHTSAL APVASSPKEC PTEDSGASAT ASSKGTLTYL ADSPSPLGVS
810 820 830 840 850
VSPQTKRPPT KKGSAGPDTP IGNLSSPVSP VEASFLPENS LSFQGSKDSP
860 870 880 890 900
ATTHSPTPPS PKGAPTPSAV TPLSPKGVTL PPKETPTPSV VNLPFPKEGP
910 920 930 940 950
ATPAPKQAPA LSMTSSSPKK ARATPAPKGI PASPSPKGAP TPPAATPPSP
960 970 980 990 1000
KGGPATPSPK WAPTPPAATP PSPKGGPATP SPKGAPTPPA ATPPSPKGGP
1010 1020 1030 1040 1050
ATPSPKGAPT PPAVTPPSPK GSPAATPFPK GASTPPAATP PSPKGSPAAT
1060 1070 1080 1090 1100
PLPKGAPTTP AATLPSPKGG PATPSLKGAP TPPAATPPSP KGGPATPSPK
1110 1120 1130 1140 1150
GAPMPPAATP PSPKGGLATP PHKGAPTTPA ATPPSPKGGL ATPPPKGAPT
1160 1170 1180 1190 1200
TPAATPPSPK GGLATPPPKG APTTPAATPP SPKGGLATPS PKGAPTTPAA
1210 1220 1230 1240 1250
TPPSPKGGLA TPSPKGAPTT PAATPPSPKG GLATPSPKGA PTTPAATPPS
1260 1270 1280 1290 1300
PKGGPATPPP KGAPTPPAAT PPSLKGGLAT PPHKGAPNPA VVTPPSPKGG
1310 1320 1330 1340 1350
PATSPPKGAP TPPAATPPSP KGSPGTPPPK GAPTPPAVTP PSPKGTPTLP
1360 1370 1380 1390 1400
ATTPSSKGGP TTPSSKEGPT PPAATPSHKG GPAMTPPSPK RGPAIPSPKG
1410 1420 1430 1440 1450
DPTSPAVIPL SPKKAPATPV TREGAATPSK GDLTPPAVTP VSLKKAPATS
1460 1470 1480 1490 1500
APKGGPATPS SKGDPTLPAV TPPSPKEPPA PKQVATSSSP KKAPATPAPM
1510 1520 1530 1540 1550
GAPTLPAVIP SSPKEVPATP SSRRDPIAPT ATLLSKKTPA TLAPKEALIP
1560 1570 1580 1590 1600
PAMTVPSPKK TPAIPTPKEA PATPSSKEAS SPPAVTPSTY KGAPSPKELL
1610 1620 1630 1640 1650
IPPAVTSPSP KEAPTPPAVT PPSPEKGPAT PAPKGTPTSP PVTPSSLKDS
1660 1670 1680 1690 1700
PTSPASVTCK MGATVPQASK GLPAKKGPTA LKEVLVAPAP ESTPIITAPT
1710 1720 1730 1740 1750
RKGPQTKKSS ATSPPICPDP SAKNGSKGPL STVAPAPLLP VQKDSSKTAK
1760 1770 1780 1790 1800
GKDASHSPKG PLAPPESKAS TPLTAAAFEK VLPKPESASV SAAPSPPVSL
1810 1820 1830 1840 1850
PLAPSPVPTL PPKQQFLPSS PGLVLESPSK PLAPADEDEL LPLIPPEPIS
1860 1870 1880 1890 1900
GGVPFQSVLV NMPTPKSAGI PVPTPSAKQP VTKNNKGSGT ESDSDESVPE
1910 1920 1930 1940 1950
LEEQDSTQAT TQQAQLAAAA EIDEEPVSKA KQSRSEKKAR KAMSKLGLRQ
1960 1970 1980 1990 2000
VTGVTRVTIR KSKNILFVIT KPDVYKSPAS DTYIVFGEAK IEDLSQQAQL
2010 2020 2030 2040 2050
AAAEKFKVQG EAVSNIQENT QTPTVQEESE EEEVDETGVE VKDIELVMSQ
2060 2070
ANVSRAKAVR ALKNNSNDIV NAIMELTM
Length:2,078
Mass (Da):205,422
Last modified:April 5, 2011 - v1
Checksum:i9A07C05D3F24C34B
GO
Isoform 1 (identifier: Q13765-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry Q13765.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:215
Mass (Da):23,384
GO
Isoform 2 (identifier: E9PAV3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     602-644: Missing.
     665-1774: Missing.

Note: No experimental confirmation available.
Show »
Length:925
Mass (Da):94,681
Checksum:i8C2A30032C1C6287
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti417 – 4171S → N in AK096699 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti336 – 3361V → E.1 Publication
Corresponds to variant rs2958127 [ dbSNP | Ensembl ].
VAR_070547
Natural varianti405 – 4051F → S.1 Publication
Corresponds to variant rs2926743 [ dbSNP | Ensembl ].
VAR_070548
Natural varianti519 – 5191P → S.1 Publication
Corresponds to variant rs185561121 [ dbSNP | Ensembl ].
VAR_070549
Natural varianti1795 – 17951S → T.1 Publication
Corresponds to variant rs2926747 [ dbSNP | Ensembl ].
VAR_070550
Natural varianti1841 – 18411L → P.1 Publication
Corresponds to variant rs2958149 [ dbSNP | Ensembl ].
VAR_070551

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei602 – 64443Missing in isoform 2. 1 PublicationVSP_053722Add
BLAST
Alternative sequencei665 – 17741110Missing in isoform 2. 1 PublicationVSP_053723Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096699 mRNA. No translation available.
AC117378 Genomic DNA. No translation available.
CCDSiCCDS44925.2. [E9PAV3-2]
RefSeqiXP_011536691.1. XM_011538389.1. [E9PAV3-1]
UniGeneiHs.505735.

Genome annotation databases

EnsembliENST00000454682; ENSP00000403817; ENSG00000196531. [E9PAV3-1]
ENST00000550952; ENSP00000448035; ENSG00000196531. [E9PAV3-2]
GeneIDi4666.
UCSCiuc001sma.3. human. [E9PAV3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096699 mRNA. No translation available.
AC117378 Genomic DNA. No translation available.
CCDSiCCDS44925.2. [E9PAV3-2]
RefSeqiXP_011536691.1. XM_011538389.1. [E9PAV3-1]
UniGeneiHs.505735.

3D structure databases

ProteinModelPortaliE9PAV3.
SMRiE9PAV3. Positions 1942-1995.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110748. 48 interactions.
IntActiE9PAV3. 2 interactions.
STRINGi9606.ENSP00000448035.

PTM databases

iPTMnetiE9PAV3.

Proteomic databases

EPDiE9PAV3.
PaxDbiE9PAV3.
PRIDEiE9PAV3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000454682; ENSP00000403817; ENSG00000196531. [E9PAV3-1]
ENST00000550952; ENSP00000448035; ENSG00000196531. [E9PAV3-2]
GeneIDi4666.
UCSCiuc001sma.3. human. [E9PAV3-1]

Organism-specific databases

CTDi4666.
GeneCardsiNACA.
HGNCiHGNC:7629. NACA.
neXtProtiNX_E9PAV3.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2239. Eukaryota.
COG1308. LUCA.
GeneTreeiENSGT00440000033468.
OMAiECPATQS.
PhylomeDBiE9PAV3.

Miscellaneous databases

ChiTaRSiNACA. human.
GenomeRNAii4666.
NextBioi35501364.

Gene expression databases

BgeeiE9PAV3.
ExpressionAtlasiE9PAV3. baseline and differential.
GenevisibleiE9PAV3. HS.

Family and domain databases

InterProiIPR016641. EGD2/NACA.
IPR002715. Nas_poly-pep-assoc_cplx_dom.
[Graphical view]
PANTHERiPTHR21713. PTHR21713. 9 hits.
PfamiPF01849. NAC. 1 hit.
[Graphical view]
SMARTiSM01407. NAC. 1 hit.
[Graphical view]
PROSITEiPS51151. NAC_AB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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), VARIANTS GLU-336; SER-405; SER-519; THR-1795 AND PRO-1841.
    Tissue: Pericardium.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "skNAC (skeletal Naca), a muscle-specific isoform of Naca (nascent polypeptide-associated complex alpha), is required for myofibril organization."
    Li H., Randall W.R., Du S.J.
    FASEB J. 23:1988-2000(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, REPEATS, ALTERNATIVE SPLICING.
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2049, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2024; SER-2029 AND SER-2054, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-2029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-2005, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-2049; SER-2054 AND SER-2066, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-2029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNACAM_HUMAN
AccessioniPrimary (citable) accession number: E9PAV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: April 5, 2011
Last modified: May 11, 2016
This is version 42 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.