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Protein

Zinc finger CCCH domain-containing protein 18

Gene

ZC3H18

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri219 – 24527C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger CCCH domain-containing protein 18
Alternative name(s):
Nuclear protein NHN1
Gene namesi
Name:ZC3H18
Synonyms:NHN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:25091. ZC3H18.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162409533.

Polymorphism and mutation databases

BioMutaiZC3H18.
DMDMi269849528.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 953953Zinc finger CCCH domain-containing protein 18PRO_0000311242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei6 – 61PhosphoserineCombined sources
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei46 – 461PhosphoserineCombined sources
Modified residuei53 – 531PhosphoserineCombined sources
Modified residuei59 – 591PhosphoserineBy similarity
Modified residuei67 – 671PhosphoserineCombined sources
Modified residuei74 – 741PhosphoserineCombined sources
Modified residuei78 – 781PhosphoserineCombined sources
Modified residuei83 – 831PhosphoserineCombined sources
Modified residuei95 – 951PhosphoserineBy similarity
Modified residuei109 – 1091PhosphothreonineCombined sources
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei162 – 1621PhosphothreonineCombined sources
Modified residuei173 – 1731PhosphoserineCombined sources
Modified residuei532 – 5321PhosphoserineCombined sources
Modified residuei534 – 5341PhosphoserineCombined sources
Modified residuei536 – 5361PhosphoserineCombined sources
Cross-linki622 – 622Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki766 – 766Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei814 – 8141N6-acetyllysineBy similarity
Cross-linki817 – 817Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei842 – 8421PhosphoserineCombined sources
Modified residuei852 – 8521PhosphoserineBy similarity
Modified residuei868 – 8681PhosphoserineCombined sources
Modified residuei893 – 8931PhosphoserineCombined sources
Modified residuei896 – 8961PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ86VM9.
MaxQBiQ86VM9.
PaxDbiQ86VM9.
PRIDEiQ86VM9.

PTM databases

iPTMnetiQ86VM9.
PhosphoSiteiQ86VM9.

Expressioni

Gene expression databases

BgeeiQ86VM9.
CleanExiHS_ZC3H18.
ExpressionAtlasiQ86VM9. baseline and differential.
GenevisibleiQ86VM9. HS.

Organism-specific databases

HPAiHPA040847.
HPA041327.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF2Q155542EBI-1045965,EBI-706637

Protein-protein interaction databases

BioGridi125858. 134 interactions.
IntActiQ86VM9. 9 interactions.
MINTiMINT-4654755.
STRINGi9606.ENSP00000301011.

Structurei

3D structure databases

ProteinModelPortaliQ86VM9.
SMRiQ86VM9. Positions 220-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili105 – 13430Sequence analysisAdd
BLAST
Coiled coili399 – 46466Sequence analysisAdd
BLAST
Coiled coili921 – 95030Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi201 – 2044Poly-Asp
Compositional biasi259 – 29638Pro-richAdd
BLAST
Compositional biasi532 – 746215Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri219 – 24527C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IJ7N. Eukaryota.
ENOG4111IXQ. LUCA.
GeneTreeiENSGT00730000111190.
HOGENOMiHOG000155765.
HOVERGENiHBG103346.
InParanoidiQ86VM9.
KOiK13092.
OrthoDBiEOG7T7GV1.
PhylomeDBiQ86VM9.
TreeFamiTF327301.

Family and domain databases

InterProiIPR000571. Znf_CCCH.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 1 hit.
PROSITEiPS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86VM9-1) [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
MDVAESPERD PHSPEDEEQP QGLSDDDILR DSGSDQDLDG AGVRASDLED
60 70 80 90 100
EESAARGPSQ EEEDNHSDEE DRASEPKSQD QDSEVNELSR GPTSSPCEEE
110 120 130 140 150
GDEGEEDRTS DLRDEASSVT RELDEHELDY DEEVPEEPAP AVQEDEAEKA
160 170 180 190 200
GAEDDEEKGE GTPREEGKAG VQSVGEKESL EAAKEKKKED DDGEIDDGEI
210 220 230 240 250
DDDDLEEGEV KDPSDRKVRP RPTCRFFMKG NCTWGMNCRF IHPGVNDKGN
260 270 280 290 300
YSLITKADPF PPNGAPPLGP HPLMPANPWG GPVVDEILPP PPPEPPTESA
310 320 330 340 350
WERGLRHAKE VLKKATIRKE QEPDFEEKRF TVTIGEDERE FDKENEVFRD
360 370 380 390 400
WNSRIPRDVR DTVLEPYADP YYDYEIERFW RGGQYENFRV QYTETEPYHN
410 420 430 440 450
YRERERERER ENRQRERERE RERDRERERR QRERERERER ERDKERQRRK
460 470 480 490 500
EEWERERAKR DEKDRQHRDR DREKEREKEK GKPKPRSPQP PSRQAEPPKK
510 520 530 540 550
EAATTGPQVK RADEWKDPWR RSKSPKKKLG VSVSPSRARR RRKTSASSAS
560 570 580 590 600
ASNSSRSSSR SSSYSGSGSS RSRSRSSSYS SYSSRSSRHS SFSGSRSRSR
610 620 630 640 650
SFSSSPSPSP TPSPHRPSIR TKGEPAPPPG KAGEKSVKKP APPPAPPQAT
660 670 680 690 700
KTTAPVPEPT KPGDPREARR KERPARTPPR RRTLSGSGSG SGSSYSGSSS
710 720 730 740 750
RSRSLSVSSV SSVSSATSSS SSAHSVDSED MYADLASPVS SASSRSPAPA
760 770 780 790 800
QTRKEKGKSK KEDGVKEEKR KRDSSTQPPK SAKPPAGGKS SQQPSTPQQA
810 820 830 840 850
PPGQPQQGTF VAHKEIKLTL LNKAADKGSR KRYEPSDKDR QSPPPAKRPN
860 870 880 890 900
TSPDRGSRDR KSGGRLGSPK PERQRGQNSK APAAPADRKR QLSPQSKSSS
910 920 930 940 950
KVTSVPGKAS DPGAASTKSG KASTLSRREE LLKQLKAVED AIARKRAKIP

GKA
Length:953
Mass (Da):106,378
Last modified:November 24, 2009 - v2
Checksum:iF12E87B342E1F892
GO
Isoform 2 (identifier: Q86VM9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     228-228: M → MKDVVTPLSTLLPPISNSIPFRGQV
     412-469: NRQRERERERERDRERERRQRERERERERERDKERQRRKEEWERERAKRDEKDRQHRD → RE
     683-953: TLSGSGSGSG...RKRAKIPGKA → LIKEAGSAMN...PARCLGGRSC

Show »
Length:757
Mass (Da):84,100
Checksum:i883B3D5A20DCBC4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511Y → H in BAB71237 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti368 – 3681A → T.
Corresponds to variant rs34808360 [ dbSNP | Ensembl ].
VAR_037188
Natural varianti440 – 4401R → H.1 Publication
Corresponds to variant rs17855686 [ dbSNP | Ensembl ].
VAR_037189

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei228 – 2281M → MKDVVTPLSTLLPPISNSIP FRGQV in isoform 2. 1 PublicationVSP_029453
Alternative sequencei412 – 46958NRQRE…RQHRD → RE in isoform 2. 1 PublicationVSP_029454Add
BLAST
Alternative sequencei683 – 953271TLSGS…IPGKA → LIKEAGSAMNHQTRTGRALL QPSGPTHPQTEVLGTGSQVG DWAPRSQSGREARTPKPLQP RLTGSASCHPSPRAPARSRA CPAKPRIPAPPAPNQGRPAR CLGGRSC in isoform 2. 1 PublicationVSP_029455Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056632 mRNA. Translation: BAB71237.1.
AC116552 Genomic DNA. No translation available.
BC001584 mRNA. Translation: AAH01584.1.
BC050463 mRNA. Translation: AAH50463.1.
CCDSiCCDS10967.1. [Q86VM9-1]
RefSeqiNP_001281269.1. NM_001294340.1.
NP_653205.3. NM_144604.3. [Q86VM9-1]
UniGeneiHs.93670.

Genome annotation databases

EnsembliENST00000301011; ENSP00000301011; ENSG00000158545. [Q86VM9-1]
GeneIDi124245.
KEGGihsa:124245.
UCSCiuc002fky.4. human. [Q86VM9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056632 mRNA. Translation: BAB71237.1.
AC116552 Genomic DNA. No translation available.
BC001584 mRNA. Translation: AAH01584.1.
BC050463 mRNA. Translation: AAH50463.1.
CCDSiCCDS10967.1. [Q86VM9-1]
RefSeqiNP_001281269.1. NM_001294340.1.
NP_653205.3. NM_144604.3. [Q86VM9-1]
UniGeneiHs.93670.

3D structure databases

ProteinModelPortaliQ86VM9.
SMRiQ86VM9. Positions 220-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125858. 134 interactions.
IntActiQ86VM9. 9 interactions.
MINTiMINT-4654755.
STRINGi9606.ENSP00000301011.

PTM databases

iPTMnetiQ86VM9.
PhosphoSiteiQ86VM9.

Polymorphism and mutation databases

BioMutaiZC3H18.
DMDMi269849528.

Proteomic databases

EPDiQ86VM9.
MaxQBiQ86VM9.
PaxDbiQ86VM9.
PRIDEiQ86VM9.

Protocols and materials databases

DNASUi124245.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301011; ENSP00000301011; ENSG00000158545. [Q86VM9-1]
GeneIDi124245.
KEGGihsa:124245.
UCSCiuc002fky.4. human. [Q86VM9-1]

Organism-specific databases

CTDi124245.
GeneCardsiZC3H18.
H-InvDBHIX0013334.
HGNCiHGNC:25091. ZC3H18.
HPAiHPA040847.
HPA041327.
neXtProtiNX_Q86VM9.
PharmGKBiPA162409533.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ7N. Eukaryota.
ENOG4111IXQ. LUCA.
GeneTreeiENSGT00730000111190.
HOGENOMiHOG000155765.
HOVERGENiHBG103346.
InParanoidiQ86VM9.
KOiK13092.
OrthoDBiEOG7T7GV1.
PhylomeDBiQ86VM9.
TreeFamiTF327301.

Miscellaneous databases

ChiTaRSiZC3H18. human.
GenomeRNAii124245.
NextBioi81250.
PROiQ86VM9.

Gene expression databases

BgeeiQ86VM9.
CleanExiHS_ZC3H18.
ExpressionAtlasiQ86VM9. baseline and differential.
GenevisibleiQ86VM9. HS.

Family and domain databases

InterProiIPR000571. Znf_CCCH.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 1 hit.
PROSITEiPS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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).
    Tissue: Brain.
  2. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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), VARIANT HIS-440.
    Tissue: Cervix and Testis.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-78; SER-83; SER-868 AND SER-893, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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-532 AND SER-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  8. "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-868, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-67; SER-74; SER-78; THR-109; SER-110; SER-532 AND SER-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-46; SER-74; SER-78; SER-83; THR-162; SER-534; SER-536; SER-842; SER-868 AND SER-893, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-46; SER-78; SER-83; SER-173; SER-534; SER-536; SER-842; SER-868; SER-893 AND SER-896, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-46; SER-53; SER-534 AND SER-842, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-622 AND LYS-766, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-622 AND LYS-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZCH18_HUMAN
AccessioniPrimary (citable) accession number: Q86VM9
Secondary accession number(s): Q96DG4, Q96MP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 24, 2009
Last modified: May 11, 2016
This is version 111 of the entry and version 2 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 16
    Human chromosome 16: 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.