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Q5T200

- ZC3HD_HUMAN

UniProt

Q5T200 - ZC3HD_HUMAN

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Protein

Zinc finger CCCH domain-containing protein 13

Gene

ZC3H13

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

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri36 – 6429C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. 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 13
Gene namesi
Name:ZC3H13
Synonyms:KIAA0853
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:20368. ZC3H13.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134907656.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16681668Zinc finger CCCH domain-containing protein 13PRO_0000050778Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphoserine1 Publication
Modified residuei198 – 1981Phosphoserine3 Publications
Modified residuei207 – 2071Phosphoserine2 Publications
Modified residuei209 – 2091Phosphoserine2 Publications
Modified residuei237 – 2371Phosphothreonine1 Publication
Modified residuei242 – 2421Phosphoserine5 Publications
Modified residuei263 – 2631Phosphothreonine6 Publications
Modified residuei265 – 2651Phosphoserine6 Publications
Modified residuei316 – 3161Phosphoserine1 Publication
Modified residuei318 – 3181Phosphoserine1 Publication
Modified residuei325 – 3251Phosphoserine2 Publications
Modified residuei328 – 3281Phosphoserine1 Publication
Modified residuei354 – 3541Phosphothreonine1 Publication
Modified residuei364 – 3641Phosphothreonine1 Publication
Modified residuei370 – 3701Phosphoserine3 Publications
Modified residuei372 – 3721Phosphoserine3 Publications
Modified residuei381 – 3811Phosphoserine3 Publications
Modified residuei831 – 8311Phosphoserine1 Publication
Modified residuei833 – 8331Phosphoserine1 Publication
Modified residuei837 – 8371Phosphoserine1 Publication
Modified residuei845 – 8451Phosphoserine3 Publications
Modified residuei848 – 8481Phosphoserine3 Publications
Modified residuei853 – 8531Phosphoserine3 Publications
Modified residuei875 – 8751Phosphoserine1 Publication
Modified residuei877 – 8771Phosphoserine3 Publications
Modified residuei882 – 8821Phosphothreonine1 Publication
Modified residuei986 – 9861Phosphoserine3 Publications
Modified residuei993 – 9931Phosphoserine5 Publications
Modified residuei1010 – 10101Phosphoserine3 Publications
Modified residuei1014 – 10141Phosphoserine3 Publications
Modified residuei1017 – 10171Phosphoserine4 Publications
Modified residuei1170 – 11701Phosphothreonine1 Publication
Modified residuei1191 – 11911Phosphoserine1 Publication
Modified residuei1194 – 11941Phosphoserine1 Publication
Modified residuei1208 – 12081Phosphoserine2 Publications
Modified residuei1210 – 12101Phosphoserine1 Publication
Modified residuei1230 – 12301Phosphoserine1 Publication
Modified residuei1364 – 13641Phosphoserine1 Publication
Modified residuei1366 – 13661Phosphoserine1 Publication
Modified residuei1382 – 13821Phosphoserine1 Publication
Modified residuei1438 – 14381Phosphoserine1 Publication
Modified residuei1465 – 14651Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5T200.
PaxDbiQ5T200.
PRIDEiQ5T200.

PTM databases

PhosphoSiteiQ5T200.

Miscellaneous databases

PMAP-CutDBQ5T200.

Expressioni

Gene expression databases

BgeeiQ5T200.
CleanExiHS_ZC3H13.
ExpressionAtlasiQ5T200. baseline and differential.
GenevestigatoriQ5T200.

Organism-specific databases

HPAiHPA039340.
HPA040140.
HPA047806.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SCHIP1Q9P0W52EBI-2679720,EBI-1397509

Protein-protein interaction databases

BioGridi116719. 44 interactions.
IntActiQ5T200. 7 interactions.
MINTiMINT-3306871.
STRINGi9606.ENSP00000282007.

Structurei

3D structure databases

ProteinModelPortaliQ5T200.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili645 – 789145Sequence AnalysisAdd
BLAST
Coiled coili1300 – 136667Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi204 – 24239Ser-richAdd
BLAST
Compositional biasi316 – 34934Ser-richAdd
BLAST
Compositional biasi350 – 652303Arg/Ser-richAdd
BLAST
Compositional biasi653 – 842190Arg/Glu-richAdd
BLAST
Compositional biasi957 – 102872Lys-richAdd
BLAST
Compositional biasi1189 – 1295107Ser-richAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri36 – 6429C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG301709.
GeneTreeiENSGT00730000111163.
HOVERGENiHBG107115.
InParanoidiQ5T200.
OMAiSYQRTIT.
OrthoDBiEOG7DC23Q.
PhylomeDBiQ5T200.
TreeFamiTF332670.

Family and domain databases

Gene3Di4.10.1000.10. 1 hit.
InterProiIPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 1 hit.
[Graphical view]
PROSITEiPS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5T200-1) [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
MSKIRRKVTV ENTKTISDST SRRPSVFERL GPSTGSTAET QCRNWLKTGN
60 70 80 90 100
CLYGNTCRFV HGPSPRGKGY SSNYRRSPER PTGDLRERMK NKRQDVDTEP
110 120 130 140 150
QKRNTEESSS PVRKESSRGR HREKEDIKIT KERTPESEEE NVEWETNRDD
160 170 180 190 200
SDNGDINYDY VHELSLEMKR QKIQRELMKL EQENMEKREE IIIKKEVSPE
210 220 230 240 250
VVRSKLSPSP SLRKSSKSPK RKSSPKSSSA SKKDRKTSAV SSPLLDQQRN
260 270 280 290 300
SKTNQSKKKG PRTPSPPPPI PEDIALGKKY KEKYKVKDRI EEKTRDGKDR
310 320 330 340 350
GRDFERQREK RDKPRSTSPA GQHHSPISSR HHSSSSQSGS SIQRHSPSPR
360 370 380 390 400
RKRTPSPSYQ RTLTPPLRRS ASPYPSHSLS SPQRKQSPPR HRSPMREKGR
410 420 430 440 450
HDHERTSQSH DRRHERREDT RGKRDREKDS REEREYEQDQ SSSRDHRDDR
460 470 480 490 500
EPRDGRDRRD ARDTRDRREL RDSRDMRDSR EMRDYSRDTK ESRDPRDSRS
510 520 530 540 550
TRDAHDYRDR EGRDTHRKED TYPEESRSYG RNHLREESSR TEIRNESRNE
560 570 580 590 600
SRSEIRNDRM GRSRGRVPEL PEKGSRGSRG SQIDSHSSNS NYHDSWETRS
610 620 630 640 650
SYPERDRYPE RDNRDQARDS SFERRHGERD RRDNRERDQR PSSPIRHQGR
660 670 680 690 700
NDELERDERR EERRVDRVDD RRDERARERD RERERDRERE RERERERDRE
710 720 730 740 750
REKERELERE RARERERERE KERDRERDRD RDHDRERERE RERDREKERE
760 770 780 790 800
REREERERER ERERERERER ERERERARER DKERERQRDW EDKDKGRDDR
810 820 830 840 850
REKREEIRED RNPRDGHDER KSKKRYRNEG SPSPRQSPKR RREHSPDSDA
860 870 880 890 900
YNSGDDKNEK HRLLSQVVRP QESRSLSPSH LTEDRQGRWK EEDRKPERKE
910 920 930 940 950
SSRRYEEQEL KEKVSSVDKQ REQTEILESS RMRAQDIIGH HQSEDRETSD
960 970 980 990 1000
RAHDENKKKA KIQKKPIKKK KEDDVGIERG NIETTSEDGQ VFSPKKGQKK
1010 1020 1030 1040 1050
KSIEKKRKKS KGDSDISDEE AAQQSKKKRG PRTPPITTKE ELVEMCNGKN
1060 1070 1080 1090 1100
GILEDSQKKE DTAFSDWSDE DVPDRTEVTE AEHTATATTP GSTPSPLSSL
1110 1120 1130 1140 1150
LPPPPPVATA TATTVPATLA ATTAAAATSF STSAITISTS ATPTNTTNNT
1160 1170 1180 1190 1200
FANEDSHRKC HRTRVEKVET PHVTIEDAQH RKPMDQKRSS SLGSNRSNRS
1210 1220 1230 1240 1250
HTSGRLRSPS NDSAHRSGDD QSGRKRVLHS GSRDREKTKS LEITGERKSR
1260 1270 1280 1290 1300
IDQLKRGEPS RSTSSDRQDS RSHSSRRSSP ESDRQVHSRS GSFDSRDRLQ
1310 1320 1330 1340 1350
ERDRYEHDRE RERERRDTRQ REWDRDADKD WPRNRDRDRL RERERERERD
1360 1370 1380 1390 1400
KRRDLDRERE RLISDSVERD RDRDRDRTFE SSQIESVKRC EAKLEGEHER
1410 1420 1430 1440 1450
DLESTSRDSL ALDKERMDKD LGSVQGFEET NKSERTESLE GDDESKLDDA
1460 1470 1480 1490 1500
HSLGSGAGEG YEPISDDELD EILAGDAEKR EDQQDEEKMP DPLDVIDVDW
1510 1520 1530 1540 1550
SGLMPKHPKE PREPGAALLK FTPGAVMLRV GISKKLAGSE LFAKVKETCQ
1560 1570 1580 1590 1600
RLLEKPKDAD NLFEHELGAL NMAALLRKEE RASLLSNLGP CCKALCFRRD
1610 1620 1630 1640 1650
SAIRKQLVKN EKGTIKQAYT SAPMVDNELL RLSLRLFKRK TTCHAPGHEK
1660
TEDNKLSQSS IQQELCVS

Note: Gene prediction confirmed by EST data.

Length:1,668
Mass (Da):196,635
Last modified:December 21, 2004 - v1
Checksum:iB7E8118D3B5954D6
GO
Isoform 2 (identifier: Q5T200-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1440-1440: E → EA
     1558-1563: DADNLF → GSFILL
     1564-1668: Missing.

Note: Contains a phosphoserine at position 1453. Contains a phosphoserine at position 1456. Contains a phosphoserine at position 1466.

Show »
Length:1,564
Mass (Da):184,869
Checksum:iEDF7A3EA9DB7448B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti702 – 7043EKE → KAR in BAA74876. (PubMed:10048485)Curated
Sequence conflicti967 – 9671I → K in CAD38544. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1429 – 14291E → D.4 Publications
Corresponds to variant rs9534264 [ dbSNP | Ensembl ].
VAR_022727

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1440 – 14401E → EA in isoform 2. 2 PublicationsVSP_027202
Alternative sequencei1558 – 15636DADNLF → GSFILL in isoform 2. 2 PublicationsVSP_014252
Alternative sequencei1564 – 1668105Missing in isoform 2. 2 PublicationsVSP_014253Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY283618 mRNA. Translation: AAP37483.1.
AL157758, AL445232 Genomic DNA. Translation: CAI10903.1.
AL157758, AL445232 Genomic DNA. Translation: CAM13064.1.
AL445232, AL157758 Genomic DNA. Translation: CAI16505.1.
AL445232, AL157758 Genomic DNA. Translation: CAI16506.2.
AL831833 mRNA. Translation: CAD38544.1.
AL136745 mRNA. Translation: CAB66679.2.
AB020660 mRNA. Translation: BAA74876.1.
CCDSiCCDS9400.1. [Q5T200-2]
RefSeqiNP_055885.3. NM_015070.4. [Q5T200-2]
XP_005266368.1. XM_005266311.1. [Q5T200-1]
XP_005266369.1. XM_005266312.1. [Q5T200-2]
UniGeneiHs.136102.

Genome annotation databases

EnsembliENST00000242848; ENSP00000242848; ENSG00000123200. [Q5T200-1]
ENST00000282007; ENSP00000282007; ENSG00000123200. [Q5T200-2]
GeneIDi23091.
KEGGihsa:23091.
UCSCiuc001vas.1. human. [Q5T200-2]
uc001vat.1. human. [Q5T200-1]

Polymorphism databases

DMDMi68052314.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY283618 mRNA. Translation: AAP37483.1 .
AL157758 , AL445232 Genomic DNA. Translation: CAI10903.1 .
AL157758 , AL445232 Genomic DNA. Translation: CAM13064.1 .
AL445232 , AL157758 Genomic DNA. Translation: CAI16505.1 .
AL445232 , AL157758 Genomic DNA. Translation: CAI16506.2 .
AL831833 mRNA. Translation: CAD38544.1 .
AL136745 mRNA. Translation: CAB66679.2 .
AB020660 mRNA. Translation: BAA74876.1 .
CCDSi CCDS9400.1. [Q5T200-2 ]
RefSeqi NP_055885.3. NM_015070.4. [Q5T200-2 ]
XP_005266368.1. XM_005266311.1. [Q5T200-1 ]
XP_005266369.1. XM_005266312.1. [Q5T200-2 ]
UniGenei Hs.136102.

3D structure databases

ProteinModelPortali Q5T200.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116719. 44 interactions.
IntActi Q5T200. 7 interactions.
MINTi MINT-3306871.
STRINGi 9606.ENSP00000282007.

PTM databases

PhosphoSitei Q5T200.

Polymorphism databases

DMDMi 68052314.

Proteomic databases

MaxQBi Q5T200.
PaxDbi Q5T200.
PRIDEi Q5T200.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000242848 ; ENSP00000242848 ; ENSG00000123200 . [Q5T200-1 ]
ENST00000282007 ; ENSP00000282007 ; ENSG00000123200 . [Q5T200-2 ]
GeneIDi 23091.
KEGGi hsa:23091.
UCSCi uc001vas.1. human. [Q5T200-2 ]
uc001vat.1. human. [Q5T200-1 ]

Organism-specific databases

CTDi 23091.
GeneCardsi GC13M046528.
H-InvDB HIX0000705.
HIX0011294.
HIX0039579.
HGNCi HGNC:20368. ZC3H13.
HPAi HPA039340.
HPA040140.
HPA047806.
neXtProti NX_Q5T200.
PharmGKBi PA134907656.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG301709.
GeneTreei ENSGT00730000111163.
HOVERGENi HBG107115.
InParanoidi Q5T200.
OMAi SYQRTIT.
OrthoDBi EOG7DC23Q.
PhylomeDBi Q5T200.
TreeFami TF332670.

Miscellaneous databases

ChiTaRSi ZC3H13. human.
GeneWikii ZC3H13.
GenomeRNAii 23091.
NextBioi 44243.
PMAP-CutDB Q5T200.
PROi Q5T200.

Gene expression databases

Bgeei Q5T200.
CleanExi HS_ZC3H13.
ExpressionAtlasi Q5T200. baseline and differential.
Genevestigatori Q5T200.

Family and domain databases

Gene3Di 4.10.1000.10. 1 hit.
InterProi IPR000571. Znf_CCCH.
[Graphical view ]
Pfami PF00642. zf-CCCH. 1 hit.
[Graphical view ]
SMARTi SM00356. ZnF_C3H1. 1 hit.
[Graphical view ]
PROSITEi PS50103. ZF_C3H1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Shan Y.X., Yu L.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASP-1429.
  2. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-971, VARIANT ASP-1429.
    Tissue: Fetal brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-1668 (ISOFORM 2), VARIANT ASP-1429.
    Tissue: Testis.
  5. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 702-1668 (ISOFORM 1), VARIANT ASP-1429.
    Tissue: Brain.
  6. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263 AND SER-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "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-198; THR-263 AND SER-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-242; THR-263; SER-265 AND SER-993, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "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.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-209; SER-242; SER-316; SER-318; SER-325; THR-354; THR-364; SER-370; SER-372; SER-381; SER-831; SER-833; SER-837; SER-845; SER-848; SER-853; SER-875; SER-877; SER-986; SER-993; SER-1010; SER-1014 AND SER-1017, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1453; SER-1456 AND SER-1466 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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].
  13. "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-242; THR-263; SER-265; SER-986; SER-993; SER-1014 AND SER-1017, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-64; SER-198; SER-207; SER-209; SER-242; THR-263; SER-265; SER-370; SER-372; SER-381; SER-845; SER-848; SER-853; SER-877; SER-993; SER-1010; SER-1014; SER-1017; THR-1170; SER-1208; SER-1230; SER-1364; SER-1366 AND SER-1438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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-198; THR-237; SER-242; THR-263; SER-265; SER-325; SER-328; SER-370; SER-372; SER-381; SER-845; SER-848; SER-853; SER-877; THR-882; SER-986; SER-993; SER-1010; SER-1017; SER-1191; SER-1194; SER-1208; SER-1210 AND SER-1465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZC3HD_HUMAN
AccessioniPrimary (citable) accession number: Q5T200
Secondary accession number(s): A2A323
, O94936, Q5T1Z9, Q7Z7J3, Q8NDT6, Q9H0L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 91 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 13
    Human chromosome 13: 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

External Data

Dasty 3