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Protein

YTH domain-containing protein 1

Gene

YTHDC1

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

Functioni

Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed:26318451, PubMed:26876937, PubMed:25242552). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:26318451, PubMed:25242552). Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (PubMed:26876937). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (PubMed:26876937). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping: this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (PubMed:26876937). May also regulate alternative splice site selection (PubMed:20167602).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei377 – 3771N6-methyladenosine1 Publication
Binding sitei428 – 4281N6-methyladenosine1 Publication

GO - Molecular functioni

  • N6-methyladenosine-containing RNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

  • mRNA splice site selection Source: UniProtKB
  • regulation of mRNA splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

SignaLinkiQ96MU7.
SIGNORiQ96MU7.

Names & Taxonomyi

Protein namesi
Recommended name:
YTH domain-containing protein 1Curated
Alternative name(s):
Splicing factor YT5211 Publication
Short name:
YT521-B1 Publication
Gene namesi
Name:YTHDC1Imported
Synonyms:KIAA19661 Publication, YT5211 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:30626. YTHDC1.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi361 – 3611K → L: Does not affect ability to influence alternative splice site selection. 1 Publication
Mutagenesisi362 – 3621S → A: Does not affect ability to influence alternative splice site selection. 1 Publication
Mutagenesisi367 – 3671N → D: Abolished binding to N6-methyladenosine (m6A)-containing RNAs. 1 Publication
Mutagenesisi377 – 3771W → A: Abolishes binding to N6-methyladenosine (m6A)-containing RNAs. Abolishes binding to m6A-containing mRNAs; when associated with A-428. 2 Publications
Mutagenesisi377 – 3771W → D: Abolishes RNA-binding and ability to influence alternative splice site selection. 1 Publication
Mutagenesisi380 – 3801L → T: Reduced binding to N6-methyladenosine (m6A)-containing RNAs. 1 Publication
Mutagenesisi387 – 3871L → E: Does not affect ability to influence alternative splice site selection. 1 Publication
Mutagenesisi399 – 3991L → E: Does not affect ability to influence alternative splice site selection. 1 Publication
Mutagenesisi401 – 4011F → D: Does not affect ability to influence alternative splice site selection. 1 Publication
Mutagenesisi402 – 4021S → A: Does not affect ability to influence alternative splice site selection. 1 Publication
Mutagenesisi409 – 4091F → D: Abolishes RNA-binding and ability to influence alternative splice site selection. 1 Publication
Mutagenesisi411 – 4111G → I: Abolishes RNA-binding and ability to influence alternative splice site selection. 1 Publication
Mutagenesisi428 – 4281W → A: Abolishes binding to N6-methyladenosine (m6A)-containing RNAs. Abolishes binding to m6A-containing mRNAs; when associated with A-377. 2 Publications
Mutagenesisi428 – 4281W → D: Does not affect ability to influence alternative splice site selection. 1 Publication
Mutagenesisi438 – 4381M → A: Reduced binding to N6-methyladenosine (m6A)-containing RNAs. 1 Publication
Mutagenesisi447 – 4471W → D: Does not affect ability to influence alternative splice site selection. 1 Publication
Mutagenesisi466 – 4661N → D: Does not affect ability to influence alternative splice site selection. 1 Publication
Mutagenesisi475 – 4751R → A: Reduced binding affinity for N6-methyladenosine (m6A)-containing RNAs by 100-fold. 1 Publication
Mutagenesisi475 – 4751R → D: Does not affect ability to influence alternative splice site selection. 1 Publication
Mutagenesisi475 – 4751R → F: Reduced binding affinity for N6-methyladenosine (m6A)-containing RNAs by 9-fold. 1 Publication
Mutagenesisi476 – 4761D → K: Does not affect ability to influence alternative splice site selection. 1 Publication

Organism-specific databases

PharmGKBiPA143485673.

Polymorphism and mutation databases

BioMutaiYTHDC1.
DMDMi47606762.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 727727YTH domain-containing protein 1PRO_0000223076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351PhosphoserineBy similarity
Cross-linki96 – 96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei120 – 1201PhosphoserineCombined sources
Modified residuei146 – 1461PhosphoserineCombined sources
Modified residuei148 – 1481PhosphothreonineCombined sources
Modified residuei308 – 3081PhosphoserineCombined sources
Modified residuei315 – 3151PhosphoserineCombined sources
Modified residuei317 – 3171PhosphoserineCombined sources
Modified residuei318 – 3181PhosphoserineCombined sources
Modified residuei320 – 3201PhosphoserineCombined sources
Modified residuei424 – 4241PhosphoserineCombined sources
Modified residuei435 – 4351PhosphoserineCombined sources
Modified residuei545 – 5451PhosphoserineCombined sources

Post-translational modificationi

Tyrosine phosphorylated.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96MU7.
MaxQBiQ96MU7.
PaxDbiQ96MU7.
PeptideAtlasiQ96MU7.
PRIDEiQ96MU7.

PTM databases

iPTMnetiQ96MU7.
PhosphoSiteiQ96MU7.
SwissPalmiQ96MU7.

Expressioni

Gene expression databases

BgeeiQ96MU7.
CleanExiHS_YTHDC1.
ExpressionAtlasiQ96MU7. baseline and differential.
GenevisibleiQ96MU7. HS.

Organism-specific databases

HPAiHPA036462.

Interactioni

Subunit structurei

Interacts with KHDRBS1/SAM68 (By similarity). Interacts with SRSF1 (By similarity). Interacts with SRSF2 (By similarity). Interacts with TRA2B (By similarity). Interacts with SRSF3 (PubMed:26876937). Interacts with SRSF10 (PubMed:26876937). Interacts with KHDRBS3 (By similarity). Interacts with EMD (PubMed:12755701). Interacts with RBMX (PubMed:19282290).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CLK2P497603EBI-2849854,EBI-750020
DVL3Q929973EBI-2849854,EBI-739789
HNRPKQ6IBN13EBI-2849854,EBI-3440248
KHDRBS2Q5VWX13EBI-2849854,EBI-742808
KHDRBS3O755253EBI-2849854,EBI-722504
RBMY1JQ154153EBI-2849854,EBI-8642021
SDCBP2Q9H1903EBI-2849854,EBI-742426
SRPK1Q96SB43EBI-2849854,EBI-539478
SRPK2P783623EBI-2849854,EBI-593303

Protein-protein interaction databases

BioGridi124871. 62 interactions.
IntActiQ96MU7. 30 interactions.
MINTiMINT-266035.
STRINGi9606.ENSP00000339245.

Structurei

Secondary structure

1
727
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi345 – 3528Combined sources
Beta strandi355 – 3639Combined sources
Helixi365 – 37410Combined sources
Beta strandi376 – 3783Combined sources
Helixi381 – 39111Combined sources
Beta strandi394 – 40310Combined sources
Beta strandi406 – 4094Combined sources
Beta strandi411 – 4155Combined sources
Beta strandi422 – 4243Combined sources
Helixi437 – 4393Combined sources
Beta strandi442 – 4498Combined sources
Helixi455 – 4584Combined sources
Helixi464 – 4663Combined sources
Beta strandi467 – 4693Combined sources
Beta strandi478 – 4803Combined sources
Helixi482 – 49110Combined sources
Beta strandi496 – 4983Combined sources
Helixi500 – 5067Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YUDNMR-A337-509[»]
4R3HX-ray1.90A/B345-509[»]
4R3IX-ray1.80A345-509[»]
ProteinModelPortaliQ96MU7.
SMRiQ96MU7. Positions 345-507.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96MU7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini355 – 492138YTHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni361 – 3633N6-methyladenosine bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi172 – 26089Glu-richAdd
BLAST
Compositional biasi508 – 58174Arg-richAdd
BLAST
Compositional biasi601 – 64343Pro-richAdd
BLAST
Compositional biasi647 – 72781Arg-richAdd
BLAST

Domaini

The YTH domain mediates RNA-binding.1 Publication

Sequence similaritiesi

Contains 1 YTH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1902. Eukaryota.
ENOG4111F6P. LUCA.
GeneTreeiENSGT00690000102240.
HOGENOMiHOG000088650.
HOVERGENiHBG055528.
InParanoidiQ96MU7.
KOiK20100.
OrthoDBiEOG7R2BMC.
PhylomeDBiQ96MU7.
TreeFamiTF325590.

Family and domain databases

InterProiIPR007275. YTH_domain.
[Graphical view]
PfamiPF04146. YTH. 1 hit.
[Graphical view]
PROSITEiPS50882. YTH. 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: Q96MU7-1) [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
MAADSREEKD GELNVLDDIL TEVPEQDDEL YNPESEQDKN EKKGSKRKSD
60 70 80 90 100
RMESTDTKRQ KPSVHSRQLV SKPLSSSVSN NKRIVSTKGK SATEYKNEEY
110 120 130 140 150
QRSERNKRLD ADRKIRLSSS ASREPYKNQP EKTCVRKRDP ERRAKSPTPD
160 170 180 190 200
GSERIGLEVD RRASRSSQSS KEEVNSEEYG SDHETGSSGS SDEQGNNTEN
210 220 230 240 250
EEEGVEEDVE EDEEVEEDAE EDEEVDEDGE EEEEEEEEEE EEEEEEEEEY
260 270 280 290 300
EQDERDQKEE GNDYDTRSEA SDSGSESVSF TDGSVRSGSG TDGSDEKKKE
310 320 330 340 350
RKRARGISPI VFDRSGSSAS ESYAGSEKKH EKLSSSVRAV RKDQTSKLKY
360 370 380 390 400
VLQDARFFLI KSNNHENVSL AKAKGVWSTL PVNEKKLNLA FRSARSVILI
410 420 430 440 450
FSVRESGKFQ GFARLSSESH HGGSPIHWVL PAGMSAKMLG GVFKIDWICR
460 470 480 490 500
RELPFTKSAH LTNPWNEHKP VKIGRDGQEI ELECGTQLCL LFPPDESIDL
510 520 530 540 550
YQVIHKMRHK RRMHSQPRSR GRPSRREPVR DVGRRRPEDY DIHNSRKKPR
560 570 580 590 600
IDYPPEFHQR PGYLKDPRYQ EVDRRFSGVR RDVFLNGSYN DYVREFHNMG
610 620 630 640 650
PPPPWQGMPP YPGMEQPPHH PYYQHHAPPP QAHPPYSGHH PVPHEARYRD
660 670 680 690 700
KRVHDYDMRV DDFLRRTQAV VSGRRSRPRE RDRERERDRP RDNRRDRERD
710 720
RGRDRERERE RLCDRDRDRG ERGRYRR
Length:727
Mass (Da):84,700
Last modified:May 24, 2004 - v3
Checksum:i536032FD44582EAF
GO
Isoform 2 (identifier: Q96MU7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     325-342: Missing.

Show »
Length:709
Mass (Da):82,692
Checksum:iC02121B27DDEFF0E
GO

Sequence cautioni

The sequence AAY41024.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAB71181.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti619 – 6191H → Q in BAB71181 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti183 – 1831H → R.
Corresponds to variant rs3813832 [ dbSNP | Ensembl ].
VAR_053746

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei325 – 34218Missing in isoform 2. 2 PublicationsVSP_006818Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056430 mRNA. Translation: BAB71181.1. Different initiation.
AC074378 Genomic DNA. Translation: AAY41024.1. Sequence problems.
BC041119 mRNA. Translation: AAH41119.1.
BC053863 mRNA. Translation: AAH53863.1.
AB075846 mRNA. Translation: BAB85552.1.
CCDSiCCDS33992.1. [Q96MU7-1]
CCDS3522.2. [Q96MU7-2]
RefSeqiNP_001026902.1. NM_001031732.2. [Q96MU7-1]
NP_588611.2. NM_133370.2. [Q96MU7-2]
UniGeneiHs.175955.

Genome annotation databases

EnsembliENST00000344157; ENSP00000339245; ENSG00000083896. [Q96MU7-1]
ENST00000355665; ENSP00000347888; ENSG00000083896. [Q96MU7-2]
ENST00000613637; ENSP00000484604; ENSG00000275272. [Q96MU7-2]
ENST00000615500; ENSP00000479213; ENSG00000275272. [Q96MU7-1]
GeneIDi91746.
KEGGihsa:91746.
UCSCiuc003hdx.4. human. [Q96MU7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056430 mRNA. Translation: BAB71181.1. Different initiation.
AC074378 Genomic DNA. Translation: AAY41024.1. Sequence problems.
BC041119 mRNA. Translation: AAH41119.1.
BC053863 mRNA. Translation: AAH53863.1.
AB075846 mRNA. Translation: BAB85552.1.
CCDSiCCDS33992.1. [Q96MU7-1]
CCDS3522.2. [Q96MU7-2]
RefSeqiNP_001026902.1. NM_001031732.2. [Q96MU7-1]
NP_588611.2. NM_133370.2. [Q96MU7-2]
UniGeneiHs.175955.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YUDNMR-A337-509[»]
4R3HX-ray1.90A/B345-509[»]
4R3IX-ray1.80A345-509[»]
ProteinModelPortaliQ96MU7.
SMRiQ96MU7. Positions 345-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124871. 62 interactions.
IntActiQ96MU7. 30 interactions.
MINTiMINT-266035.
STRINGi9606.ENSP00000339245.

PTM databases

iPTMnetiQ96MU7.
PhosphoSiteiQ96MU7.
SwissPalmiQ96MU7.

Polymorphism and mutation databases

BioMutaiYTHDC1.
DMDMi47606762.

Proteomic databases

EPDiQ96MU7.
MaxQBiQ96MU7.
PaxDbiQ96MU7.
PeptideAtlasiQ96MU7.
PRIDEiQ96MU7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344157; ENSP00000339245; ENSG00000083896. [Q96MU7-1]
ENST00000355665; ENSP00000347888; ENSG00000083896. [Q96MU7-2]
ENST00000613637; ENSP00000484604; ENSG00000275272. [Q96MU7-2]
ENST00000615500; ENSP00000479213; ENSG00000275272. [Q96MU7-1]
GeneIDi91746.
KEGGihsa:91746.
UCSCiuc003hdx.4. human. [Q96MU7-1]

Organism-specific databases

CTDi91746.
GeneCardsiYTHDC1.
HGNCiHGNC:30626. YTHDC1.
HPAiHPA036462.
neXtProtiNX_Q96MU7.
PharmGKBiPA143485673.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1902. Eukaryota.
ENOG4111F6P. LUCA.
GeneTreeiENSGT00690000102240.
HOGENOMiHOG000088650.
HOVERGENiHBG055528.
InParanoidiQ96MU7.
KOiK20100.
OrthoDBiEOG7R2BMC.
PhylomeDBiQ96MU7.
TreeFamiTF325590.

Enzyme and pathway databases

SignaLinkiQ96MU7.
SIGNORiQ96MU7.

Miscellaneous databases

ChiTaRSiYTHDC1. human.
EvolutionaryTraceiQ96MU7.
GeneWikiiYTHDC1.
GenomeRNAii91746.
PROiQ96MU7.

Gene expression databases

BgeeiQ96MU7.
CleanExiHS_YTHDC1.
ExpressionAtlasiQ96MU7. baseline and differential.
GenevisibleiQ96MU7. HS.

Family and domain databases

InterProiIPR007275. YTH_domain.
[Graphical view]
PfamiPF04146. YTH. 1 hit.
[Graphical view]
PROSITEiPS50882. YTH. 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).
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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] (ISOFORMS 1 AND 2).
    Tissue: Skin.
  4. "Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-727 (ISOFORM 1).
    Tissue: Brain.
  5. Cited for: INTERACTION WITH EMD.
  6. "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-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-315; SER-317; SER-318; SER-320 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA."
    Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R., Stamm S.
    J. Biol. Chem. 284:14303-14315(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBMX.
  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-146; THR-148; SER-308; SER-424 AND SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-120; SER-308; SER-424 AND SER-545, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; THR-148 AND SER-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "structural basis for the discriminative recognition of N6-methyladenosine RNA by the human YT521-B homology domain family of proteins."
    Xu C., Liu K., Ahmed H., Loppnau P., Schapira M., Min J.
    J. Biol. Chem. 290:24902-24913(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, MUTAGENESIS OF ASN-367; LEU-380 AND MET-438.
  17. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SRSF3 AND SRSF10, MUTAGENESIS OF TRP-377 AND TRP-428.
  18. Cited for: STRUCTURE BY NMR OF 334-509, RNA-BINDING, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF LYS-361; SER-362; TRP-377; LEU-387; LEU-399; PHE-401; SER-402; PHE-409; GLY-411; TRP-428; TRP-447; ASN-466; ARG-475 AND ASP-476.
  19. "Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain."
    Xu C., Wang X., Liu K., Roundtree I.A., Tempel W., Li Y., Lu Z., He C., Min J.
    Nat. Chem. Biol. 10:927-929(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 345-509 IN COMPLEX WITH N6-METHYLADENOSINE (M6A)-CONTAINING RNA, FUNCTION, RNA-BINDING, MUTAGENESIS OF TRP-377; TRP-428 AND ARG-475.

Entry informationi

Entry nameiYTDC1_HUMAN
AccessioniPrimary (citable) accession number: Q96MU7
Secondary accession number(s): Q4W5Q3, Q7Z622, Q8TF35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 24, 2004
Last modified: July 6, 2016
This is version 140 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.