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Q9H6S0

- YTDC2_HUMAN

UniProt

Q9H6S0 - YTDC2_HUMAN

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Protein

Probable ATP-dependent RNA helicase YTHDC2

Gene
YTHDC2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi216 – 2238ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. helicase activity Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. RNA-dependent ATPase activity Source: AgBase
  6. RNA polymerase binding Source: AgBase

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. positive regulation by host of viral genome replication Source: AgBase
  3. response to interleukin-1 Source: AgBase
  4. response to tumor necrosis factor Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase YTHDC2 (EC:3.6.4.13)
Gene namesi
Name:YTHDC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:24721. YTHDC2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: AgBase
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134912676.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14301430Probable ATP-dependent RNA helicase YTHDC2PRO_0000249340Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei1089 – 10891Phosphoserine1 Publication
Modified residuei1092 – 10921Phosphoserine1 Publication
Modified residuei1263 – 12631Phosphoserine By similarity
Modified residuei1267 – 12671Phosphoserine By similarity
Modified residuei1281 – 12811Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H6S0.
PaxDbiQ9H6S0.
PeptideAtlasiQ9H6S0.
PRIDEiQ9H6S0.

PTM databases

PhosphoSiteiQ9H6S0.

Expressioni

Gene expression databases

ArrayExpressiQ9H6S0.
BgeeiQ9H6S0.
CleanExiHS_YTHDC2.
GenevestigatoriQ9H6S0.

Organism-specific databases

HPAiHPA037364.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Irak1Q99J342EBI-1057466,EBI-6117042From a different organism.
IRF4Q153062EBI-1057466,EBI-751345

Protein-protein interaction databases

BioGridi122321. 11 interactions.
IntActiQ9H6S0. 10 interactions.
MINTiMINT-6944358.
STRINGi9606.ENSP00000161863.

Structurei

Secondary structure

1
1430
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1289 – 129810
Helixi1299 – 13068
Beta strandi1309 – 13113
Helixi1317 – 132610
Beta strandi1330 – 134213
Beta strandi1344 – 13485
Beta strandi1352 – 13543
Beta strandi1368 – 13758
Helixi1381 – 13844
Beta strandi1404 – 14063
Helixi1410 – 14156
Helixi1416 – 14194

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YU6NMR-A1288-1421[»]
ProteinModelPortaliQ9H6S0.
SMRiQ9H6S0. Positions 190-368, 492-1057, 1288-1421.

Miscellaneous databases

EvolutionaryTraceiQ9H6S0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 10669R3HAdd
BLAST
Domaini203 – 369167Helicase ATP-bindingAdd
BLAST
Repeati506 – 53833ANK 1Add
BLAST
Repeati539 – 57133ANK 2Add
BLAST
Domaini612 – 784173Helicase C-terminalAdd
BLAST
Domaini1288 – 1418131YTHAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi316 – 3194DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 3117Gly-richAdd
BLAST
Compositional biasi1248 – 128134Ser-richAdd
BLAST

Domaini

The YTH domain mediates RNA-binding By similarity.

Sequence similaritiesi

Contains 2 ANK repeats.
Contains 1 R3H domain.
Contains 1 YTH domain.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG1643.
HOGENOMiHOG000155703.
HOVERGENiHBG063891.
InParanoidiQ9H6S0.
OMAiPNMPVRY.
OrthoDBiEOG7Z69BN.
PhylomeDBiQ9H6S0.
TreeFamiTF318311.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.30.1370.50. 1 hit.
3.40.50.1820. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR001374. R3H_ss-bd.
IPR007275. YTH_domain.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
PF01424. R3H. 1 hit.
PF04146. YTH. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 2 hits.
SM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF82708. SSF82708. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51061. R3H. 1 hit.
PS50882. YTH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H6S0-1 [UniParc]FASTAAdd to Basket

« Hide

MSRPSSVSPR QPAPGGGGGG GPSPCGPGGG GRAKGLKDIR IDEEVKIAVN     50
IALERFRYGD QREMEFPSSL TSTERAFIHR LSQSLGLVSK SKGKGANRYL 100
TVKKKDGSET AHAMMTCNLT HNTKHAVRSL IQRFPVTNKE RTELLPKTER 150
GNVFAVEAEN REMSKTSGRL NNGIPQIPVK RGESEFDSFR QSLPVFEKQE 200
EIVKIIKENK VVLIVGETGS GKTTQIPQFL LDDCFKNGIP CRIFCTQPRR 250
LAAIAVAERV AAERRERIGQ TIGYQIRLES RVSPKTLLTF CTNGVLLRTL 300
MAGDSTLSTV THVIVDEVHE RDRFSDFLLT KLRDLLQKHP TLKLILSSAA 350
LDVNLFIRYF GSCPVIYIQG RPFEVKEMFL EDILRTTGYT NKEMLKYKKE 400
KQQEEKQQTT LTEWYSAQEN SFKPESQRQR TVLNVTDEYD LLDDGGDAVF 450
SQLTEKDVNC LEPWLIKEMD ACLSDIWLHK DIDAFAQVFH LILTENVSVD 500
YRHSETSATA LMVAAGRGFA SQVEQLISMG ANVHSKASNG WMALDWAKHF 550
GQTEIVDLLE SYSATLEFGN LDESSLVQTN GSDLSAEDRE LLKAYHHSFD 600
DEKVDLDLIM HLLYNICHSC DAGAVLIFLP GYDEIVGLRD RILFDDKRFA 650
DSTHRYQVFM LHSNMQTSDQ KKVLKNPPAG VRKIILSTNI AETSITVNDV 700
VFVIDSGKVK EKSFDALNFV TMLKMVWISK ASAIQRKGRA GRCRPGICFR 750
LFSRLRFQNM LEFQTPELLR MPLQELCLHT KLLAPVNCPI ADFLMKAPEP 800
PPALIVRNAV QMLKTIDAMD TWEDLTELGY HLADLPVEPH LGKMVLCAVV 850
LKCLDPILTI ACTLAYRDPF VLPTQASQKR AAMLCRKRFT AGAFSDHMAL 900
LRAFQAWQKA RSDGWERAFC EKNFLSQATM EIIIGMRTQL LGQLRASGFV 950
RARGGGDIRD VNTNSENWAV VKAALVAGMY PNLVHVDREN LVLTGPKEKK 1000
VRFHPASVLS QPQYKKIPPA NGQAAAIKAL PTDWLIYDEM TRAHRIANIR 1050
CCSAVTPVTI LVFCGPARLA SNALQEPSSF RVDGIPNDSS DSEMEDKTTA 1100
NLAALKLDEW LHFTLEPEAA SLLLQLRQKW HSLFLRRMRA PSKPWSQVDE 1150
ATIRAIIAVL STEEQSAGLQ QPSGIGQRPR PMSSEELPLA SSWRSNNSRK 1200
SSADTEFSDE CTTAERVLMK SPSPALHPPQ KYKDRGILHP KRGTEDRSDQ 1250
SSLKSTDSSS YPSPCASPSP PSSGKGSKSP SPRPNMPVRY FIMKSSNLRN 1300
LEISQQKGIW STTPSNERKL NRAFWESSIV YLVFSVQGSG HFQGFSRMSS 1350
EIGREKSQDW GSAGLGGVFK VEWIRKESLP FQFAHHLLNP WNDNKKVQIS 1400
RDGQELEPLV GEQLLQLWER LPLGEKNTTD 1430
Length:1,430
Mass (Da):160,248
Last modified:June 16, 2009 - v2
Checksum:iA0C3B45771A3DE16
GO

Sequence cautioni

The sequence BAB15183.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti652 – 6521S → N.
Corresponds to variant rs10071816 [ dbSNP | Ensembl ].
VAR_058002
Natural varianti1409 – 14091L → Q.1 Publication
Corresponds to variant rs1132528 [ dbSNP | Ensembl ].
VAR_058003

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti860 – 8601I → V in BAB15183. 1 Publication
Sequence conflicti993 – 9931L → S in BAB15183. 1 Publication
Sequence conflicti1230 – 12301Q → R in BAB15183. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC093208 Genomic DNA. No translation available.
AC010389 Genomic DNA. No translation available.
BC137285 mRNA. Translation: AAI37286.1.
AK025593 mRNA. Translation: BAB15183.1. Different initiation.
CCDSiCCDS4113.1.
RefSeqiNP_073739.3. NM_022828.3.
UniGeneiHs.231942.

Genome annotation databases

EnsembliENST00000161863; ENSP00000161863; ENSG00000047188.
GeneIDi64848.
KEGGihsa:64848.
UCSCiuc003kqn.3. human.

Polymorphism databases

DMDMi239938805.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC093208 Genomic DNA. No translation available.
AC010389 Genomic DNA. No translation available.
BC137285 mRNA. Translation: AAI37286.1 .
AK025593 mRNA. Translation: BAB15183.1 . Different initiation.
CCDSi CCDS4113.1.
RefSeqi NP_073739.3. NM_022828.3.
UniGenei Hs.231942.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YU6 NMR - A 1288-1421 [» ]
ProteinModelPortali Q9H6S0.
SMRi Q9H6S0. Positions 190-368, 492-1057, 1288-1421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122321. 11 interactions.
IntActi Q9H6S0. 10 interactions.
MINTi MINT-6944358.
STRINGi 9606.ENSP00000161863.

PTM databases

PhosphoSitei Q9H6S0.

Polymorphism databases

DMDMi 239938805.

Proteomic databases

MaxQBi Q9H6S0.
PaxDbi Q9H6S0.
PeptideAtlasi Q9H6S0.
PRIDEi Q9H6S0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000161863 ; ENSP00000161863 ; ENSG00000047188 .
GeneIDi 64848.
KEGGi hsa:64848.
UCSCi uc003kqn.3. human.

Organism-specific databases

CTDi 64848.
GeneCardsi GC05P112877.
HGNCi HGNC:24721. YTHDC2.
HPAi HPA037364.
neXtProti NX_Q9H6S0.
PharmGKBi PA134912676.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1643.
HOGENOMi HOG000155703.
HOVERGENi HBG063891.
InParanoidi Q9H6S0.
OMAi PNMPVRY.
OrthoDBi EOG7Z69BN.
PhylomeDBi Q9H6S0.
TreeFami TF318311.

Miscellaneous databases

EvolutionaryTracei Q9H6S0.
GenomeRNAii 64848.
NextBioi 66962.
PROi Q9H6S0.

Gene expression databases

ArrayExpressi Q9H6S0.
Bgeei Q9H6S0.
CleanExi HS_YTHDC2.
Genevestigatori Q9H6S0.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
3.30.1370.50. 1 hit.
3.40.50.1820. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR001374. R3H_ss-bd.
IPR007275. YTH_domain.
[Graphical view ]
Pfami PF12796. Ank_2. 1 hit.
PF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
PF01424. R3H. 1 hit.
PF04146. YTH. 1 hit.
[Graphical view ]
SMARTi SM00248. ANK. 2 hits.
SM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF82708. SSF82708. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51061. R3H. 1 hit.
PS50882. YTH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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].
    Tissue: Brain.
  3. "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] OF 730-1430, VARIANT GLN-1409.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092 AND SER-1281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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].
  6. "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-1089, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "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-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Solution structure of the YTH domain in YTH domain-containing protein 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1288-1421.

Entry informationi

Entry nameiYTDC2_HUMAN
AccessioniPrimary (citable) accession number: Q9H6S0
Secondary accession number(s): B2RP66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 16, 2009
Last modified: September 3, 2014
This is version 94 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

External Data

Dasty 3

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