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Q7Z388 (D19L4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable C-mannosyltransferase DPY19L4

EC=2.4.1.-
Alternative name(s):
Dpy-19-like protein 4
Protein dpy-19 homolog 4
Gene names
Name:DPY19L4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins By similarity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Widely expressed. Ref.5

Sequence similarities

Belongs to the dpy-19 family.

Sequence caution

The sequence BAC85664.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiontransferase activity, transferring glycosyl groups

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 723722Probable C-mannosyltransferase DPY19L4
PRO_0000311881

Regions

Transmembrane52 – 7221Helical; Potential
Transmembrane161 – 17818Helical; Potential
Transmembrane184 – 20219Helical; Potential
Transmembrane222 – 24019Helical; Potential
Transmembrane260 – 28021Helical; Potential
Transmembrane292 – 31019Helical; Potential
Transmembrane316 – 33722Helical; Potential
Transmembrane349 – 37022Helical; Potential
Transmembrane421 – 44121Helical; Potential
Transmembrane466 – 48621Helical; Potential
Transmembrane489 – 50921Helical; Potential
Transmembrane522 – 54221Helical; Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.6

Experimental info

Sequence conflict31E → D in CAD98049. Ref.2
Sequence conflict4401I → T in BAC85664. Ref.1
Sequence conflict6541M → T in BAC85675. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7Z388 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: F1B385FF181F7193

FASTA72383,756
        10         20         30         40         50         60 
MAEEEGPPVE LRQRKKPKSS ENKESAKEEK ISDIPIPERA PKHVLFQRFA KIFIGCLAAV 

        70         80         90        100        110        120 
TSGMMYALYL SAYHERKFWF SNRQELEREI TFQGDSAIYY SYYKDMLKAP SFERGVYELT 

       130        140        150        160        170        180 
HNNKTVSLKT INAVQQMSLY PELIASILYQ ATGSNEIIEP VYFYIGIVFG LQGIYVTALF 

       190        200        210        220        230        240 
VTSWLMSGTW LAGMLTVAWF VINRVDTTRI EYSIPLRENW ALPYFACQIA ALTGYLKSNL 

       250        260        270        280        290        300 
NTYGERFCYL LMSASTYTFM MMWEYSHYLL FLQAISLFLL DTFSVEQSDK VYEVYKIYIF 

       310        320        330        340        350        360 
SLFLGYLLQF ENPALLVSPL LSLVAALMLA KCLQLNVKKG SFVAKIIKVI NFYLVCTLTI 

       370        380        390        400        410        420 
TLNIIMKMFV PHKENGHMLK FLEVKFGLNM TKNFTMNWLL CQESLQAPSQ DFFLRLTQSS 

       430        440        450        460        470        480 
LLPFYILVLI ICFLSMLQVI FRRINGKSLK ETVTLEDGRI GERPEIIYHV IHTILLGSLA 

       490        500        510        520        530        540 
MVIEGLKYIW IPYVCMLAAF GVCSPELWMT LFKWLRLRTV HPILLALILS MAVPTIIGLS 

       550        560        570        580        590        600 
LWKEFFPRLM TELMELQEFY DPDTVELMTW IKRQAPVAAV FAGSPQLMGA IKLCTGWMVT 

       610        620        630        640        650        660 
SLPLYNDDDL LKRNENIYQI YSKRSAEDIY KILTSYKANY LIVEDAICNE VGPMRGCRVK 

       670        680        690        700        710        720 
DLLDIANGHM VCEEGDKLTY SKYGRFCHEV KINYSPYVNY FTRVYWNRSY FVYKINTVIS 


FQS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
Tissue: Tongue.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon endothelium and Uterus.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Eye.
[5]"Duplication and relocation of the functional DPY19L2 gene within low copy repeats."
Carson A.R., Cheung J., Scherer S.W.
BMC Genomics 7:45-45(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK123618 mRNA. Translation: BAC85664.1. Different initiation.
AK123682 mRNA. Translation: BAC85675.1.
BX538048 mRNA. Translation: CAD97987.1.
BX538174 mRNA. Translation: CAD98049.1.
CH471060 Genomic DNA. Translation: EAW91723.1.
BC110870 mRNA. Translation: AAI10871.1.
BC126193 mRNA. Translation: AAI26194.1.
BC130576 mRNA. Translation: AAI30577.1.
CCDSCCDS34924.1.
RefSeqNP_861452.2. NM_181787.2.
UniGeneHs.567828.

3D structure databases

ProteinModelPortalQ7Z388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130313. 4 interactions.
IntActQ7Z388. 1 interaction.
STRING9606.ENSP00000389630.

PTM databases

PhosphoSiteQ7Z388.

Polymorphism databases

DMDM74713335.

Proteomic databases

MaxQBQ7Z388.
PaxDbQ7Z388.
PRIDEQ7Z388.

Protocols and materials databases

DNASU286148.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000414645; ENSP00000389630; ENSG00000156162.
GeneID286148.
KEGGhsa:286148.
UCSCuc003ygx.2. human.

Organism-specific databases

CTD286148.
GeneCardsGC08P095802.
HGNCHGNC:27829. DPY19L4.
HPAHPA024780.
MIM613895. gene.
neXtProtNX_Q7Z388.
PharmGKBPA142671955.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236656.
HOGENOMHOG000007319.
HOVERGENHBG107792.
InParanoidQ7Z388.
OMAASTYTFM.
OrthoDBEOG7N37BZ.
PhylomeDBQ7Z388.
TreeFamTF313376.

Gene expression databases

ArrayExpressQ7Z388.
BgeeQ7Z388.
CleanExHS_DPY19L4.
GenevestigatorQ7Z388.

Family and domain databases

InterProIPR018732. Dpy-19.
[Graphical view]
PfamPF10034. Dpy19. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDPY19L4. human.
GenomeRNAi286148.
NextBio96034.
PROQ7Z388.
SOURCESearch...

Entry information

Entry nameD19L4_HUMAN
AccessionPrimary (citable) accession number: Q7Z388
Secondary accession number(s): Q6ZW32, Q6ZW42, Q7Z329
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM