P49750 (YLPM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: YLP motif-containing protein 1 Alternative name(s): Nuclear protein ZAP3 ZAP113 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1951 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Plays a role in the reduction of telomerase activity during differentiation of embryonic stem cells by binding to the core promoter of TERT and controlling its down-regulation By similarity. |
| Subunit structure | Interacts with PPP1CA and NCOA5. Forms a complex with ILF2, ILF3, KHDRBS1, RBMX, NCOA5 and PPP1CA By similarity. |
| Subcellular location | Nucleus. Nucleus speckle By similarity. Note: Migrates to nucleolar caps upon blockage of transcription. Ref.7 |
| Tissue specificity | Expressed in neuronal, neuroblastoma and embryonic kidney cell lines (at protein level). Ref.7 |
| Sequence caution | The sequence AAC42008.1 differs from that shown. Reason: Frameshift at position 1723. The sequence AAF61275.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing |
| Molecular function | Repressor |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | |||||||||
| Isoform 1 (identifier: P49750-1) 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. | |||||||||
| Note: No experimental confirmation available. | |||||||||
| Isoform 3 (identifier: P49750-3) The sequence of this isoform differs from the canonical sequence as follows: 1843-1862: GYIPKSKWEMDTSEAKLDKL → VGDRPTTLNSVSLLKFLKKV 1863-1951: Missing. | |||||||||
Sequence annotation (Features) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
| Sequence conflict | 1861 | 1 | K → E in AAC42008. Ref.3 | ||||||
| Isoform 4 (identifier: P49750-4) The sequence of this isoform differs from the canonical sequence as follows: 431-432: AT → TMSVDMQLRH...VMPLPPLSSA | |||||||||
Sequence annotation (Features) | |||||||||
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
| Sequence conflict | 524 | 1 | S → P in AK095760. Ref.2 | ||||||
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1951 | 1951 | YLP motif-containing protein 1 | PRO_0000066298 | |||||
Regions | |||||||||
| Region | 1901 – 1908 | 8 | Involved in interaction with PPP1CA By similarity | ||||||
| Compositional bias | 15 – 205 | 191 | Pro-rich | ||||||
| Compositional bias | 382 – 430 | 49 | Gln-rich | ||||||
| Compositional bias | 807 – 1209 | 403 | Arg-rich | ||||||
| Compositional bias | 1488 – 1577 | 90 | Arg-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 634 | 1 | Phosphoserine Ref.5 Ref.8 Ref.9 Ref.10 Ref.11 | ||||||
| Modified residue | 924 | 1 | Phosphoserine Ref.6 | ||||||
Natural variations | |||||||||
| Alternative sequence | 431 – 432 | 2 | AT → TMSVDMQLRHYEMQQQQFQH LYQEWEREFQLWEEQLHSYP HKDQLQEYEKQWKTWQGHMK ATQSYLQEKVNSFQNMKNQY MGNMSMPPPFVPYSQMPPPL PTMPPPVLPPSLPPPVMPPA LPATVPPPGMPPPVMPPSLP TSVPPPGMPPSLSSAGPPPV LPPPSLSSAGPPPVLPPPSL SSTAPPPVMPLPPLSSA in isoform 4. | VSP_040649 | |||||
| Alternative sequence | 1843 – 1862 | 20 | GYIPK…KLDKL → VGDRPTTLNSVSLLKFLKKV in isoform 3. | VSP_012538 | |||||
| Alternative sequence | 1863 – 1951 | 89 | Missing in isoform 3. | VSP_012539 | |||||
Experimental info | |||||||||
| Sequence conflict | 421 | 1 | Q → R in AK095760. Ref.2 | ||||||
| Sequence conflict | 621 | 1 | P → S in AAC42006. Ref.3 | ||||||
| Sequence conflict | 1404 | 1 | T → I in AAC42008. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. Weissenbach J.Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-433 (ISOFORM 4). |
| [3] | "Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease." Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F., Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L. St George-Hyslop P.H.Nature 375:754-760(1995) [PubMed: 7596406] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 539-847 AND 1397-1951 (ISOFORM 3). Tissue: Brain. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1566-1951 (ISOFORM 1). Tissue: Skin. |
| [5] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [7] | "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G." Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G. Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed: 17890166] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| [8] | "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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [9] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [11] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [12] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AC007956 Genomic DNA. Translation: AAF61275.1. Sequence problems. AK095760 mRNA. No translation available. L40403 mRNA. Translation: AAC42008.1. Frameshift. L40400 mRNA. Translation: AAC42006.1. BC007792 mRNA. Translation: AAH07792.1. |
| IPI | IPI00165434. IPI00514265. IPI00940874. |
| RefSeq | NP_062535.2. NM_019589.2. |
| UniGene | Hs.531111. |
3D structure databases | |
| ProteinModelPortal | P49750. |
| SMR | P49750. Positions 1637-1776. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P49750. 11 interactions. |
| STRING | P49750. |
PTM databases | |
| PhosphoSite | P49750. |
Polymorphism databases | |
| DMDM | 57015374. |
Proteomic databases | |
| PRIDE | P49750. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000423680; ENSP00000409619; ENSG00000119596. |
| GeneID | 56252. |
| KEGG | hsa:56252. |
| UCSC | uc001xqj.2. human. |
Organism-specific databases | |
| CTD | 56252. |
| GeneCards | GC14P075230. |
| HGNC | HGNC:17798. YLPM1. |
| neXtProt | NX_P49750. |
| PharmGKB | PA134962086. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG10331. |
| GeneTree | ENSGT00440000039837. |
| HOVERGEN | HBG079363. |
| InParanoid | P49750. |
| OMA | QSYLAPT. |
Gene expression databases | |
| ArrayExpress | P49750. |
| Bgee | P49750. |
| CleanEx | HS_YLPM1. |
| Genevestigator | P49750. |
| GermOnline | ENSG00000119596. Homo sapiens. |
Family and domain databases | |
| ProtoNet | Search... |
Entry information
| Entry name | YLPM1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P49750 Secondary accession number(s): P49752, Q96I64, Q9P1V7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| Human chromosome 14 Human chromosome 14: entries, gene names and cross-references to MIM |

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