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Q14157

- UBP2L_HUMAN

UniProt

Q14157 - UBP2L_HUMAN

Protein

Ubiquitin-associated protein 2-like

Gene

UBAP2L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (27 Jun 2006)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. binding of sperm to zona pellucida Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-associated protein 2-like
    Alternative name(s):
    Protein NICE-4
    Gene namesi
    Name:UBAP2L
    Synonyms:KIAA0144, NICE4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:29877. UBAP2L.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134883839.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10871087Ubiquitin-associated protein 2-likePRO_0000211020Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei416 – 4161Phosphoserine6 Publications
    Modified residuei425 – 4251Phosphothreonine1 Publication
    Modified residuei439 – 4391Phosphoserine3 Publications
    Modified residuei454 – 4541Phosphoserine4 Publications
    Modified residuei467 – 4671Phosphoserine4 Publications
    Modified residuei470 – 4701Phosphoserine1 Publication
    Modified residuei471 – 4711Phosphoserine1 Publication
    Modified residuei477 – 4771Phosphoserine3 Publications
    Modified residuei605 – 6051Phosphoserine1 Publication
    Modified residuei608 – 6081Phosphoserine1 Publication
    Modified residuei609 – 6091Phosphoserine3 Publications
    Modified residuei852 – 8521Phosphoserine1 Publication
    Modified residuei859 – 8591Phosphoserine2 Publications

    Post-translational modificationi

    Acetylated.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14157.
    PaxDbiQ14157.
    PRIDEiQ14157.

    PTM databases

    PhosphoSiteiQ14157.

    Miscellaneous databases

    PMAP-CutDBQ14157.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ14157.
    BgeeiQ14157.
    CleanExiHS_UBAP2L.
    GenevestigatoriQ14157.

    Organism-specific databases

    HPAiHPA035068.

    Interactioni

    Protein-protein interaction databases

    BioGridi115227. 34 interactions.
    IntActiQ14157. 7 interactions.
    MINTiMINT-1032368.
    STRINGi9606.ENSP00000355343.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14157.
    SMRiQ14157. Positions 19-111.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini49 – 8941UBAPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 UBA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000138192.
    HOVERGENiHBG058387.
    InParanoidiQ14157.
    OMAiPLYEQRS.
    OrthoDBiEOG7Z95KJ.
    PhylomeDBiQ14157.
    TreeFamiTF328468.

    Family and domain databases

    InterProiIPR022166. DUF3697_Uba2.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    [Graphical view]
    PfamiPF12478. DUF3697. 1 hit.
    [Graphical view]
    SMARTiSM00165. UBA. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    PROSITEiPS50030. UBA. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14157-2) [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

    MMTSVGTNRA RGNWEQPQNQ NQTQHKQRPQ ATAEQIRLAQ MISDHNDADF     50
    EEKVKQLIDI TGKNQDECVI ALHDCNGDVN RAINVLLEGN PDTHSWEMVG 100
    KKKGVSGQKD GGQTESNEEG KENRDRDRDY SRRRGGPPRR GRGASRGREF 150
    RGQENGLDGT KSGGPSGRGT ERGRRGRGRG RGGSGRRGGR FSAQGMGTFN 200
    PADYAEPANT DDNYGNSSGN TWNNTGHFEP DDGTSAWRTA TEEWGTEDWN 250
    EDLSETKIFT ASNVSSVPLP AENVTITAGQ RIDLAVLLGK TPSTMENDSS 300
    NLDPSQAPSL AQPLVFSNSK QTAISQPASG NTFSHHSMVS MLGKGFGDVG 350
    EAKGGSTTGS QFLEQFKTAQ ALAQLAAQHS QSGSTTTSSW DMGSTTQSPS 400
    LVQYDLKNPS DSAVHSPFTK RQAFTPSSTM MEVFLQEKSP AVATSTAAPP 450
    PPSSPLPSKS TSAPQMSPGS SDNQSSSPQP AQQKLKQQKK KASLTSKIPA 500
    LAVEMPGSAD ISGLNLQFGA LQFGSEPVLS DYESTPTTSA SSSQAPSSLY 550
    TSTASESSST ISSNQSQESG YQSGPIQSTT YTSQNNAQGP LYEQRSTQTR 600
    RYPSSISSSP QKDLTQAKNG FSSVQATQLQ TTQSVEGATG SAVKSDSPST 650
    SSIPPLNETV SAASLLTTTN QHSSSLGGLS HSEEIPNTTT TQHSSTLSTQ 700
    QNTLSSSTSS GRTSTSTLLH TSVESEANLH SSSSTFSTTS STVSAPPPVV 750
    SVSSSLNSGS SLGLSLGSNS TVTASTRSSV ATTSGKAPPN LPPGVPPLLP 800
    NPYIMAPGLL HAYPPQVYGY DDLQMLQTRF PLDYYSIPFP TPTTPLTGRD 850
    GSLASNPYSG DLTKFGRGDA SSPAPATTLA QPQQNQTQTH HTTQQTFLNP 900
    ALPPGYSYTS LPYYTGVPGL PSTFQYGPAV FPVAPTSSKQ HGVNVSVNAS 950
    ATPFQQPSGY GSHGYNTGVS VTSSNTGVPD ISGSVYSKTQ QSFEKQGFHS 1000
    GTPAASFNLP SALGSGGPIN PATAAAYPPA PFMHILTPHQ QPHSQILHHH 1050
    LQQDGQTGSG QRSQTSSIPQ KPQTNKSAYN SYSWGAN 1087
    Length:1,087
    Mass (Da):114,535
    Last modified:June 27, 2006 - v2
    Checksum:iFED18847387AA1F5
    GO
    Isoform 2 (identifier: Q14157-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         969-1087: VSVTSSNTGV...AYNSYSWGAN → RKYPPPYKHFWTAES

    Note: Contains a N6-acetyllysine at position 976.

    Show »
    Length:983
    Mass (Da):103,930
    Checksum:i50579CFA293EEA68
    GO
    Isoform 3 (identifier: Q14157-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1057-1087: TGSGQRSQTSSIPQKPQTNKSAYNSYSWGAN → DILNFVDDQLGE

    Show »
    Length:1,068
    Mass (Da):112,580
    Checksum:i86703186E7D5FC73
    GO
    Isoform 4 (identifier: Q14157-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         143-150: GASRGREF → V
         969-1087: VSVTSSNTGV...AYNSYSWGAN → RKYPPPYKHFWTAES

    Note: No experimental confirmation available. Contains a N6-acetyllysine at position 969.

    Show »
    Length:976
    Mass (Da):103,168
    Checksum:iBF593BEA38DF9579
    GO
    Isoform 5 (identifier: Q14157-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1055-1055: G → GQLPYLQMILCCQRQQEE

    Show »
    Length:1,104
    Mass (Da):116,640
    Checksum:iA361FC99B94E0988
    GO

    Sequence cautioni

    The sequence CAB65100.2 differs from that shown. Reason: Frameshift at position 1085.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 911P → S in BAG64560. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti482 – 4821Q → H.
    Corresponds to variant rs17849745 [ dbSNP | Ensembl ].
    VAR_026829

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei143 – 1508GASRGREF → V in isoform 4. 1 PublicationVSP_038235
    Alternative sequencei969 – 1087119VSVTS…SWGAN → RKYPPPYKHFWTAES in isoform 2 and isoform 4. 2 PublicationsVSP_019417Add
    BLAST
    Alternative sequencei1055 – 10551G → GQLPYLQMILCCQRQQEE in isoform 5. 1 PublicationVSP_042167
    Alternative sequencei1057 – 108731TGSGQ…SWGAN → DILNFVDDQLGE in isoform 3. 1 PublicationVSP_021728Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63478 mRNA. Translation: BAA09765.1.
    AK303533 mRNA. Translation: BAG64560.1.
    AL590431 Genomic DNA. Translation: CAH71283.1.
    AL590431 Genomic DNA. Translation: CAH71284.1.
    AL590431 Genomic DNA. Translation: CAH71285.1.
    BC003170 mRNA. Translation: AAH03170.1.
    AJ243668 mRNA. Translation: CAB65099.1.
    AJ243670 mRNA. Translation: CAB65101.2.
    AJ243669 mRNA. Translation: CAB65100.2. Frameshift.
    CCDSiCCDS1063.1. [Q14157-2]
    CCDS44229.1. [Q14157-1]
    RefSeqiNP_001120792.1. NM_001127320.2. [Q14157-1]
    NP_001274744.1. NM_001287815.1. [Q14157-4]
    NP_001274745.1. NM_001287816.1.
    NP_055662.3. NM_014847.3. [Q14157-2]
    XP_005245731.1. XM_005245674.1. [Q14157-1]
    UniGeneiHs.490551.

    Genome annotation databases

    EnsembliENST00000343815; ENSP00000345308; ENSG00000143569. [Q14157-1]
    ENST00000361546; ENSP00000355343; ENSG00000143569. [Q14157-2]
    ENST00000428931; ENSP00000389445; ENSG00000143569. [Q14157-2]
    GeneIDi9898.
    KEGGihsa:9898.
    UCSCiuc001fep.4. human. [Q14157-2]
    uc009wot.3. human. [Q14157-1]
    uc010pek.2. human. [Q14157-4]

    Polymorphism databases

    DMDMi109940042.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63478 mRNA. Translation: BAA09765.1 .
    AK303533 mRNA. Translation: BAG64560.1 .
    AL590431 Genomic DNA. Translation: CAH71283.1 .
    AL590431 Genomic DNA. Translation: CAH71284.1 .
    AL590431 Genomic DNA. Translation: CAH71285.1 .
    BC003170 mRNA. Translation: AAH03170.1 .
    AJ243668 mRNA. Translation: CAB65099.1 .
    AJ243670 mRNA. Translation: CAB65101.2 .
    AJ243669 mRNA. Translation: CAB65100.2 . Frameshift.
    CCDSi CCDS1063.1. [Q14157-2 ]
    CCDS44229.1. [Q14157-1 ]
    RefSeqi NP_001120792.1. NM_001127320.2. [Q14157-1 ]
    NP_001274744.1. NM_001287815.1. [Q14157-4 ]
    NP_001274745.1. NM_001287816.1.
    NP_055662.3. NM_014847.3. [Q14157-2 ]
    XP_005245731.1. XM_005245674.1. [Q14157-1 ]
    UniGenei Hs.490551.

    3D structure databases

    ProteinModelPortali Q14157.
    SMRi Q14157. Positions 19-111.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115227. 34 interactions.
    IntActi Q14157. 7 interactions.
    MINTi MINT-1032368.
    STRINGi 9606.ENSP00000355343.

    PTM databases

    PhosphoSitei Q14157.

    Polymorphism databases

    DMDMi 109940042.

    Proteomic databases

    MaxQBi Q14157.
    PaxDbi Q14157.
    PRIDEi Q14157.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343815 ; ENSP00000345308 ; ENSG00000143569 . [Q14157-1 ]
    ENST00000361546 ; ENSP00000355343 ; ENSG00000143569 . [Q14157-2 ]
    ENST00000428931 ; ENSP00000389445 ; ENSG00000143569 . [Q14157-2 ]
    GeneIDi 9898.
    KEGGi hsa:9898.
    UCSCi uc001fep.4. human. [Q14157-2 ]
    uc009wot.3. human. [Q14157-1 ]
    uc010pek.2. human. [Q14157-4 ]

    Organism-specific databases

    CTDi 9898.
    GeneCardsi GC01P154192.
    H-InvDB HIX0001103.
    HGNCi HGNC:29877. UBAP2L.
    HPAi HPA035068.
    neXtProti NX_Q14157.
    PharmGKBi PA134883839.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000138192.
    HOVERGENi HBG058387.
    InParanoidi Q14157.
    OMAi PLYEQRS.
    OrthoDBi EOG7Z95KJ.
    PhylomeDBi Q14157.
    TreeFami TF328468.

    Miscellaneous databases

    ChiTaRSi UBAP2L. human.
    GeneWikii UBAP2L.
    GenomeRNAii 9898.
    NextBioi 37319.
    PMAP-CutDB Q14157.
    PROi Q14157.

    Gene expression databases

    ArrayExpressi Q14157.
    Bgeei Q14157.
    CleanExi HS_UBAP2L.
    Genevestigatori Q14157.

    Family and domain databases

    InterProi IPR022166. DUF3697_Uba2.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    [Graphical view ]
    Pfami PF12478. DUF3697. 1 hit.
    [Graphical view ]
    SMARTi SM00165. UBA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    PROSITEi PS50030. UBA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Bone marrow.
    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.
      , 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 4).
      Tissue: Thymus.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Skin.
    5. "Identification of human epidermal differentiation complex (EDC)-encoded genes by subtractive hybridization of entire YACs to a gridded keratinocyte cDNA library."
      Marenholz I., Zirra M., Fischer D.F., Backendorf C., Ziegler A., Mischke D.
      Genome Res. 11:341-355(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-137 (ISOFORMS 1/2/3), NUCLEOTIDE SEQUENCE [MRNA] OF 671-1087 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 760-1087 (ISOFORM 5), TISSUE SPECIFICITY.
      Tissue: Keratinocyte.
    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 SER-416, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. "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-416; SER-439 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-439; SER-454; SER-467; SER-471; SER-477; SER-605; SER-608; SER-609; SER-852 AND SER-859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-454; SER-470; SER-477 AND SER-859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-976 (ISOFORM 2), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-969 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-416; THR-425; SER-439; SER-454 AND SER-609, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-416; SER-467; SER-477 AND SER-609, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBP2L_HUMAN
    AccessioniPrimary (citable) accession number: Q14157
    Secondary accession number(s): B4E0U8
    , Q5VU75, Q5VU76, Q9BTU3, Q9UGL2, Q9UGL3, Q9UGL4, Q9UGL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: June 27, 2006
    Last modified: October 1, 2014
    This is version 123 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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