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Q14157 (UBP2L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-associated protein 2-like
Alternative name(s):
Protein NICE-4
Gene names
Name:UBAP2L
Synonyms:KIAA0144, NICE4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1087 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Tissue specificity

Ubiquitous. Ref.5

Post-translational modification

Acetylated.

Sequence similarities

Contains 1 UBA domain.

Sequence caution

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

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14157-2)

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.
Isoform 2 (identifier: Q14157-1)

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.
Isoform 3 (identifier: Q14157-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1057-1087: TGSGQRSQTSSIPQKPQTNKSAYNSYSWGAN → DILNFVDDQLGE
Isoform 4 (identifier: Q14157-4)

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.
Isoform 5 (identifier: Q14157-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10871087Ubiquitin-associated protein 2-like
PRO_0000211020

Regions

Domain49 – 8941UBA

Amino acid modifications

Modified residue11N-acetylmethionine Ref.14 Ref.21
Modified residue4161Phosphoserine Ref.6 Ref.10 Ref.12 Ref.13 Ref.18 Ref.20
Modified residue4251Phosphothreonine Ref.18
Modified residue4391Phosphoserine Ref.12 Ref.13 Ref.18
Modified residue4541Phosphoserine Ref.9 Ref.13 Ref.16 Ref.18
Modified residue4671Phosphoserine Ref.12 Ref.13 Ref.15 Ref.20
Modified residue4701Phosphoserine Ref.16
Modified residue4711Phosphoserine Ref.13
Modified residue4771Phosphoserine Ref.13 Ref.16 Ref.20
Modified residue6051Phosphoserine Ref.13
Modified residue6081Phosphoserine Ref.13
Modified residue6091Phosphoserine Ref.13 Ref.18 Ref.20
Modified residue8521Phosphoserine Ref.13
Modified residue8591Phosphoserine Ref.13 Ref.16

Natural variations

Alternative sequence143 – 1508GASRGREF → V in isoform 4.
VSP_038235
Alternative sequence969 – 1087119VSVTS…SWGAN → RKYPPPYKHFWTAES in isoform 2 and isoform 4.
VSP_019417
Alternative sequence10551G → GQLPYLQMILCCQRQQEE in isoform 5.
VSP_042167
Alternative sequence1057 – 108731TGSGQ…SWGAN → DILNFVDDQLGE in isoform 3.
VSP_021728
Natural variant4821Q → H.
Corresponds to variant rs17849745 [ dbSNP | Ensembl ].
VAR_026829

Experimental info

Sequence conflict911P → S in BAG64560. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: FED18847387AA1F5

FASTA1,087114,535
        10         20         30         40         50         60 
MMTSVGTNRA RGNWEQPQNQ NQTQHKQRPQ ATAEQIRLAQ MISDHNDADF EEKVKQLIDI 

        70         80         90        100        110        120 
TGKNQDECVI ALHDCNGDVN RAINVLLEGN PDTHSWEMVG KKKGVSGQKD GGQTESNEEG 

       130        140        150        160        170        180 
KENRDRDRDY SRRRGGPPRR GRGASRGREF RGQENGLDGT KSGGPSGRGT ERGRRGRGRG 

       190        200        210        220        230        240 
RGGSGRRGGR FSAQGMGTFN PADYAEPANT DDNYGNSSGN TWNNTGHFEP DDGTSAWRTA 

       250        260        270        280        290        300 
TEEWGTEDWN EDLSETKIFT ASNVSSVPLP AENVTITAGQ RIDLAVLLGK TPSTMENDSS 

       310        320        330        340        350        360 
NLDPSQAPSL AQPLVFSNSK QTAISQPASG NTFSHHSMVS MLGKGFGDVG EAKGGSTTGS 

       370        380        390        400        410        420 
QFLEQFKTAQ ALAQLAAQHS QSGSTTTSSW DMGSTTQSPS LVQYDLKNPS DSAVHSPFTK 

       430        440        450        460        470        480 
RQAFTPSSTM MEVFLQEKSP AVATSTAAPP PPSSPLPSKS TSAPQMSPGS SDNQSSSPQP 

       490        500        510        520        530        540 
AQQKLKQQKK KASLTSKIPA LAVEMPGSAD ISGLNLQFGA LQFGSEPVLS DYESTPTTSA 

       550        560        570        580        590        600 
SSSQAPSSLY TSTASESSST ISSNQSQESG YQSGPIQSTT YTSQNNAQGP LYEQRSTQTR 

       610        620        630        640        650        660 
RYPSSISSSP QKDLTQAKNG FSSVQATQLQ TTQSVEGATG SAVKSDSPST SSIPPLNETV 

       670        680        690        700        710        720 
SAASLLTTTN QHSSSLGGLS HSEEIPNTTT TQHSSTLSTQ QNTLSSSTSS GRTSTSTLLH 

       730        740        750        760        770        780 
TSVESEANLH SSSSTFSTTS STVSAPPPVV SVSSSLNSGS SLGLSLGSNS TVTASTRSSV 

       790        800        810        820        830        840 
ATTSGKAPPN LPPGVPPLLP NPYIMAPGLL HAYPPQVYGY DDLQMLQTRF PLDYYSIPFP 

       850        860        870        880        890        900 
TPTTPLTGRD GSLASNPYSG DLTKFGRGDA SSPAPATTLA QPQQNQTQTH HTTQQTFLNP 

       910        920        930        940        950        960 
ALPPGYSYTS LPYYTGVPGL PSTFQYGPAV FPVAPTSSKQ HGVNVSVNAS ATPFQQPSGY 

       970        980        990       1000       1010       1020 
GSHGYNTGVS VTSSNTGVPD ISGSVYSKTQ QSFEKQGFHS GTPAASFNLP SALGSGGPIN 

      1030       1040       1050       1060       1070       1080 
PATAAAYPPA PFMHILTPHQ QPHSQILHHH LQQDGQTGSG QRSQTSSIPQ KPQTNKSAYN 


SYSWGAN 

« Hide

Isoform 2 [UniParc].

Checksum: 50579CFA293EEA68
Show »

FASTA983103,930
Isoform 3 [UniParc].

Checksum: 86703186E7D5FC73
Show »

FASTA1,068112,580
Isoform 4 [UniParc].

Checksum: BF593BEA38DF9579
Show »

FASTA976103,168
Isoform 5 [UniParc].

Checksum: A361FC99B94E0988
Show »

FASTA1,104116,640

References

« Hide 'large scale' references
[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. 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] (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. expand/collapse author list , 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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1063.1. [Q14157-2]
CCDS44229.1. [Q14157-1]
RefSeqNP_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]
UniGeneHs.490551.

3D structure databases

ProteinModelPortalQ14157.
SMRQ14157. Positions 19-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115227. 36 interactions.
IntActQ14157. 7 interactions.
MINTMINT-1032368.
STRING9606.ENSP00000355343.

PTM databases

PhosphoSiteQ14157.

Polymorphism databases

DMDM109940042.

Proteomic databases

MaxQBQ14157.
PaxDbQ14157.
PRIDEQ14157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343815; ENSP00000345308; ENSG00000143569. [Q14157-1]
ENST00000361546; ENSP00000355343; ENSG00000143569. [Q14157-2]
ENST00000428931; ENSP00000389445; ENSG00000143569. [Q14157-2]
GeneID9898.
KEGGhsa:9898.
UCSCuc001fep.4. human. [Q14157-2]
uc009wot.3. human. [Q14157-1]
uc010pek.2. human. [Q14157-4]

Organism-specific databases

CTD9898.
GeneCardsGC01P154192.
H-InvDBHIX0001103.
HGNCHGNC:29877. UBAP2L.
HPAHPA035068.
neXtProtNX_Q14157.
PharmGKBPA134883839.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000138192.
HOVERGENHBG058387.
InParanoidQ14157.
OMAPLYEQRS.
OrthoDBEOG7Z95KJ.
PhylomeDBQ14157.
TreeFamTF328468.

Gene expression databases

ArrayExpressQ14157.
BgeeQ14157.
CleanExHS_UBAP2L.
GenevestigatorQ14157.

Family and domain databases

InterProIPR022166. DUF3697_Uba2.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PfamPF12478. DUF3697. 1 hit.
[Graphical view]
SMARTSM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS50030. UBA. 1 hit.
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Other

ChiTaRSUBAP2L. human.
GeneWikiUBAP2L.
GenomeRNAi9898.
NextBio37319.
PMAP-CutDBQ14157.
PROQ14157.

Entry information

Entry nameUBP2L_HUMAN
AccessionPrimary (citable) accession number: Q14157
Secondary accession number(s): B4E0U8 expand/collapse secondary AC list , Q5VU75, Q5VU76, Q9BTU3, Q9UGL2, Q9UGL3, Q9UGL4, Q9UGL5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 27, 2006
Last modified: July 9, 2014
This is version 121 of the entry and version 2 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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM