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Q14157

- UBP2L_HUMAN

UniProt

Q14157 - UBP2L_HUMAN

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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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. binding of sperm to zona pellucida Source: UniProtKB
Complete GO annotation...

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

BgeeiQ14157.
CleanExiHS_UBAP2L.
ExpressionAtlasiQ14157. baseline and differential.
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.
GeneTreeiENSGT00390000003453.
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

        10         20         30         40         50
MMTSVGTNRA RGNWEQPQNQ NQTQHKQRPQ ATAEQIRLAQ MISDHNDADF
60 70 80 90 100
EEKVKQLIDI TGKNQDECVI ALHDCNGDVN RAINVLLEGN PDTHSWEMVG
110 120 130 140 150
KKKGVSGQKD GGQTESNEEG KENRDRDRDY SRRRGGPPRR GRGASRGREF
160 170 180 190 200
RGQENGLDGT KSGGPSGRGT ERGRRGRGRG RGGSGRRGGR FSAQGMGTFN
210 220 230 240 250
PADYAEPANT DDNYGNSSGN TWNNTGHFEP DDGTSAWRTA TEEWGTEDWN
260 270 280 290 300
EDLSETKIFT ASNVSSVPLP AENVTITAGQ RIDLAVLLGK TPSTMENDSS
310 320 330 340 350
NLDPSQAPSL AQPLVFSNSK QTAISQPASG NTFSHHSMVS MLGKGFGDVG
360 370 380 390 400
EAKGGSTTGS QFLEQFKTAQ ALAQLAAQHS QSGSTTTSSW DMGSTTQSPS
410 420 430 440 450
LVQYDLKNPS DSAVHSPFTK RQAFTPSSTM MEVFLQEKSP AVATSTAAPP
460 470 480 490 500
PPSSPLPSKS TSAPQMSPGS SDNQSSSPQP AQQKLKQQKK KASLTSKIPA
510 520 530 540 550
LAVEMPGSAD ISGLNLQFGA LQFGSEPVLS DYESTPTTSA SSSQAPSSLY
560 570 580 590 600
TSTASESSST ISSNQSQESG YQSGPIQSTT YTSQNNAQGP LYEQRSTQTR
610 620 630 640 650
RYPSSISSSP QKDLTQAKNG FSSVQATQLQ TTQSVEGATG SAVKSDSPST
660 670 680 690 700
SSIPPLNETV SAASLLTTTN QHSSSLGGLS HSEEIPNTTT TQHSSTLSTQ
710 720 730 740 750
QNTLSSSTSS GRTSTSTLLH TSVESEANLH SSSSTFSTTS STVSAPPPVV
760 770 780 790 800
SVSSSLNSGS SLGLSLGSNS TVTASTRSSV ATTSGKAPPN LPPGVPPLLP
810 820 830 840 850
NPYIMAPGLL HAYPPQVYGY DDLQMLQTRF PLDYYSIPFP TPTTPLTGRD
860 870 880 890 900
GSLASNPYSG DLTKFGRGDA SSPAPATTLA QPQQNQTQTH HTTQQTFLNP
910 920 930 940 950
ALPPGYSYTS LPYYTGVPGL PSTFQYGPAV FPVAPTSSKQ HGVNVSVNAS
960 970 980 990 1000
ATPFQQPSGY GSHGYNTGVS VTSSNTGVPD ISGSVYSKTQ QSFEKQGFHS
1010 1020 1030 1040 1050
GTPAASFNLP SALGSGGPIN PATAAAYPPA PFMHILTPHQ QPHSQILHHH
1060 1070 1080
LQQDGQTGSG QRSQTSSIPQ KPQTNKSAYN SYSWGAN
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. Curated

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:
EMBLi
GenBanki
DDBJi
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]
CCDS72925.1. [Q14157-4]
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]
ENST00000613315; ENSP00000478447; ENSG00000143569. [Q14157-4]
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:
EMBLi
GenBanki
DDBJi
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 ]
CCDS72925.1. [Q14157-4 ]
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 ]
ENST00000613315 ; ENSP00000478447 ; ENSG00000143569 . [Q14157-4 ]
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.
GeneTreei ENSGT00390000003453.
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

Bgeei Q14157.
CleanExi HS_UBAP2L.
ExpressionAtlasi Q14157. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 124 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