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Q9UBC2

- EP15R_HUMAN

UniProt

Q9UBC2 - EP15R_HUMAN

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Protein

Epidermal growth factor receptor substrate 15-like 1

Gene

EPS15L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi172 – 18413PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. epidermal growth factor receptor signaling pathway Source: Reactome
  3. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_12484. EGFR downregulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermal growth factor receptor substrate 15-like 1
Alternative name(s):
Eps15-related protein
Short name:
Eps15R
Gene namesi
Name:EPS15L1
Synonyms:EPS15R
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:24634. EPS15L1.

Subcellular locationi

Cell membrane By similarity; Peripheral membrane protein By similarity. Nucleus By similarity. Membranecoated pit By similarity
Note: Localized to plasma membrane coated pits.By similarity

GO - Cellular componenti

  1. clathrin coat of coated pit Source: Ensembl
  2. membrane Source: UniProtKB
  3. nucleus Source: UniProtKB-KW
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134906266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 864863Epidermal growth factor receptor substrate 15-like 1PRO_0000146118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei74 – 741PhosphotyrosineBy similarity
Modified residuei108 – 1081PhosphoserineBy similarity
Modified residuei229 – 2291Phosphoserine1 Publication
Modified residuei244 – 2441Phosphoserine1 Publication
Modified residuei255 – 2551Phosphoserine4 Publications
Modified residuei560 – 5601Phosphoserine1 Publication
Modified residuei564 – 5641PhosphotyrosineBy similarity
Modified residuei577 – 5771Phosphothreonine1 Publication
Modified residuei797 – 7971Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues by EGFR.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UBC2.
PaxDbiQ9UBC2.
PRIDEiQ9UBC2.

Expressioni

Gene expression databases

BgeeiQ9UBC2.
CleanExiHS_EPS15L1.
ExpressionAtlasiQ9UBC2. baseline and differential.
GenevestigatoriQ9UBC2.

Organism-specific databases

HPAiHPA019237.

Interactioni

Subunit structurei

Interacts with EPS15, AGFG1/HRB and AGFG2/HRBL. Associates with the clathrin-associated adapter protein complex 2 (AP-2) By similarity. Interacts with FCHO1. Interacts with FCHO2. Interacts (via EH domains) with DAB2.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRKCDBPQ969G52EBI-2556746,EBI-3893101

Protein-protein interaction databases

BioGridi121840. 19 interactions.
IntActiQ9UBC2. 12 interactions.
MINTiMINT-1538779.
STRINGi9606.ENSP00000248070.

Structurei

3D structure databases

ProteinModelPortaliQ9UBC2.
SMRiQ9UBC2. Positions 11-105, 121-214, 269-362, 438-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 10490EH 1PROSITE-ProRule annotationAdd
BLAST
Domaini127 – 21589EH 2PROSITE-ProRule annotationAdd
BLAST
Domaini159 – 19436EF-handPROSITE-ProRule annotationAdd
BLAST
Domaini275 – 36591EH 3PROSITE-ProRule annotationAdd
BLAST
Repeati618 – 62031
Repeati640 – 64232
Repeati645 – 64733
Repeati650 – 65234
Repeati656 – 65835
Repeati661 – 66336
Repeati667 – 66937
Repeati685 – 68738
Repeati690 – 69239
Repeati709 – 711310
Repeati728 – 730311
Repeati754 – 756312
Repeati806 – 808313
Repeati812 – 814314
Repeati833 – 835315

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni15 – 368354Interaction with DAB2By similarityAdd
BLAST
Regioni618 – 83521815 X 3 AA repeats of D-P-FAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi750 – 81667Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 3 EH domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG301764.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000004804.
HOVERGENiHBG005591.
InParanoidiQ9UBC2.
OMAiMDDPFKN.
OrthoDBiEOG7JHM68.
PhylomeDBiQ9UBC2.
TreeFamiTF324293.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
SM00027. EH. 3 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 4 hits.
PS50031. EH. 3 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UBC2-1) [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
MAAPLIPLSQ QIPTGNSLYE SYYKQVDPAY TGRVGASEAA LFLKKSGLSD
60 70 80 90 100
IILGKIWDLA DPEGKGFLDK QGFYVALRLV ACAQSGHEVT LSNLNLSMPP
110 120 130 140 150
PKFHDTSSPL MVTPPSAEAH WAVRVEEKAK FDGIFESLLP INGLLSGDKV
160 170 180 190 200
KPVLMNSKLP LDVLGRVWDL SDIDKDGHLD RDEFAVAMHL VYRALEKEPV
210 220 230 240 250
PSALPPSLIP PSKRKKTVFP GAVPVLPASP PPKDSLRSTP SHGSVSSLNS
260 270 280 290 300
TGSLSPKHSL KQTQPTVNWV VPVADKMRFD EIFLKTDLDL DGYVSGQEVK
310 320 330 340 350
EIFMHSGLTQ NLLAHIWALA DTRQTGKLSK DQFALAMYFI QQKVSKGIDP
360 370 380 390 400
PQVLSPDMVP PSERGTPGPD SSGSLGSGEF TGVKELDDIS QEIAQLQREK
410 420 430 440 450
YSLEQDIREK EEAIRQKTSE VQELQNDLDR ETSSLQELEA QKQDAQDRLD
460 470 480 490 500
EMDQQKAKLR DMLSDVRQKC QDETQMISSL KTQIQSQESD LKSQEDDLNR
510 520 530 540 550
AKSELNRLQQ EETQLEQSIQ AGRVQLETII KSLKSTQDEI NQARSKLSQL
560 570 580 590 600
HESRQEAHRS LEQYDQVLDG AHGASLTDLA NLSEGVSLAE RGSFGAMDDP
610 620 630 640 650
FKNKALLFSN NTQELHPDPF QTEDPFKSDP FKGADPFKGD PFQNDPFAEQ
660 670 680 690 700
QTTSTDPFGG DPFKESDPFR GSATDDFFKK QTKNDPFTSD PFTKNPSLPS
710 720 730 740 750
KLDPFESSDP FSSSSVSSKG SDPFGTLDPF GSGSFNSAEG FADFSQMSKP
760 770 780 790 800
PPSGPFTSSL GGAGFSDDPF KSKQDTPALP PKKPAPPRPK PPSGKSTPVS
810 820 830 840 850
QLGSADFPEA PDPFQPLGAD SGDPFQSKKG FGDPFSGKDP FVPSSAAKPS
860
KASASGFADF TSVS
Length:864
Mass (Da):94,255
Last modified:May 1, 2000 - v1
Checksum:iF4126069F6E00387
GO
Isoform 2 (identifier: Q9UBC2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     863-864: VS → FGNEEQQLAWAKRESEKAEQERLARLRRQEQEDLELAIALSKADMPAA

Show »
Length:910
Mass (Da):99,606
Checksum:iF56CC554F539B5FE
GO
Isoform 3 (identifier: Q9UBC2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     750-864: PPPSGPFTSS...SGFADFTSVS → VKVHL

Show »
Length:754
Mass (Da):83,248
Checksum:i5FFC0740FA78FC8B
GO
Isoform 4 (identifier: Q9UBC2-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     598-601: DDPF → VKVE
     602-864: Missing.

Note: No experimental confirmation available.

Show »
Length:601
Mass (Da):66,479
Checksum:i9709A5D16D1E126A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti680 – 6801K → E in BAG59115. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei598 – 6014DDPF → VKVE in isoform 4. 1 PublicationVSP_046904
Alternative sequencei602 – 864263Missing in isoform 4. 1 PublicationVSP_046905Add
BLAST
Alternative sequencei750 – 864115PPPSG…FTSVS → VKVHL in isoform 3. 2 PublicationsVSP_045429Add
BLAST
Alternative sequencei863 – 8642VS → FGNEEQQLAWAKRESEKAEQ ERLARLRRQEQEDLELAIAL SKADMPAA in isoform 2. 1 PublicationVSP_042200

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF110265 mRNA. Translation: AAF21930.1.
AB015346 mRNA. Translation: BAA88118.1.
AK024166 mRNA. Translation: BAG51266.1.
AK296473 mRNA. Translation: BAG59115.1.
AC008764 Genomic DNA. No translation available.
AC020917 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84542.1.
BC131590 mRNA. Translation: AAI31591.1.
BC142716 mRNA. Translation: AAI42717.1.
CCDSiCCDS32944.1. [Q9UBC2-1]
CCDS58653.1. [Q9UBC2-3]
CCDS58654.1. [Q9UBC2-2]
CCDS59363.1. [Q9UBC2-4]
RefSeqiNP_001245303.1. NM_001258374.1. [Q9UBC2-2]
NP_001245304.1. NM_001258375.1. [Q9UBC2-3]
NP_001245305.1. NM_001258376.1. [Q9UBC2-4]
NP_067058.1. NM_021235.2. [Q9UBC2-1]
UniGeneiHs.654639.
Hs.744842.

Genome annotation databases

GeneIDi58513.
KEGGihsa:58513.
UCSCiuc002ndx.4. human. [Q9UBC2-2]
uc002ndz.2. human. [Q9UBC2-1]
uc002nea.2. human.
uc002nec.2. human.

Polymorphism databases

DMDMi61223942.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF110265 mRNA. Translation: AAF21930.1 .
AB015346 mRNA. Translation: BAA88118.1 .
AK024166 mRNA. Translation: BAG51266.1 .
AK296473 mRNA. Translation: BAG59115.1 .
AC008764 Genomic DNA. No translation available.
AC020917 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84542.1 .
BC131590 mRNA. Translation: AAI31591.1 .
BC142716 mRNA. Translation: AAI42717.1 .
CCDSi CCDS32944.1. [Q9UBC2-1 ]
CCDS58653.1. [Q9UBC2-3 ]
CCDS58654.1. [Q9UBC2-2 ]
CCDS59363.1. [Q9UBC2-4 ]
RefSeqi NP_001245303.1. NM_001258374.1. [Q9UBC2-2 ]
NP_001245304.1. NM_001258375.1. [Q9UBC2-3 ]
NP_001245305.1. NM_001258376.1. [Q9UBC2-4 ]
NP_067058.1. NM_021235.2. [Q9UBC2-1 ]
UniGenei Hs.654639.
Hs.744842.

3D structure databases

ProteinModelPortali Q9UBC2.
SMRi Q9UBC2. Positions 11-105, 121-214, 269-362, 438-499.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121840. 19 interactions.
IntActi Q9UBC2. 12 interactions.
MINTi MINT-1538779.
STRINGi 9606.ENSP00000248070.

Polymorphism databases

DMDMi 61223942.

Proteomic databases

MaxQBi Q9UBC2.
PaxDbi Q9UBC2.
PRIDEi Q9UBC2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 58513.
KEGGi hsa:58513.
UCSCi uc002ndx.4. human. [Q9UBC2-2 ]
uc002ndz.2. human. [Q9UBC2-1 ]
uc002nea.2. human.
uc002nec.2. human.

Organism-specific databases

CTDi 58513.
GeneCardsi GC19M016466.
HGNCi HGNC:24634. EPS15L1.
HPAi HPA019237.
neXtProti NX_Q9UBC2.
PharmGKBi PA134906266.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG301764.
GeneTreei ENSGT00760000118985.
HOGENOMi HOG000004804.
HOVERGENi HBG005591.
InParanoidi Q9UBC2.
OMAi MDDPFKN.
OrthoDBi EOG7JHM68.
PhylomeDBi Q9UBC2.
TreeFami TF324293.

Enzyme and pathway databases

Reactomei REACT_12484. EGFR downregulation.

Miscellaneous databases

ChiTaRSi EPS15L1. human.
GeneWikii EPS15L1.
GenomeRNAii 58513.
NextBioi 65055.
PROi Q9UBC2.

Gene expression databases

Bgeei Q9UBC2.
CleanExi HS_EPS15L1.
ExpressionAtlasi Q9UBC2. baseline and differential.
Genevestigatori Q9UBC2.

Family and domain databases

Gene3Di 1.10.238.10. 3 hits.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
[Graphical view ]
SMARTi SM00054. EFh. 3 hits.
SM00027. EH. 3 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 4 hits.
PS50031. EH. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Nakashima S., Morinaka K., Ikeda M., Kishida S., Koyama S., Kikuchi A.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Selection system for genes encoding nuclear-targeted proteins."
    Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
    Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], SUBCELLULAR LOCATION.
    Tissue: Fetal brain.
  3. "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] (ISOFORMS 2 AND 3).
    Tissue: Thalamus.
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 3 AND 4).
  7. "eps15 and eps15R are essential components of the endocytic pathway."
    Carbone R., Fre S., Iannolo G., Belleudi F., Mancini P., Pelicci P.G., Torrisi M.R., Di Fiore P.P.
    Cancer Res. 57:5498-5504(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "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-244; SER-255; SER-560; THR-577 AND THR-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "FCHo proteins are nucleators of clathrin-mediated endocytosis."
    Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., McMahon H.T.
    Science 328:1281-1284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCHO2.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "The clathrin adaptor Dab2 recruits EH domain scaffold proteins to regulate integrin beta1 endocytosis."
    Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.
    Mol. Biol. Cell 23:2905-2916(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DAB2.
  18. "Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
    Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
    Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCHO1.

Entry informationi

Entry nameiEP15R_HUMAN
AccessioniPrimary (citable) accession number: Q9UBC2
Secondary accession number(s): A2RRF3, A5PL29, B4DKA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 129 of the entry and version 1 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3