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Q00587

- BORG5_HUMAN

UniProt

Q00587 - BORG5_HUMAN

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Protein

Cdc42 effector protein 1

Gene

CDC42EP1

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

Functioni

Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts.1 Publication

GO - Biological processi

  1. positive regulation of pseudopodium assembly Source: UniProtKB
  2. regulation of cell shape Source: UniProtKB
  3. Rho protein signal transduction Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ00587.

Names & Taxonomyi

Protein namesi
Recommended name:
Cdc42 effector protein 1
Alternative name(s):
Binder of Rho GTPases 5
Serum protein MSE55
Gene namesi
Name:CDC42EP1
Synonyms:BORG5, CEP1, MSE55
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:17014. CDC42EP1.

Subcellular locationi

Endomembrane system 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasmcytoskeleton 1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. cytoplasm Source: HPA
  3. focal adhesion Source: UniProtKB
  4. Golgi apparatus Source: HPA
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 4712DMISH…GDFRH → AMISHALGDFRA: No binding with CDC42. 1 PublicationAdd
BLAST

Organism-specific databases

PharmGKBiPA38430.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Cdc42 effector protein 1PRO_0000212657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei101 – 1011Phosphoserine2 Publications
Modified residuei113 – 1131Phosphoserine2 Publications
Modified residuei121 – 1211Phosphoserine3 Publications
Modified residuei190 – 1901Phosphoserine1 Publication
Modified residuei192 – 1921Phosphoserine3 Publications
Modified residuei195 – 1951Phosphoserine1 Publication
Modified residuei350 – 3501Phosphoserine3 Publications
Modified residuei353 – 3531Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ00587.
PaxDbiQ00587.
PRIDEiQ00587.

PTM databases

PhosphoSiteiQ00587.

Expressioni

Tissue specificityi

Endothelial and bone marrow stromal cells.

Gene expression databases

BgeeiQ00587.
CleanExiHS_CDC42EP1.
ExpressionAtlasiQ00587. baseline and differential.
GenevestigatoriQ00587.

Organism-specific databases

HPAiHPA006379.

Interactioni

Subunit structurei

Interacts with RHOQ and CDC42, in a GTP-dependent manner.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC42P609533EBI-744130,EBI-81752

Protein-protein interaction databases

BioGridi116308. 11 interactions.
IntActiQ00587. 12 interactions.
MINTiMINT-1454089.
STRINGi9606.ENSP00000249014.

Structurei

3D structure databases

ProteinModelPortaliQ00587.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 5215CRIBPROSITE-ProRule annotationAdd
BLAST
Repeati220 – 22671
Repeati227 – 23372
Repeati234 – 24073
Repeati241 – 24774
Repeati248 – 25475
Repeati255 – 26176
Repeati262 – 26877
Repeati269 – 27578

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni220 – 275568 X 7 AA tandem repeats of [PT]-[AT]-A-[ENT]-[PT]-[PTS]-[AG]Add
BLAST

Domaini

The CRIB domain mediates interaction with CDC42.

Sequence similaritiesi

Belongs to the BORG/CEP family.Curated
Contains 1 CRIB domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG45247.
GeneTreeiENSGT00730000110869.
HOGENOMiHOG000095252.
HOVERGENiHBG080906.
InParanoidiQ00587.
OMAiTVQANTF.
OrthoDBiEOG7V1FSH.
PhylomeDBiQ00587.
TreeFamiTF331725.

Family and domain databases

InterProiIPR029273. Cdc42_effect.
IPR000095. CRIB_dom.
[Graphical view]
PfamiPF14957. BORG_CEP. 1 hit.
PF00786. PBD. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
[Graphical view]
PROSITEiPS50108. CRIB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q00587) [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
MPGPQGGRGA ATMSLGKLSP VGWVSSSQGK RRLTADMISH PLGDFRHTMH
60 70 80 90 100
VGRGGDVFGD TSFLSNHGGS SGSTHRSPRS FLAKKLQLVR RVGAPPRRMA
110 120 130 140 150
SPPAPSPAPP AISPIIKNAI SLPQLNQAAY DSLVVGKLSF DSSPTSSTDG
160 170 180 190 200
HSSYGLDSGF CTISRLPRSE KPHDRDRDGS FPSEPGLRRS DSLLSFRLDL
210 220 230 240 250
DLGPSLLSEL LGVMSLPEAP AAETPAPAAN PPAPTANPTG PAANPPATTA
260 270 280 290 300
NPPAPAANPS APAATPTGPA ANPPAPAASS TPHGHCPNGV TAGLGPVAEV
310 320 330 340 350
KSSPVGGGPR GPAGPALGRH WGAGWDGGHH YPEMDARQER VEVLPQARAS
360 370 380 390
WESLDEEWRA PQAGSRTPVP STVQANTFEF ADAEEDDEVK V
Length:391
Mass (Da):40,295
Last modified:February 1, 1994 - v1
Checksum:i625EA3C71F20CF2B
GO
Isoform 2 (identifier: Q00587-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     258-264: Missing.

Show »
Length:384
Mass (Da):39,686
Checksum:i3D056D62399AE422
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei258 – 2647Missing in isoform 2. 2 PublicationsVSP_004325

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M88338 mRNA. Translation: AAA36606.1.
CR456524 mRNA. Translation: CAG30410.1.
AK292190 mRNA. Translation: BAF84879.1.
AL022315 Genomic DNA. Translation: CAB42833.1.
CH471095 Genomic DNA. Translation: EAW60164.1.
BC009356 mRNA. Translation: AAH09356.1.
CCDSiCCDS13949.1. [Q00587-1]
PIRiA42973.
RefSeqiNP_689449.1. NM_152243.2. [Q00587-1]
XP_006724170.1. XM_006724107.1. [Q00587-1]
XP_006724171.1. XM_006724108.1. [Q00587-1]
XP_006724172.1. XM_006724109.1. [Q00587-1]
UniGeneiHs.225356.

Genome annotation databases

EnsembliENST00000249014; ENSP00000249014; ENSG00000128283. [Q00587-1]
GeneIDi11135.
KEGGihsa:11135.
UCSCiuc003asz.4. human. [Q00587-1]

Polymorphism databases

DMDMi462623.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M88338 mRNA. Translation: AAA36606.1 .
CR456524 mRNA. Translation: CAG30410.1 .
AK292190 mRNA. Translation: BAF84879.1 .
AL022315 Genomic DNA. Translation: CAB42833.1 .
CH471095 Genomic DNA. Translation: EAW60164.1 .
BC009356 mRNA. Translation: AAH09356.1 .
CCDSi CCDS13949.1. [Q00587-1 ]
PIRi A42973.
RefSeqi NP_689449.1. NM_152243.2. [Q00587-1 ]
XP_006724170.1. XM_006724107.1. [Q00587-1 ]
XP_006724171.1. XM_006724108.1. [Q00587-1 ]
XP_006724172.1. XM_006724109.1. [Q00587-1 ]
UniGenei Hs.225356.

3D structure databases

ProteinModelPortali Q00587.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116308. 11 interactions.
IntActi Q00587. 12 interactions.
MINTi MINT-1454089.
STRINGi 9606.ENSP00000249014.

PTM databases

PhosphoSitei Q00587.

Polymorphism databases

DMDMi 462623.

Proteomic databases

MaxQBi Q00587.
PaxDbi Q00587.
PRIDEi Q00587.

Protocols and materials databases

DNASUi 11135.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000249014 ; ENSP00000249014 ; ENSG00000128283 . [Q00587-1 ]
GeneIDi 11135.
KEGGi hsa:11135.
UCSCi uc003asz.4. human. [Q00587-1 ]

Organism-specific databases

CTDi 11135.
GeneCardsi GC22P037956.
H-InvDB HIX0016445.
HGNCi HGNC:17014. CDC42EP1.
HPAi HPA006379.
MIMi 606084. gene.
neXtProti NX_Q00587.
PharmGKBi PA38430.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG45247.
GeneTreei ENSGT00730000110869.
HOGENOMi HOG000095252.
HOVERGENi HBG080906.
InParanoidi Q00587.
OMAi TVQANTF.
OrthoDBi EOG7V1FSH.
PhylomeDBi Q00587.
TreeFami TF331725.

Enzyme and pathway databases

SignaLinki Q00587.

Miscellaneous databases

GeneWikii CDC42EP1.
GenomeRNAii 11135.
NextBioi 42326.
PROi Q00587.
SOURCEi Search...

Gene expression databases

Bgeei Q00587.
CleanExi HS_CDC42EP1.
ExpressionAtlasi Q00587. baseline and differential.
Genevestigatori Q00587.

Family and domain databases

InterProi IPR029273. Cdc42_effect.
IPR000095. CRIB_dom.
[Graphical view ]
Pfami PF14957. BORG_CEP. 1 hit.
PF00786. PBD. 1 hit.
[Graphical view ]
SMARTi SM00285. PBD. 1 hit.
[Graphical view ]
PROSITEi PS50108. CRIB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and molecular characterization of MSE55, a novel human serum constituent protein that displays bone marrow stromal/endothelial cell-specific expression."
    Bahou W.F., Campbell A.D., Wicha M.S.
    J. Biol. Chem. 267:13986-13992(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] (ISOFORM 2).
    Tissue: Mammary gland.
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [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] (ISOFORM 2).
    Tissue: Pancreas.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 166-175.
    Tissue: Platelet.
  8. "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins."
    Joberty G., Perlungher R.R., Macara I.G.
    Mol. Cell. Biol. 19:6585-6597(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RHOQ AND CDC42.
    Tissue: Embryo.
  9. "MSE55, a Cdc42 effector protein, induces long cellular extensions in fibroblasts."
    Burbelo P.D., Snow D.M., Bahou W., Spiegel S.
    Proc. Natl. Acad. Sci. U.S.A. 96:9083-9088(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC42, SUBCELLULAR LOCATION, MUTAGENESIS OF 36-ASP--HIS-47.
  10. "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.
  11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-19; SER-101; SER-113; SER-121 AND SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-190; SER-192; SER-195; SER-350 AND SER-353, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-101; SER-113; SER-121; SER-192; SER-350 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBORG5_HUMAN
AccessioniPrimary (citable) accession number: Q00587
Secondary accession number(s): A8K825, Q96GN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 29, 2014
This is version 132 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3