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Q9H3Q1

- BORG4_HUMAN

UniProt

Q9H3Q1 - BORG4_HUMAN

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Protein
Cdc42 effector protein 4
Gene
CDC42EP4, BORG4, CEP4
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. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.

GO - Molecular functioni

  1. GTP-Rho binding Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

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

Keywords - Biological processi

Cell shape

Names & Taxonomyi

Protein namesi
Recommended name:
Cdc42 effector protein 4
Alternative name(s):
Binder of Rho GTPases 4
Gene namesi
Synonyms:BORG4, CEP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:17147. CDC42EP4.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. cytoplasm Source: UniProtKB-KW
  3. endomembrane system Source: UniProtKB-SubCell
  4. microtubule cytoskeleton Source: HPA
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Cdc42 effector protein 4
PRO_0000212655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphoserine2 Publications
Modified residuei118 – 1181Phosphoserine1 Publication
Modified residuei138 – 1381Phosphoserine1 Publication
Modified residuei140 – 1401Phosphoserine1 Publication
Modified residuei142 – 1421Phosphoserine1 Publication
Modified residuei174 – 1741Phosphoserine3 Publications
Modified residuei292 – 2921Phosphoserine2 Publications
Modified residuei295 – 2951Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H3Q1.
PaxDbiQ9H3Q1.
PeptideAtlasiQ9H3Q1.
PRIDEiQ9H3Q1.

PTM databases

PhosphoSiteiQ9H3Q1.

Expressioni

Tissue specificityi

Not detected in any of the adult tissues tested. May be expressed only in fetal or embryonic tissues.

Gene expression databases

ArrayExpressiQ9H3Q1.
BgeeiQ9H3Q1.
CleanExiHS_CDC42EP4.
GenevestigatoriQ9H3Q1.

Organism-specific databases

HPAiHPA023335.
HPA024797.

Interactioni

Subunit structurei

Interacts with CDC42 and RHOQ, in a GTP-dependent manner By similarity.

Protein-protein interaction databases

BioGridi117115. 10 interactions.
IntActiQ9H3Q1. 5 interactions.
MINTiMINT-1464445.
STRINGi9606.ENSP00000338258.

Structurei

3D structure databases

ProteinModelPortaliQ9H3Q1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 4115CRIB
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi70 – 745Poly-Ser

Sequence similaritiesi

Belongs to the BORG/CEP family.
Contains 1 CRIB domain.

Phylogenomic databases

eggNOGiNOG44582.
HOGENOMiHOG000231054.
HOVERGENiHBG052803.
InParanoidiQ9H3Q1.
OMAiKEFSFMD.
PhylomeDBiQ9H3Q1.
TreeFamiTF331725.

Family and domain databases

InterProiIPR029273. Cdc42_effect.
IPR000095. CRIB_dom.
[Graphical view]
PfamiPF14957. BORG_CEP. 1 hit.
PF00786. 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: Q9H3Q1-1) [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

MPILKQLVSS SVHSKRRSRA DLTAEMISAP LGDFRHTMHV GRAGDAFGDT    50
SFLNSKAGEP DGESLDEQPS SSSSKRSLLS RKFRGSKRSQ SVTRGEREQR 100
DMLGSLRDSA LFVKNAMSLP QLNEKEAAEK GTSKLPKSLS SSPVKKANDG 150
EGGDEEAGTE EAVPRRNGAA GPHSPDPLLD EQAFGDLTDL PVVPKATYGL 200
KHAESIMSFH IDLGPSMLGD VLSIMDKEEW DPEEGEGGYH GDEGAAGTIT 250
QAPPYAVAAP PLARQEGKAG PDLPSLPSHA LEDEGWAAAA PSPGSARSMG 300
SHTTRDSSSL SSCTSGILEE RSPAFRGPDR ARAAVSRQPD KEFSFMDEEE 350
EDEIRV 356
Length:356
Mass (Da):37,980
Last modified:March 1, 2001 - v1
Checksum:i2CF677C60C6EF1B5
GO
Isoform 2 (identifier: Q9H3Q1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     57-126: Missing.

Note: No experimental confirmation available.

Show »
Length:286
Mass (Da):30,214
Checksum:i7DAD551791D000F2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei57 – 12670Missing in isoform 2.
VSP_055544Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21P → L in AAH10451. 1 Publication
Sequence conflicti33 – 331D → T in AAD16299. 1 Publication
Sequence conflicti288 – 2881A → T in AAD16299. 1 Publication
Sequence conflicti296 – 2961A → T in AAD16299. 1 Publication
Sequence conflicti339 – 3391P → PP in AAD16299. 1 Publication
Sequence conflicti355 – 3551Missing in AAD16299. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB042237 mRNA. Translation: BAB17272.1.
AF099664 mRNA. Translation: AAD16299.1.
AK097835 mRNA. Translation: BAG53539.1.
AC087301 Genomic DNA. No translation available.
BC002774 mRNA. Translation: AAH02774.1.
BC010451 mRNA. Translation: AAH10451.1.
CCDSiCCDS11695.1.
RefSeqiNP_036253.2. NM_012121.4.
XP_005257239.1. XM_005257182.2.
UniGeneiHs.3903.

Genome annotation databases

EnsembliENST00000335793; ENSP00000338258; ENSG00000179604.
ENST00000439510; ENSP00000404270; ENSG00000179604.
GeneIDi23580.
KEGGihsa:23580.
UCSCiuc002jjn.3. human.

Polymorphism databases

DMDMi21362403.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB042237 mRNA. Translation: BAB17272.1 .
AF099664 mRNA. Translation: AAD16299.1 .
AK097835 mRNA. Translation: BAG53539.1 .
AC087301 Genomic DNA. No translation available.
BC002774 mRNA. Translation: AAH02774.1 .
BC010451 mRNA. Translation: AAH10451.1 .
CCDSi CCDS11695.1.
RefSeqi NP_036253.2. NM_012121.4.
XP_005257239.1. XM_005257182.2.
UniGenei Hs.3903.

3D structure databases

ProteinModelPortali Q9H3Q1.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117115. 10 interactions.
IntActi Q9H3Q1. 5 interactions.
MINTi MINT-1464445.
STRINGi 9606.ENSP00000338258.

PTM databases

PhosphoSitei Q9H3Q1.

Polymorphism databases

DMDMi 21362403.

Proteomic databases

MaxQBi Q9H3Q1.
PaxDbi Q9H3Q1.
PeptideAtlasi Q9H3Q1.
PRIDEi Q9H3Q1.

Protocols and materials databases

DNASUi 23580.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335793 ; ENSP00000338258 ; ENSG00000179604 .
ENST00000439510 ; ENSP00000404270 ; ENSG00000179604 .
GeneIDi 23580.
KEGGi hsa:23580.
UCSCi uc002jjn.3. human.

Organism-specific databases

CTDi 23580.
GeneCardsi GC17M071279.
HGNCi HGNC:17147. CDC42EP4.
HPAi HPA023335.
HPA024797.
MIMi 605468. gene.
neXtProti NX_Q9H3Q1.
PharmGKBi PA38439.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG44582.
HOGENOMi HOG000231054.
HOVERGENi HBG052803.
InParanoidi Q9H3Q1.
OMAi KEFSFMD.
PhylomeDBi Q9H3Q1.
TreeFami TF331725.

Miscellaneous databases

ChiTaRSi CDC42EP4. human.
GeneWikii CDC42EP4.
GenomeRNAii 23580.
NextBioi 46182.
PROi Q9H3Q1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H3Q1.
Bgeei Q9H3Q1.
CleanExi HS_CDC42EP4.
Genevestigatori Q9H3Q1.

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 ]
PROSITEi PS50108. CRIB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis, gene expression, and chromosomal assignment of mouse Borg4 gene and its human orthologue."
    Osada N., Kusuda J., Suzuki Y., Sugano S., Hashimoto K.
    J. Hum. Genet. 45:374-377(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Ileal mucosa.
  2. "A new family of Cdc42 effector proteins, CEPs, function in fibroblast and epithelial cell shape changes."
    Hirsch D.S., Pirone D.M., Burbelo P.D.
    J. Biol. Chem. 276:875-883(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Eye.
  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: Testis.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Brain and Skin.
  6. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-292 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-138; SER-174; SER-292 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-64; SER-118; SER-140; SER-142; SER-174 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiBORG4_HUMAN
AccessioniPrimary (citable) accession number: Q9H3Q1
Secondary accession number(s): B3KUS7, O95828, Q96FT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 114 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 17
    Human chromosome 17: 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

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