SH3RF1 Polyclonal Antibody for Human(Homo sapiens) | EIAab.comSH3RF1 Polyclonal Antibody for Human(Homo sapiens)

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SH3RF1 (Gene name),

E3 ubiquitin-protein ligase SH3RF1 (Protein name ), SH3R1_HUMAN from NCBI database.

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General Annotation

Antigen Annotation

Predicted Eptitope

Vaild Sequence

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Gene name:

SH3RF1(KIAA1494;POSH;RNF142;SH3MD2);

Protein name:

E3 ubiquitin-protein ligase SH3RF1;

Alternative:

RING finger protein 142;Plenty of SH3s(Protein POSH);SH3 multiple domains protein 2;SH3 domain-containing RING finger protein 1;

Organism:

Human (Homo sapiens).

General Annotation

Sub Unit:

Interacts with Rac; in a GTP-dependent manner (By similarity). Interacts with MAP3K10 and MAP3K11. Interacts with MAPK8IP; this interaction leads to the PJAC complex (POSH-JIP or SH3RF1/MAPK8IP apoptotic complex) with a 1:1 ratio. Interacts with SIAH1. Interacts with HERP1. Probably part of a signaling complex that may contain SH3RF1, MAPK8IP, DLK1, MAP2K4, MAP2K7, MAPK8, MAPK9, AKT1 and AKT2.

Function:

Plays an essential role in the targeting of HIV-1 Gag to the plasma membrane, this function is dependent on it's RING domain, and hence it's E3 ligase activity.

Subcellular Location:

Cytoplasm perinuclear region Cell projection lamellipodium Cytoplasm Golgi apparatus trans-Golgi network Colocalizes, with AKT2, in lamellipodia (By similarity). Colocalizes, with HERP1, in trans-Golgi network.

Protein Attributes:

Sequence length:

888

Sequence:

50:

100:

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300:

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650:

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888:

KEGDIVFVHK | KREDGWFKGT | LQRNGKTGLF | PGSFVENI

3D Structure:

N/A

Predicted Eptitope:

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Vaild Sequence:

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Related Databases

Pfam:

PF00018

UniGene:

Hs.301804

STRING:

9606.ENSP00000284637

SMR:

Q7Z6J0

String:

Q7Z6J0

KEGG:

hsa:57630

Pfam:

PF00097

Uniprot:

Q7Z6J0

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ELISA Kit for Human E3 ubiquitin-protein ligase SH3RF1

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E15485h

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96T

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ELISA Kit for Human E3 ubiquitin-protein ligase SH3RF1

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E15485m

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96T

ELISA Kit for Human E3 ubiquitin-protein ligase SH3RF1

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E15485b

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96T

ELISA Kit for Human E3 ubiquitin-protein ligase SH3RF1

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E15485r

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96T

CLIA Kit for Human E3 ubiquitin-protein ligase SH3RF1

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U15485m

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96T

CLIA Kit for Human E3 ubiquitin-protein ligase SH3RF1

Cat.:

U15485b

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96T

CLIA Kit for Human E3 ubiquitin-protein ligase SH3RF1

Cat.:

U15485r

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96T

CLIA Kit for Human E3 ubiquitin-protein ligase SH3RF1

Cat.:

U15485h

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96T

Polyclonal Antibody for Human E3 ubiquitin-protein ligase SH3RF1

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P15485Rb-r

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40ug/0.2ml

Polyclonal Antibody for Human E3 ubiquitin-protein ligase SH3RF1

Cat.:

P15485Rb-h

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40ug/0.2ml

Polyclonal Antibody for Human E3 ubiquitin-protein ligase SH3RF1

Cat.:

P15485Rb-m

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Packing:

40ug/0.2ml

Monoclonal Antibody for Human E3 ubiquitin-protein ligase SH3RF1

Protein for Human E3 ubiquitin-protein ligase SH3RF1

R&D Technical Data

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Precision

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Recovery

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Linearity

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References

1.

"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]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1);NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-888 (ISOFORM 2)
tissue: Eye.
tissue: Ovary.
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. , more...
Nat. Genet.36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-712 (ISOFORM 1)
tissue: Embryo.
3.

"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T. , Kikuno R. , Ishikawa K. , Hirosawa M. , Ohara O.
DNA Res.7:143-150(2000) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 251-888 (ISOFORM 1)
tissue: Brain.
4.

"POSH acts as a scaffold for a multiprotein complex that mediates JNK activation in apoptosis."
Xu Z. , Kukekov N.V. , Greene L.A.
EMBO J.22:252-261(2003) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH MAP3K10; MAP3K11; DLK1; MAP2K4; MAP2K7; MAPK8 AND MAPK9
5.

"Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex."
Figueroa C. , Tarras S. , Taylor J. , Vojtek A.B.
J. Biol. Chem.278:47922-47927(2003) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH AKT1 AND AKT2
6.

"The trans-Golgi network-associated human ubiquitin-protein ligase POSH is essential for HIV type 1 production."
Alroy I. , Tuvia S. , Greener T. , Gordon D. , Barr H.M. , Taglicht D. , Mandil-Levin R. , Ben-Avraham D. , Konforty D. , Nir A. , Levius O. , Bicoviski V. , Dori M. , Cohen S. , Yaar L. , Erez O. , Propheta-Meiran O. , Koskas M. , more...
Proc. Natl. Acad. Sci. U.S.A.102:1478-1483(2005) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE;FUNCTION IN HIV-1 PLASMA MEMBRANE TARGETING;SUBCELLULAR LOCATION;SELF-UBIQUITINATION
7.

"Siah1 interacts with the scaffold protein POSH to promote JNK activation and apoptosis."
Xu Z. , Sproul A. , Wang W. , Kukekov N. , Greene L.A.
J. Biol. Chem.281:303-312(2006) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH SIAH1
8.

"Direct interaction of the molecular scaffolds POSH and JIP is required for apoptotic activation of JNKs."
Kukekov N.V. , Xu Z. , Greene L.A.
J. Biol. Chem.281:15517-15524(2006) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH MAPK8IP
9.

"Regulation of the pro-apoptotic scaffolding protein POSH by Akt."
Lyons T.R. , Thorburn J. , Ryan P.W. , Thorburn A. , Anderson S.M. , Kassenbrock C.K.
J. Biol. Chem.282:21987-21997(2007) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH AKT1 AND AKT2;PHOSPHORYLATION AT SER-304;MUTAGENESIS OF SER-304;IDENTIFICATION BY MASS SPECTROMETRY
10.

"The ubiquitin E3 ligase POSH regulates calcium homeostasis through spatial control of Herp."
Tuvia S. , Taglicht D. , Erez O. , Alroy I. , Alchanati I. , Bicoviski V. , Dori-Bachash M. , Ben-Avraham D. , Reiss Y.
J. Cell Biol.177:51-61(2007) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH HERP1;SUBCELLULAR LOCATION;MUTAGENESIS OF VAL-14
11.

"POSH stimulates the ubiquitination and the clathrin-independent endocytosis of ROMK1 channels."
Lin D.H. , Yue P. , Pan C.Y. , Sun P. , Zhang X. , Han Z. , Roos M. , Caplan M. , Giebisch G. , Wang W.H.
J. Biol. Chem.284:29614-29624(2009) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE
12.

"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]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
tissue: Cervix carcinoma.

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