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Identification
HMDB Protein ID HMDBP08579
Secondary Accession Numbers
  • 14294
Name Putative E3 ubiquitin-protein ligase SH3RF1
Synonyms
  1. Plenty of SH3s
  2. Protein POSH
  3. RING finger protein 142
  4. SH3 domain-containing RING finger protein 1
  5. SH3 multiple domains protein 2
Gene Name SH3RF1
Protein Type Unknown
Biological Properties
General Function Involved in protein binding
Specific Function Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin- conjugating enzymes such as UBE2D1 or UBE2N and then transfers it to substrates. In the absence of an external substrate, it can catalyze self-ubiquitination
Pathways Not Available
Reactions Not Available
GO Classification
Function
ion binding
cation binding
metal ion binding
binding
transition metal ion binding
zinc ion binding
protein binding
Cellular Location
  1. Cytoplasm
  2. Cytoplasm
  3. perinuclear region
  4. Golgi apparatus
  5. Cell projection
  6. lamellipodium
  7. trans-Golgi network
Gene Properties
Chromosome Location Chromosome:4
Locus 4q32.3
SNPs SH3RF1
Gene Sequence
>2667 bp
ATGGATGAATCAGCCTTGTTGGATCTTTTGGAGTGTCCGGTGTGTCTAGAGCGCCTTGAT
GCTTCTGCGAAGGTCTTGCCTTGCCAGCATACGTTTTGCAAGCGATGTTTGCTGGGGATC
GTAGGTTCTCGAAATGAACTCAGATGTCCCGAGTGCAGGACTCTTGTTGGCTCGGGTGTC
GAGGAGCTTCCCAGTAACATCTTGCTGGTCAGACTTCTGGATGGCATCAAACAGAGGCCT
TGGAAACCTGGTCCTGGTGGGGGAAGTGGGACCAACTGCACAAATGCATTAAGGTCTCAG
AGCAGCACTGTGGCTAATTGTAGCTCAAAAGATCTGCAGAGCTCCCAGGGCGGACAGCAG
CCTCGGGTGCAATCCTGGAGCCCCCCAGTGAGGGGTATACCTCAGTTACCATGTGCCAAA
GCATTATACAACTATGAAGGAAAAGAGCCTGGAGACCTTAAATTCAGCAAAGGTGACATC
ATCATTTTGCGAAGACAAGTGGATGAAAATTGGTACCATGGGGAAGTCAATGGAATCCAT
GGCTTTTTCCCCACCAACTTTGTGCAGATTATTAAACCGTTACCTCAGCCCCCACCTCAG
TGCAAAGCACTTTATGACTTTGAAGTGAAAGACAAGGAAGCAGACAAAGATTGCCTTCCA
TTTGCAAAGGATGATGTTCTGACTGTGATCCGAAGAGTGGATGAAAACTGGGCTGAAGGA
ATGCTGGCAGACAAAATAGGAATATTTCCAATTTCATATGTTGAGTTTAACTCGGCTGCT
AAGCAGCTGATAGAATGGGATAAGCCTCCTGTGCCAGGAGTTGATGCTGGAGAATGTTCC
TCGGCAGCAGCCCAGAGCAGCACTGCCCCAAAGCACTCCGACACCAAGAAGAACACCAAA
AAGCGGCACTCCTTCACTTCCCTCACTATGGCCAACAAGTCCTCCCAGGCATCCCAGAAC
CGCCACTCCATGGAGATCAGCCCCCCTGTCCTCATCAGCTCCAGCAACCCCACTGCTGCT
GCACGGATCAGCGAGCTGTCTGGGCTCTCCTGCAGTGCCCCTTCTCAGGTTCATATAAGT
ACCACCGGGTTAATTGTGACCCCGCCCCCAAGCAGCCCAGTGACAACTGGCCCCTCGTTT
ACTTTCCCATCAGATGTTCCCTACCAAGCTGCCCTTGGAACTTTGAATCCTCCTCTTCCA
CCACCCCCTCTCCTGGCTGCCACTGTCCTTGCCTCCACACCACCAGGCGCCACCGCCGCT
GCTGCTGCTGCTGGAATGGGACCGAGGCCCATGGCAGGATCCACTGACCAGATTGCACAT
TTACGGCCGCAGACTCGCCCCAGTGTGTATGTTGCTATATATCCATACACTCCTCGGAAA
GAGGATGAACTAGAGCTGAGAAAAGGGGAGATGTTTTTAGTGTTTGAGCGCTGCCAGGAT
GGCTGGTTCAAAGGGACATCCATGCATACCAGCAAGATAGGGGTTTTCCCTGGCAATTAT
GTGGCACCAGTCACAAGGGCGGTGACAAATGCTTCCCAAGCTAAAGTCCCTATGTCTACA
GCTGGCCAGACAAGTCGGGGAGTGACCATGGTCAGTCCTTCCACGGCAGGAGGGCCTGCC
CAGAAGCTCCAGGGAAATGGCGTGGCTGGGAGTCCCAGTGTTGTCCCCGCAGCTGTGGTA
TCAGCAGCTCACATCCAGACAAGTCCTCAGGCTAAGGTCTTGTTGCACATGACGGGGCAA
ATGACAGTCAACCAGGCCCGCAATGCTGTGAGGACAGTTGCAGCGCACAACCAGGAACGC
CCCACGGCAGCAGTGACACCCATCCAGGTACAGAATGCCGCCGGCCTCAGCCCTGCATCT
GTGGGCCTGTCCCATCACTCGCTGGCCTCCCCACAACCTGCGCCTCTGATGCCAGGCTCA
GCCACGCACACTGCTGCCATCAGTATCAGTCGAGCCAGTGCCCCTCTGGCCTGTGCAGCA
GCTGCTCCACTGACTTCCCCAAGCATCACCAGTGCTTCTCTGGAGGCTGAGCCCAGTGGC
CGGATAGTGACCGTTCTCCCTGGACTCCCCACATCTCCTGACAGTGCTTCATCAGCTTGT
GGGAACAGTTCAGCAACCAAACCAGACAAGGATAGCAAAAAAGAAAAAAAGGGTTTGTTG
AAGTTGCTTTCTGGCGCCTCCACTAAACGGAAGCCCCGCGTGTCTCCTCCAGCATCGCCC
ACCCTAGAAGTGGAGCTGGGCAGTGCAGAGCTTCCTCTCCAGGGAGCGGTGGGGCCCGAA
CTGCCACCAGGAGGTGGCCATGGCAGGGCAGGCTCCTGCCCTGTGGACGGGGACGGACCG
GTCACGACTGCAGTGGCAGGAGCAGCCCTGGCCCAGGATGCTTTTCATAGGAAGGCAAGT
TCCCTGGACTCCGCAGTTCCCATCGCTCCACCTCCTCGCCAGGCCTGTTCCTCCCTGGGT
CCTGTCTTGAATGAGTCTAGACCTGTCGTTTGTGAAAGGCACAGGGTGGTGGTTTCCTAT
CCTCCTCAGAGTGAGGCAGAACTTGAACTTAAAGAAGGAGATATTGTGTTTGTTCATAAA
AAACGAGAGGATGGCTGGTTCAAAGGCACATTACAACGTAATGGGAAAACTGGCCTTTTC
CCAGGAAGCTTTGTGGAAAACATATGA
Protein Properties
Number of Residues 888
Molecular Weight 93128.1
Theoretical pI 8.66
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Putative E3 ubiquitin-protein ligase SH3RF1
MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGV
EELPSNILLVRLLDGIKQRPWKPGPGGGSGTNCTNALRSQSSTVANCSSKDLQSSQGGQQ
PRVQSWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIILRRQVDENWYHGEVNGIH
GFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEG
MLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDAGECSSAAAQSSTAPKHSDTKKNTK
KRHSFTSLTMANKSSQASQNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHIS
TTGLIVTPPPSSPVTTGPSFTFPSDVPYQAALGTLNPPLPPPPLLAATVLASTPPGATAA
AAAAGMGPRPMAGSTDQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQD
GWFKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQTSRGVTMVSPSTAGGPA
QKLQGNGVAGSPSVVPAAVVSAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQER
PTAAVTPIQVQNAAGLSPASVGLSHHSLASPQPAPLMPGSATHTAAISISRASAPLACAA
AAPLTSPSITSASLEAEPSGRIVTVLPGLPTSPDSASSACGNSSATKPDKDSKKEKKGLL
KLLSGASTKRKPRVSPPASPTLEVELGSAELPLQGAVGPELPPGGGHGRAGSCPVDGDGP
VTTAVAGAALAQDAFHRKASSLDSAVPIAPPPRQACSSLGPVLNESRPVVCERHRVVVSY
PPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI
GenBank ID Protein 51988887
UniProtKB/Swiss-Prot ID Q7Z6J0
UniProtKB/Swiss-Prot Entry Name SH3R1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_020870.3
GeneCard ID SH3RF1
GenAtlas ID SH3RF1
HGNC ID HGNC:17650
References
General References
  1. 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: 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. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed:10819331 ]
  4. Xu Z, Kukekov NV, Greene LA: POSH acts as a scaffold for a multiprotein complex that mediates JNK activation in apoptosis. EMBO J. 2003 Jan 15;22(2):252-61. [PubMed:12514131 ]
  5. Figueroa C, Tarras S, Taylor J, Vojtek AB: Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex. J Biol Chem. 2003 Nov 28;278(48):47922-7. Epub 2003 Sep 21. [PubMed:14504284 ]
  6. Alroy I, Tuvia S, Greener T, Gordon D, Barr HM, 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, Caspi-Bachar E, Alchanati I, Sela-Brown A, Moskowitz H, Tessmer U, Schubert U, Reiss Y: The trans-Golgi network-associated human ubiquitin-protein ligase POSH is essential for HIV type 1 production. Proc Natl Acad Sci U S A. 2005 Feb 1;102(5):1478-83. Epub 2005 Jan 19. [PubMed:15659549 ]
  7. Xu Z, Sproul A, Wang W, Kukekov N, Greene LA: Siah1 interacts with the scaffold protein POSH to promote JNK activation and apoptosis. J Biol Chem. 2006 Jan 6;281(1):303-12. Epub 2005 Oct 17. [PubMed:16230351 ]
  8. Kukekov NV, Xu Z, Greene LA: Direct interaction of the molecular scaffolds POSH and JIP is required for apoptotic activation of JNKs. J Biol Chem. 2006 Jun 2;281(22):15517-24. Epub 2006 Mar 29. [PubMed:16571722 ]
  9. Lyons TR, Thorburn J, Ryan PW, Thorburn A, Anderson SM, Kassenbrock CK: Regulation of the Pro-apoptotic scaffolding protein POSH by Akt. J Biol Chem. 2007 Jul 27;282(30):21987-97. Epub 2007 May 29. [PubMed:17535800 ]
  10. Tuvia S, Taglicht D, Erez O, Alroy I, Alchanati I, Bicoviski V, Dori-Bachash M, Ben-Avraham D, Reiss Y: The ubiquitin E3 ligase POSH regulates calcium homeostasis through spatial control of Herp. J Cell Biol. 2007 Apr 9;177(1):51-61. [PubMed:17420289 ]