wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-ribosomal protein eS31 fusion protein [Cleaved into: Ubiquitin; Small ribosomal subunit protein eS31 (40S ribosomal protein S27a)] (P62980)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- ZZ-type domain-containing protein
- ZZ-type domain-containing protein
- 40S ribosomal protein S29
- 40S ribosomal protein S25
- Small ribosomal subunit protein eS25
- 60S ribosomal protein L29
- 40S ribosomal protein S28
- 40S ribosomal protein S19
- 60S ribosomal protein L11
- 40S ribosomal protein S28
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGAKKRKKKTYTKPKKIKHKKKKVKLAVLQFYKVDDTGKVQRLRKECPNAECGAGTFMANHFDRHYCGKCGLTYVYNKAGGD
Protein: Rab-like protein 6 (GTP-binding protein Parf) (Partner of ARF) (Rab-like protein 1) (RBEL1) (Q3YEC7)
Organism: Homo sapiens (Human)
Function: May enhance cellular proliferation. May reduce growth inhibitory activity of CDKN2A.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:17962191}. Note=Predominantly cytoplasmic (PubMed:17962191).; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:17962191}. Note=Predominantly nuclear (PubMed:17962191).
Interaction partners:
- Transforming growth factor beta regulator 1
- Methyl-CpG-binding domain protein 3
Sequence:
MFSALKKLVGSDQAPGRDKNIPAGLQSMNQALQRRFAKGVQYNMKIVIRGDRNTGKTALWHRLQGRPFVEEYIPTQEIQVTSIHWSYKTTDDIVKVEVWDVVDKGKCKKRGDGLKMENDPQEAESEMALDAEFLDVYKNCNGVVMMFDITKQWTFNYILRELPKVPTHVPVCVLGNYRDMGEHRVILPDDVRDFIDNLDRPPGSSYFRYAESSMKNSFGLKYLHKFFNIPFLQLQRETLLRQLETNQLDMDATLEELSVQQETEDQNYGIFLEMMEARSRGHASPLAANGQSPSPGSQSPVVPAGAVSTGSSSPGTPQPAPQLPLNAAPPSSVPPVPPSEALPPPACPSAPAPRRSIISRLFGTSPATEAAPPPPEPVPAAEGPATVQSVEDFVPDDRLDRSFLEDTTPARDEKKVGAKAAQQDSDSDGEALGGNPMVAGFQDDVDLEDQPRGSPPLPAGPVPSQDITLSSEEEAEVAAPTKGPAPAPQQCSEPETKWSSIPASKPRRGTAPTRTAAPPWPGGVSVRTGPEKRSSTRPPAEMEPGKGEQASSSESDPEGPIAAQMLSFVMDDPDFESEGSDTQRRADDFPVRDDPSDVTDEDEGPAEPPPPPKLPLPAFRLKNDSDLFGLGLEEAGPKESSEEGKEGKTPSKEKKKKKKKGKEEEEKAAKKKSKHKKSKDKEEGKEERRRRQQRPPRSRERTAADELEAFLGGGAPGGRHPGGGDYEEL
Protein: Anti-sigma factor (C5AW20)
Organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens)
Interaction partners:
- Phyllosphere-induced regulator PhyR
- RNA polymerase sigma factor
Sequence:
MWRQGDLERMNENEPAGAFPSGDRPTRGRGDNGLNDQTQRRIGSHLRTLYDSVVQQPIPDRFRDLIARLEDEPANPDDPASV
Protein: Uncharacterized mitochondrial carrier C1271.11 (O94344)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:16823372}; Multi-pass membrane protein {ECO:0000305|PubMed:16823372}.
Interaction partners:
- Serine/threonine-protein kinase oca2
Sequence:
MTDDEVQWKPILVGGLSGLVAETLVFPLSTIITRVQSSLSFQQAGGFQHLYRGLSSVLVSTLPSASSFFFVYEYAKARQKPGVRNHLVSASVAEVVSCGILAPAEVVRQRAQISKTSVSQIFQSMIHNYRDLWHSFKGMCGRNVPATAFQFVLYEQFKKKFSATDHVFGAPKGAALSGAITAAVLTPLDVIKTQINLRPESYRKVVRRIYKENGIFGFEKGLGLRVFASSLGLSIYLGTYEHVKSHLHIRKAGEVSVA
Protein: E3 ubiquitin-protein ligase dbl4 (EC 2.3.2.31) (DNA-break-localizing protein 4) (Histone E3 ligase 1) (RING-type E3 ubiquitin transferase dbl4) (Q9P3U4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes to DNA double-strand breaks (DSBs). {ECO:0000269|PubMed:23628481}.
Interaction partners:
- Peroxisomal membrane associated protein 20
- Translation initiation factor eIF2B subunit epsilon
- Phosphatidylinositol 4-phosphate 5-kinase its3
- Uncharacterized mitochondrial carrier C8C9.12c
- Polyubiquitin
- Ubiquitin-conjugating enzyme E2 14
- RING-box protein pip1
- Ubiquitin-like protein 1
- E3 ubiquitin-protein ligase itt1
- Transcription factor prr1
Sequence:
MSDLLDDEFYEEEFENDLLDASEFEDEFDEDAEIDDDGFTVERKRRRAHSVSYRVVSVRDLRASLNEKINQLTSIIDLTREQVLGLYRYFKWNRERLLERYIDAPEESLQKAGVGLSGSKQREVVHHEGTCEICYDEGCLPFFSAECDHEFCLACYRQYLDSRISEGESVIQCPEESCTQIVSIQSITKVLDEKSLDRYHRLLDRSFVDDNDHLRWCPAPDCEFAIECHVTQASLSSVVPTVTCNCGKQFCFGCGHDNHQPTICPLVKIWLQKCQDDSETANWIHANTKECPKCSTTIEKNGGCNHMTCKKCKYEFCWVCLGPWTEHGNNWYTCNRYEEKSSTSARDSQSKSRASLERYLHYYNRFANHEQSAKLDHELYEHTHKRMTQMQVDSNLSWVEVQFLKNAVDILFQCRQTLKWTYAFAYYLARNNQTEIFEDNQRDLELAVENLSELCERPCQDCSLSVFKQRVLDKTVYVRSRRDVLLDDTARGLAEGRWEYVVDV
Protein: Nup98 (A1YK36)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
Sequence:
KLSSEADATRATNPAAQQAVLDLTSNQYKISTSNNPAPMKVKTLGSTLNRKSLFDGLEEFDASVEGFNLKPSAKRLVIKPKVKSVEGGNPSSSIGSAPNTPQSRPKGATPNKERESFSGAIPSEPLPPAGNSPGATNGRESQDNGRRESWLHPNNLEKVRQHNIQTGMDQGSPHNSTLNELVPRKPLDTYRPSSTVRLSVSTIPENPFEDQSSTIARRETFTSQQANESVLSNRSNEAEDSAANRSRLALEAAAAEAADDESHPTGIVLRRVGYYTIPSLDDLRSYLAEDGSCVVPNFTVGREGYGNVFFGKEMDVAGLNLDEIVHFRNKEIIIYPDDENKPPIGQGLNRDAQVTLDQVWPLDKTKHEAIKDPQRLLEMDWEGKLRRVCDKNDTRFIEYRPETGSWVFRVKHF
Protein: Plant UBX domain-containing protein 2 (PUX2) (AtPUB3) (CDC48-interacting UBX-domain protein 2) (Q9ZU93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Facilitates the interaction of SYP31 and CDC48A, thereby regulating an CDC48A membrane-associated function (Ref.8). Appears to act as a negative regulator mediating the powdery mildew-plant interaction.
Subcellular location: Membrane; Peripheral membrane protein {ECO:0000269|Ref.8}.
Interaction partners:
- Plant UBX domain-containing protein 11
- Plant UBX domain-containing protein 6
- Plant UBX domain-containing protein 3
- Plant UBX domain-containing protein 5
- Plant UBX domain-containing protein 4
- Cell division control protein 48 homolog A
- F13M7.16 protein
- Cell division control protein 48 homolog D
- Cell division control protein 48 homolog E
- U-box domain-containing protein 3
Sequence:
MDDVKDKLKGFMKKVNLSSSSGKFKGQGRVLGSSSSSSAPPVNPIQNRFNSSQAPNPTPRPKPNPNPLPEKPLSSSDQKISGSTRNPDHDPVRAPQDGFDPYGAFITSSNRSQNGYSLSMFECPICKNPFTSEEEVSVHVESCLGDTNGDESSFEKDNNDNDKSEMEKLVVVYLSGKPSESSIDVLLRLFKNIVKEPENAKFRKVRMSNAKIKEAIGDVAGGVELLELVGFELKEENDEIWAVMDVPSEEQSILINKVVGYLEKRKTESSGSSAQVMEPVAPKKIDREIRVFFSVSENVASRIEVPDSFYSLSADEIKREADLRRKKIAESQLLIPRSYKEKQAKAARKRYKRSMIRVQFPDGVVLQGVFAPWEPTFALYEFVSSALKEPSLQFELLDPVLVKRRVIPHTPAPGQKPITLEDEELVPSALIRFRPIETDSLVFTGLRNELLEISEPLS
Protein: 40S ribosomal protein S6 (Q8IDR9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 60S ribosomal protein L5, putative
- Large ribosomal subunit protein uL22
- 60S ribosomal protein L27a, putative
- 60S ribosomal protein L28
- Ubiquitin-60S ribosomal protein L40
- Ribosomal protein L37
- Ribosomal protein L15
- 60S ribosomal protein L11a, putative
- 40S ribosomal protein S25
- 60S ribosomal protein L23
Sequence:
MKLNISNPLNNVQKSIEIDDEKKLLPFMEKRIGNAVPGDSIGEEFTGYVFRITGGNDKQGFPMIQGVLTNNRVRLLFKKGMKCYRPRKKGERKRKSVRGCIVGQDLSALNLTLVKKGVNEIPGLTDKAVGKKLGPKRASKIRKLFNLDKSDDVRKYVIGRAITKNGKTKFIKPKIQRLVTEKRLLRKRNLLQAKEKRRLEKKQQLKEYKQLLNKYRSELNQQHDVETTKKKKVKKSLSKTNKTASKSKLNTKQEQKDKTEKKQNKTNNIKNDKSEKKEQAKKKTKTNENTQQTKQNKPDKKNKAKK
Protein: Elicitin (Q548N3)
Organism: Phytophthora nicotianae (Potato buckeye rot agent) (Phytophthora parasitica)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU368111}.
Interaction partners:
Sequence:
MNFRALFAATVAALVGSTSATTCTTTQQTAAYVALVSILSDTSFNQCSTDSGYSMLTATSLPTTEQYKLMCASTACKTMINKIVTLNPPDCELTVPTSGLVLNVFTYANGFSSTCASL
Protein: KiSS-1 receptor (KiSS-1R) (G-protein coupled receptor 54) (G-protein coupled receptor OT7T175) (mOT7T175) (Kisspeptins receptor) (Metastin receptor) (Q91V45)
Organism: Mus musculus (Mouse)
Function: Receptor for metastin (kisspeptin-52 or kp-52), a C-terminally amidated peptide of KiSS1. KiSS1 is a metastasis suppressor protein. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. The receptor is essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/KISS1R system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. Analysis of the transduction pathways activated by the receptor identifies coupling to phospholipase C and intracellular calcium release through pertussis toxin-insensitive G(q) proteins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Metastasis-suppressor KiSS-1
- Guanine nucleotide-binding protein G
- Tachykinin-3
- Beta-arrestin-1
- Beta-arrestin-2
- Progonadoliberin-1
- Guanine nucleotide-binding protein subunit alpha-11
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
Sequence:
MATEATLAPNVTWWAPSNASGCPGCGVNASDDPGSAPRPLDAWLVPLFFATLMLLGLVGNSLVIYVICRHKHMQTVTNFYIANLAATDVTFLLCCVPFTALLYPLPAWVLGDFMCKFVNYIQQVSVQATCATLTAMSVDRWYVTVFPLRALHRRTPRLALAVSLSIWVGSAAVSAPVLALHRLSPGPRTYCSEAFPSRALERAFALYNLLALYLLPLLATCACYGAMLRHLGRAAVRPAPTDGALQGQLLAQRAGAVRTKVSRLVAAVVLLFAACWGPIQLFLVLQALGPSGAWHPRSYAAYAVKIWAHCMSYSNSALNPLLYAFLGSHFRQAFCRVCPCCRQRQRRPHTSAHSDRAATHTVPHSRAAHPVRIRSPEPGNPVVRSPCAQSERTASL
Protein: Glucosamine 6-phosphate N-acetyltransferase 1 (EC 2.3.1.4) (Glucose-6-phosphate acetyltransferase 1) (OsGNA1) (Phosphoglucosamine acetylase 1) (Phosphoglucosamine transacetylase 1) (Q5U9F2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Acetyltransferase involved in de novo biosynthesis of UDP-N-acetylglucosamine (UDP-GlcNAc) in roots and is required for maintaining normal root cell shape. UDP-GlcNAc is an essential metabolite that serves as an initial sugar donor for N-glycan synthesis and thus plays an important role in protein and lipid glycosylation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Phosphoacetylglucosamine mutase
- Os12g0131100 protein
- Os11g0133700 protein
- Hexokinase-8
- Hexokinase-7
- Hexokinase-10
- Hexokinase-9
- Hexokinase-3
- Hexokinase-4, chloroplastic
- Arginase 1, mitochondrial
Sequence:
MEQPLPTAAAEAAAAGGDGEAYRIRPLELADISRGFLGLLNQLSPSPPLTEEAFRARFEELAALGADHLVLVAEDAATGRLAAAGAVLVERKFIRRCGRVGHVEDVVVDAAARGRGLGERVVRRLVEHARGRGCYKVIINCTPELTGFYAKCGFVEKNVQMGLYF
Protein: E3 ubiquitin-protein ligase SspH1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SspH1) (Salmonella secreted protein H1) (Secreted effector protein SspH1) (D0ZVG2)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation. Can ubiquitinate ubiquitin, giving rise to polyubiquitin chains (in vitro). Polyubiquitinates host PKN1, leading to its proteasomal degradation. Down-modulates production of host pro-inflammatory cytokines by inhibiting NF-kappa-B-dependent gene expression; this depends only partially on its E3 ubiquitin-protein ligase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:10861017}. Host cytoplasm {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:10861017}. Host nucleus {ECO:0000269|PubMed:16611232}. Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 T3SS), and delivered into the host cytoplasm. Localizes predominantly to the host nucleus. {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:10861017}.
Interaction partners:
Sequence:
MFNIRNTQPSVSMQAIAGAAAPEASPEEIVWEKIQVFFPQENYEEAQQCLAELCHPARGMLPDHISSQFARLKALTFPAWEENIQCNRDGINQFCILDAGSKEILSITLDDAGNYTVNCQGYSEAHDFIMDTEPGEECTEFAEGASGTSLRPATTVSQKAAEYDAVWSKWERDAPAGESPGRAAVVQEMRDCLNNGNPVLNVGASGLTTLPDRLPPHITTLVIPDNNLTSLPELPEGLRELEVSGNLQLTSLPSLPQGLQKLWAYNNWLASLPTLPPGLGDLAVSNNQLTSLPEMPPALRELRVSGNNLTSLPALPSGLQKLWAYNNRLTSLPEMSPGLQELDVSHNQLTRLPQSLTGLSSAARVYLDGNPLSVRTLQALRDIIGHSGIRIHFDMAGPSVPREARALHLAVADWLTSAREGEAAQADRWQAFGLEDNAAAFSLVLDRLRETENFKKDAGFKAQISSWLTQLAEDAALRAKTFAMATEATSTCEDRVTHALHQMNNVQLVHNAEKGEYDNNLQGLVSTGREMFRLATLEQIAREKAGTLALVDDVEVYLAFQNKLKESLELTSVTSEMRFFDVSGVTVSDLQAAELQVKTAENSGFSKWILQWGPLHSVLERKVPERFNALREKQISDYEDTYRKLYDEVLKSSGLVDDTDAERTIGVSAMDSAKKEFLDGLRALVDEVLGSYLTARWRLN
Protein: Nuclear hormone receptor family member odr-7 (Odorant response abnormal protein 7) (P41933)
Organism: Caenorhabditis elegans
Function: Required for the function of one pair of chemosensory neurons called AWA neurons that are involved in chemotaxis to volatile odorants. Acts in a pathway that specifies olfactory neuronal fate. Regulates the transcription of olfactory signaling molecules such as odr-10 that specify AWA neuron identity and function. Represses the expression in AWA neurons of factors such as str-2 which specify AWC neuron identity.
Subcellular location: Nucleus. Cytoplasm, perinuclear region.
Interaction partners:
- LIM/homeobox protein lim-4
- Homeobox protein ceh-36
- Guanine nucleotide-binding protein alpha-17 subunit
- Serpentine receptor class r-10
- Transcription factor che-1
Sequence:
MIVPDTEGLLIYSYGLMYGSYCMACQMLIPHFQCIPGIFPNFRISTELIKTMTDKLEQPNNNVPQQPWGPFPPAFGGRPSGEQTDGNPGEFDNDAAHQQTAPFMTHFFPRIGLQFPDFTEYQRFNGFQRNAFFPNPFGSQFTGQAFAQSFPLHNSMTTMDGFNLTHAPHPFSTNTNSTKPKDIENTVQSTIKHSSENIQDKPPVLSVEYPVKYDSELKFDANVDFTAVPKQESSDDSTLKNLKKSDQQLQQPQQFTFPPPLLAEKSFEQPRMREDVLPFHPQFYPAPLDMGTNFKQEMRTPPIDGHIDYRKFDASGKRMEFQPPGALHDCQVCLSTHANGLHFGARTCAACAAFFRRTISDDKRYVCKRNQRCNNASRDGTGYRKICRSCRMKRCLEIGMLPENVQHKRNRRDSGSPPRKTPFDTFFNGFYPSFQPSGSAAQPITVSSSESPRHTTN
Protein: TRPM8 channel-associated factor 3 (Experimental autoimmune prostatitis antigen 2) (Q6QR59)
Organism: Mus musculus (Mouse)
Function: May play a role in the regulation of the cation channel TRPM8 activity.
Interaction partners:
Sequence:
MATTPDAAFETLMNGVTSWDLPKEPIPSELLLTGESAFPVMVNDKGQVLIAASSYGQGRLVVVSHESYLLHDGLVPFLLNVVKWLCPCPGAPIAVHSSLASLVNILGDSGINALVQPEPGEALGVYCIDAYNDALTEKLIQFLKNGGGLLIGGQALNWAAHHGHDKVLSIFPGNQVTSVAGVYFTDISANRDWFKVSKEIPNLRLYVQCEDELEDDQQQLLKGMSEIYIEAGVIPSQLLVHGQRAFPLGVDNSLNCFLAAARYGRGRVVLGGNESLILNQTMLPFVLNALHWLMGNQTGRIGLASDMKVLKSMLPNSSFQWSESELLTSDLSVFCCCSLANIDSEEVEEFVAEGGGLLIGAEAWSWGRRNPYSSCMTQYPDNIVLKRFGLGITSHVAQRGSFPFPNPEGTNYHFRRALSQFESVIYSRGSSLHESWLNKLSQDCFYMFQMTHQRISIYDSVKKHALKMIQSKDFPSVTEQYPIARGSSQAFLLSLAYELFKSGVDRSQLLPPPALLPPTESPITIKISTDNDNSWVSTGLYLPEGQVAQVLLPSEATHAKLKVLIGCHRDNISQARTYFRPPVMTYVYHLTSSQTSISWLYGGLLYIMVPNKYNQDNVSVTIRGAVSAPYFRLGKTTQEEWKNLITHSKAPWGELATDNIILTIPTVNLKELQDPYPLLQLWDKMVRAVAKLAARPFPFQRAERVVLDKQISFGFLHSGYPIMGLISIVEGIISEFKIRSHGIWGVIHELGHNHQKSGWTFPPHTTEALCNLWTIYVHETVLNIPREQAHPSLNPELRRQRIKYHLNKGAPLSNWIMWTALETYLQLQEGFGWEPFIQVFADYRTLSGLPQNNEDKMNLWVKKFSEAVHKNLAPFFEAWGWPVKYAVAKSLASLPEWQENPMKRYTAEGTEGRE
Protein: Tubulin beta-3 chain (Beta-3-tubulin) (Q6VAF8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Classical arabinogalactan protein 5
- microtubule-severing ATPase
- microtubule-severing ATPase
- Tubulin-specific chaperone A
- Tubulin-specific chaperone A
Sequence:
MREILHVQGGQCGNQIGSKFWEVVCDEHGIDPTGRYIGSSDLQLERVNVYYNEASCGRFVPRAVLMDLEPGTMDSVRTGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDAVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEADEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPRGLSMASTFVGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSGYQQIPGRYR
Protein: Growth arrest and DNA damage-inducible protein GADD45 alpha (DNA damage-inducible transcript 1 protein) (DDIT-1) (P24522)
Organism: Homo sapiens (Human)
Function: In T-cells, functions as a regulator of p38 MAPKs by inhibiting p88 phosphorylation and activity (By similarity). Might affect PCNA interaction with some CDK (cell division protein kinase) complexes; stimulates DNA excision repair in vitro and inhibits entry of cells into S phase.
Subcellular location: Nucleus {ECO:0000269|PubMed:7973727}.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 4
- Cyclin-dependent kinase 1
- Cellular tumor antigen p53
- G/T mismatch-specific thymine DNA glycosylase
- Proliferating cell nuclear antigen
- Large ribosomal subunit protein mL64
- G2/mitotic-specific cyclin-B1
- Cyclin-dependent kinase inhibitor 1
- Growth arrest and DNA damage-inducible protein GADD45 beta
- Aurora kinase A
Sequence:
MTLEEFSAGEQKTERMDKVGDALEEVLSKALSQRTITVGVYEAAKLLNVDPDNVVLCLLAADEDDDRDVALQIHFTLIQAFCCENDINILRVSNPGRLAELLLLETDAGPAASEGAEQPPDLHCVLVTNPHSSQWKDPALSQLICFCRESRYMDQWVPVINLPER
Protein: Alpha-1,2-galactosyltransferase (EC 2.4.1.-) (Q09174)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the O- and N-linked oligosaccharide modification of proteins transported through the Golgi stack. This occurs in cis Golgi where the enzyme transfers galactose from UDP-galactose to a variety of mannose based acceptors.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:7522655}; Single-pass type II membrane protein {ECO:0000269|PubMed:7522655}.
Interaction partners:
- Hydrolase C26A3.11
- UDP-galactose transporter
- Mannan polymerase complex subunit mnn9
- Mannan polymerase II complex anp1 subunit
- Uncharacterized protein C5H10.12c
- Uncharacterized protein C4C3.09
- Meiotically up-regulated gene 136 protein
- Initiation-specific alpha-1,6-mannosyltransferase
- Uncharacterized alpha-1,2-galactosyltransferase C8D2.17
- GTP-binding protein ypt5
Sequence:
MRFAPYLISAVVITTIILGGAWWTSAMDTKLQTKMKEIIDQHTSTWTPVVSSVTSTQTDTLRVTISEVVSVTATLTETFTATPTVTSVVHALATTDPHPDNSKIVILMGSNFQNDANSPLHPFAQSIIKNRREYAERHGYKFEFLDADAYASRVTGHLMPWVKVPMLQDTMKKYPDAEWIWWLDHDALVMNKDLNVVDHVLKHDRLNTILTREAEYKSGAGIPADGFRTPKDQDAKDVHFIISQDFNGINAGSLFIRNSEVGRWIVDLWFEPLYLDHIQGYAEQQAFSHMVFYHPQVYKHVGVVPLKAINAYDFDDNIWGYDDGDLCIHFAGCNYFKNCPEKFLKYAQILSSKQGSDWMSAQEKDHIQNLLKPSS
Protein: 2-methylcitrate synthase 1 (2-MCS) (MCS) (EC 2.3.3.5) (Citrate synthase 1) (CS) (EC 2.3.3.16) (Q8NSH7)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with propionyl-CoA but with a lower specificity.
Interaction partners:
- 2-methylcitrate dehydratase 1
- Probable 2-methylisocitrate lyase 1
- Phosphate acetyltransferase
- 2-oxoglutarate dehydrogenase E1/E2 component
- Uncharacterized protein involved in propionate catabolism
- Phosphoenolpyruvate carboxylase
- Malate dehydrogenase
- NAD-dependent aldehyde dehydrogenases
- methylmalonate-semialdehyde dehydrogenase
- Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit
Sequence:
MSDSQVRKGLNGVISDYTSISKVMPESNSLTYRGYAVEDLVENCSFEEVIYLLWFGELPTTEQLRTFNTTGRSYRSLDAGLISLIHSLPNTCHPMDVLRTAVSYMGTFDPDPFTRDADHIRSIGHNLLAQLPMVVAMDIRRRSGEEIIAPDHNKGIASNFLSMVFGNDDGSVANSADDIRDFERSLILYAEHSFNASTFSARVISSTRSDTYSAITGAIGALKGPLHGGANEFVMHTMLDIDDPNNAADWMGKALDRKERIMGFGHRVYKNGDSRVPSMEKSMRSLAARHRGQKWVHMYESMQEVMEARTGIKPNLDFPAGPAYYMLGFPVDFFTPLFVLARVSGWTAHIVEQFENNALIRPLSAYNGVEEREVVPISERT
Protein: Protein NUCLEAR FUSION DEFECTIVE 6, chloroplastic/mitochondrial (F4JX57)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASRFMSRSSVSSFKSAIRSSFRNSPIGTGSSPAAASSAGFRIPSKPAASPLPRFSFSRCPSELGCVQSLLPLHSTVAAARLTSCLSTTSRSSRALTQDGTFSPKVTRYIHEEYYY
Protein: Probable transcriptional regulator WhiBTM4 (Q9ZX29)
Organism: Mycobacterium phage TM4 (Mycobacteriophage TM4)
Function: A dominant-negative regulator of endogenous whiB2 expression. Low level expression in liquid culture in M.smegmatis leads to elongated and highly branched cells, with multiple nucleoids, similar to the effects seen in deletion experiments for whiB2 in M.smegmatis, as well as loss of acid-fastness. High level expression is lethal. Represses expression of endogenous whiB2. The apo-form binds to the whiB2 promoter found in M.tuberculosis. M.smegmatis cells expressing this protein will not grow on plates. Low level expression in M.smegmatis leads to superinfection exclusion, possibly via modification to the cell wall.
Subcellular location: Host cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MHMHMGGDPSAICAQTDPELWFPDKGQSTRDAKRMCMRCPLLDECRALALRDPHLVGVWGGLSAQERRRIRKGASA
Protein: Innexin (Q8I6U2)
Organism: Hirudo medicinalis (Medicinal leech)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}.
Interaction partners:
Sequence:
MDRLFKSVSSIREIKFRMDDDYVDRLSRQYTVVILICFGFLVSTKQFVGKPITCWCPAQFTSSHRDYTDAVCWFSNTYFLPLEDELKADHLSIHTNIRMISYYQWIPLILIFQALLAFVPCLLWRFVNKRSGVNMAAIMDAARHCSQAHYLEIREKAIRYIVNQMDRYLLAQREYRTGCVVRIKHVIAKFCCFVGGKLYGNYLISCYMVIKVLYLINALGQIFLLEAFLKIDFHLYGVHVMERLARGMDWSHSDKFPRVTLCEFEIRQHSRMHNYIVQCALTINLFNEKLFIFVWFWYVFLAFITAVNALRWLFRSLYWPGHVQYLRKQLRAFDATQREAGILAKFAENYLRRDGMFIIRLIGNNMGEVVAGEVICGLWNNYSMERRSIAEKSGRKALNKASRTTSGAHRMEVV