wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-2,8-sialyltransferase 8B (EC 2.4.3.-) (Sialyltransferase 8B) (SIAT8-B) (Sialyltransferase St8Sia II) (ST8SiaII) (Sialyltransferase X) (STX) (Q92186)
Organism: Homo sapiens (Human)
Function: May transfer sialic acid through alpha-2,8-linkages to the alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked oligosaccharides of glycoproteins and may be involved in PSA (polysialic acid) expression.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:9852130}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:9852130}. Cell membrane {ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:9852130}. Note=Also trafficks to the cell surface. {ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:9852130}.
Interaction partners:
- Neural cell adhesion molecule 1
- Syntaxin-2
- Syntaxin-1A
- Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase
- DnaJ homolog subfamily B member 11
Sequence:
MQLQFRSWMLAALTLLVVFLIFADISEIEEEIGNSGGRGTIRSAVNSLHSKSNRAEVVINGSSSPAVVDRSNESIKHNIQPASSKWRHNQTLSLRIRKQILKFLDAEKDISVLKGTLKPGDIIHYIFDRDSTMNVSQNLYELLPRTSPLKNKHFGTCAIVGNSGVLLNSGCGQEIDAHSFVIRCNLAPVQEYARDVGLKTDLVTMNPSVIQRAFEDLVNATWREKLLQRLHSLNGSILWIPAFMARGGKERVEWVNELILKHHVNVRTAYPSLRLLHAVRGYWLTNKVHIKRPTTGLLMYTLATRFCKQIYLYGFWPFPLDQNQNPVKYHYYDSLKYGYTSQASPHTMPLEFKALKSLHEQGALKLTVGQCDGAT
Protein: Nuclear pore complex protein Nup155 (Nucleoporin 155) (Q7ZW07)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
Sequence:
MPSSLGSSSPAAVLQEALENSSRLIDRHLQEDRCFPDLSELLNVPSHNMPSLSGVSDMDYPLQGPALISVPSLPELSSIRRVPLPPELVEQFGHMQCNCMMGVFPEISRAWLTIDNDVFMWNYEDGSDVAYFDGLSETILSVGLVKPKPGIFQPHIHFLLVLATPVDVVILGLSFPKVQTGLNDSTCGAMQLLPDPLYTIPTDNTYLLAITSTDTGRIFMAGKDGCLYEVAYQAEAGWFSQRCRKINHSKSSLSFLIPSLLQFSFSEDDPVVQIAVDNSRNILYTRSEKGVLQVYDLGADGQGMSRVAAISQSSIVSAAGNIARTIDRSVFKPIVQIAVIDRSESSDCQLLAVTHAGVRLYFSTIPFAPPNAKHVSARPSILALVHVRLPPGFSASSTLRKPAKVHKALYSRGVLLMAVSQTEDSDLLWCINHDSFPFKKPLMEAQMTVNVDGHSWALCSIEDKKSPRILTPLNKDLIPVTDSPLVVQQHNVPPQKFVLLSAQGSHIFHKLRPVDQLRHLLVSSAGGESEEIERFFKLHREEQACATALILACSNAACDREVSVWATRAFFRYGGEAQMRFPSALSAPSNVGPLFSSPVPGSPMPIGSPLPNPSFLATPAPGMFPPNVSTPYVPATPMSPGGAPITAVSSGPEVVFSGKHNGISIYFTRILGNIWDGSLAMETPINKGTQTVMILESTASSSDLELVLMQLQDLKEFLDKNSQFSPTSLGVANFSSPANLQQRLLGFMRPDGSSSQQMQQELQRKYHTEAQAYEKASLQAMQQLIHRSCQTLALWKLLCDHQFSLILSEMPKEFQDQMKAVSFKDVVVCGRELSGALITALINVYIKDSASVDTLSAHLRDICPLLYSSDDSICSKANELLQSSRQIQSKLEKERTLKESLRLYQQISHNTDLPLVCSQYRQVRFYEGVMELCLTAADKKDHQRLGLHFYRNGEPEEDASGQQAFQERLLCYKCITDTMQELVNQSKAAPQSPSVPKQPGPPVMTSDPNMLGNEDAAAHFEQMLGLAQRSQDELFHIALYNWLIQADLTDKLLEVNSPYLEDHLMHMIKQDQSKVRNMDLLWRYYEKNRSFGKAAHVLARLADMHSTEISLKQRLEYISRAILSAKSSSSVSSLGADGEFLHELEEKMEVVRIQVQIQETLRRQFSQHPSVQGAITQLDSELMDITKLYGEFADHFRLSECKLAIIHCAGHSDPILVHSLWQEIIEKELNDSVVMSPSDRMRAVSLKLVSLGKVYAGTPRYFPLDFLVKFLEQEVCRLNWDVGFVTFTMQEIGVQLPRLLEVYDQLFKTRDPCWQRLKKPLHLVECIHVLLSGYVDDPSRVPTYDRRRFTNACLDNICGYLVELQSLSPNAALQDIIRNFKSLQAKLEKLH
Protein: Deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) (Cyclobutane pyrimidine dimer photolyase) (CPD photolyase) (DNA photolyase PhrA) (Photoreactivating enzyme PhrA) (A9CJC9)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Photolyase involved in the repair of UV radiation-induced DNA damage. By using blue-light energy, catalyzes the photoreactivation of cyclobutane pyrimidine dimers (CPDs), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. Can repair CPD lesions in ssDNA as well as in dsDNA.
Interaction partners:
- 
Sequence:
MSLKTAPVIVWFRKDLRLSDNLALLAAVEHGGPVIPVYIREKSAGPLGGAQEWWLHHSLAALSSSLEKAGGRLVLASGDAERILRDLISETGADTVVWNRRYDPTGMATDKALKQKLRDDGLTVRSFSGQLLHEPSRLQTKSGGPYRVYTPFWRALEGSDEPHAPADPPKSLTAPKVWPKSEKLSNWKLLPTKPDWAKDFSDIWTPGETGALDKLDDFIDGALKGYEEGRDFPAKPATSLLSPHLAAGEISPAAVWHATKGLSRHIASNDISRFRKEIVWREFCYHLLFHFPELGEKNWNDSFDAFSWRDDEKSFKAWTRGMTGYPIVDAGMRQLWQHGTMHNRVRMIVASFLIKHLLIDWRKGEKWFRDTLVDADPASNAANWQWVAGSGADASPFFRIFNPILQGEKFDGDGDYVRRFVPELEKLERKYIHKPFEAPKDALKKAGVELGKTYPLPIVDHGKARERALAAYAAVKKTT
Protein: Tyrosine-protein phosphatase non-receptor type (EC 3.1.3.48) (A0A8I5YBL2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000927}.
Interaction partners:
Sequence:
MLRCGLHTTSSGTGYSAAVMTSRLRALGGRINNIRTSELPKEKTRSEVTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGLPCILHFRVRYFIPDPNTLQQEQTRHLYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHIGDFNSSIHHPGYLADSQFIPDQNDDFLSKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCKNLWKSCVEHHSFFQAKKLLPQEKNVLSQYWTLGSRNPKKSVNNQYCKKVIGGMVWNPVMRRSLSVERLETKSLPSRSPPITPNWRSPRLRHEIRKPRHSSADNLANEMTYITETEDVFYTYKGSLSPKDSDSEVSQNHSPHRGSLSENNPAQSCLTQKSSSSVSPCSNAPGSFSPDGVDQQFLEDYHKVTKGGSIEEASQYYCDKNDDGDGYLVLIRITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRESHSRELALVIRRKAVRSLAEIRSEDELSQLFPEAMFPACPEGGDSLEGSMELLKKGLESGTVLIQFEQLYRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEEGLVQTLDPS
Protein: Ras-related protein Rap-1b (EC 3.6.5.2) (GTP-binding protein smg p21B) (P61224)
Organism: Homo sapiens (Human)
Function: GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function.
Subcellular location: Cell membrane {ECO:0000269|PubMed:3141412}. Cytoplasm, cytosol {ECO:0000269|PubMed:3141412}. Cell junction {ECO:0000269|PubMed:20332120}. Note=May shuttle between plasma membrane and cytosol (PubMed:3141412). Presence of KRIT1 and CDH5 is required for its localization to the cell junction (PubMed:20332120). {ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:3141412}.
Interaction partners:
- Rap guanine nucleotide exchange factor 4
- Krev interaction trapped protein 1
- RAS guanyl-releasing protein 2
- Rap guanine nucleotide exchange factor 2
- Ral guanine nucleotide dissociation stimulator
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Rap guanine nucleotide exchange factor 3
- Talin-1
- RAS guanyl-releasing protein 1
- Ras association domain-containing protein 5
Sequence:
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL
Protein: Probable eukaryotic translation initiation factor 5-2 (eIF-5 2) (Q9S825)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]) (By similarity).
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit B
Sequence:
MALQNIGASNRNDAFYRYKMPKMVTKTEGKGNGIKTNIINNVEIAKALARPPSYTTKYFGCELGAQSKFDEKTGTSLVNGAHNTSKLAGLLENFIKKFVQCYGCGNPETEIIITKTQMVNLKCAACGFISEVDMRDKLTNFILKNPPEQKKVSKDKKAMRKAEKERLKEGELADEEQRKLKAKKKALSNGKDSKTSKNHSSDEDISPKHDENALEVDEDEDDDDGVEWQTDTSREAAEKRMMEQLSAKTAEMVMLSAMEVEEKKAPKSKSNGNVVKTENPPPQEKNLVQDMKEYLKKGSPISALKSFISSLSEPPQDIMDALFNALFDGVGKGFAKEVTKKKNYLAAAATMQEDGSQMHLLNSIGTFCGKNGNEEALKEVALVLKALYDQDIIEEEVVLDWYEKGLTGADKSSPVWKNVKPFVEWLQSAESESEEED
Protein: Cyclin dependent kinase 16 (E5RGN0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDRMKKIKRQLSMTLRGGRGIDKTNGAPEQIGLDESGGGGGSDPGEAPTRAAPGELRSARGPLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNIINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILVFCAMKPCSQPFRDR
Protein: Large ribosomal subunit protein eL15z (60S ribosomal protein L15-1) (O23515)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS8z
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein uL18z
- Large ribosomal subunit protein uL22y
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Large ribosomal subunit protein eL13z
- Large ribosomal subunit protein eL8z
- Large ribosomal subunit protein uL4z
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL24z
Sequence:
MGAYKYVSELWRKKQSDVMRFLQRVRCWEYRQQPSIVRLVRPTRPDKARRLGYKAKQGFVVYRVRVRRGGRKRPVPKGIVYGKPTNQGVTQLKFQRSKRSVAEERAGRKLGGLRVVNSYWLNEDSTYKYYEIILVDPAHNAVRNDPRINWICNPVHKHRELRGLTSEGKKNRGLRGKGHNNHKNRPSRRATWKKNNSLSLRRYR
Protein: X-linked retinitis pigmentosa GTPase regulator (mRpgr) (Q9R0X5)
Organism: Mus musculus (Mouse)
Function: Could be a guanine-nucleotide releasing factor (By similarity). Plays a role in ciliogenesis (By similarity). Probably regulates cilia formation by regulating actin stress filaments and cell contractility (By similarity). May be involved in microtubule organization and regulation of transport in primary cilia (By similarity). Plays an important role in photoreceptor integrity. Isoform 5 may play a critical role in spermatogenesis and in intraflagellar transport processes.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:15772089, ECO:0000269|PubMed:16043481, ECO:0000269|PubMed:20007830, ECO:0000269|PubMed:9677393}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q92834}. Cell projection, cilium {ECO:0000269|PubMed:29899041, ECO:0000269|PubMed:38536817}. Note=In the retinal photoreceptor cell layer, localizes at the connecting cilium (PubMed:29899041, PubMed:38536817). Colocalizes with WHRN in the photoreceptor connecting cilium (PubMed:22323458). Colocalizes with CEP290 in the photoreceptor connecting cilium (PubMed:16632484). Colocalizes with RPGRIP1 in the photoreceptor connecting cilium (PubMed:15772089). Colocalizes with RPGR at the primary cilia of epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q9N1T2, ECO:0000269|PubMed:15772089, ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:22323458, ECO:0000269|PubMed:29899041, ECO:0000269|PubMed:38536817}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:20007830}.
Interaction partners:
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- Centrosomal protein of 290 kDa
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- IQ calmodulin-binding motif-containing protein 1
- Protein fantom
- Nephrocystin-4
- Intraflagellar transport protein 88 homolog
- Nephrocystin-1
- Spermatogenesis-associated protein 7 homolog
- E3 SUMO-protein ligase RanBP2
Sequence:
MAESESLVPDTGAVFTFGKTKFAENIPSKFWFKNDIPICLSCGDEHTAIVTGNNKLYMFGSNNWGQLGLGSKAAIIKPTCIKALKPEKVKLAACGRNHTLVSTDTGGVYAAGGNNEGQLGLGDTDDRDTFHQIVFFTPADTIKQLSAGANTSAALTEDGKLFMWGDNSEGQIGLEDKSNVCIPHEVTVGKPISWISCGYYHSAFVTMDGELYTFGEPENGKLGLPNELLMNHRSPQRVLGIPERVIQVACGGGHTVVLTEKVVYAFGLGQFGQLGLGTFLFETSEPKIIERIKDQKICHISCGENHTALMTELGLLYTFGDGRHGKLGLGMENFTNQFFPTLCSNFLRFAVQLIACGGCHMLVFATPRLGTIDEPKFEDVYEPYISTGSFSINDLSPRSSLNRSLSARLRRRERERPPCSASMVGTLPPLEGTSASTSAYFYPSSPPFHLSVNNYPEKSPSESMEPLDSDYFEDKMNKDTETENSSAVDSENFGETNDILNMTHMMTTSSNEKLLDFSPIQKQQNQDTFEKVMESTPCTENEDSYEYEEMSKIKEVTVYKQYLAKGIYMIRPAEILEAFSDEEVGNGLDQVEEPRVFTDGKGLQSKQVGKESDEEIVSEKKTEVMEVADVKKIRESEENSKSDSLFDDLPDKTMNSESEDNKDIAEERRSSEQNMTFDSETELVEEPDSYMECERHSEQDSAEELEQPKLVEYSSEEKDEKDEKDDDEVETENLWYDRNCTEQETENVFRATRFFPKFDLKHDHLSGIPEEQEGPEDSEGNVVVEQVVQAQKENLEFEGDRKEAKAEAPSDVITEKEAPQLSETVKPEEGEMDEEISILNVEDTVEEERKEGEKEIVEEGSIPETEGSETIDITDEKLDEVLKEEDSASLLQRALREYNENPKGHMYDRVKSSSSEILGGNDPTSKDIKKAKKISFFNRMSLTGQKLMQNTNDPLPEIKPIGDQIALQSDKKDANQNHMGQNLQDSTTPNMEGKSKSCTIL
Protein: RPM1 interacting protein 3 (F4KD92)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGITYLHISVATTALSFVGLQVWTELSLDRLRADGIITKNISLGNSENTLELLLSSHTTIALLASFVLNIYILLVLSLKTLFFGDLYAIETRKLVERLANYIIYKGTFLPFVVPRTVFQGVLWTIWLTVLCTLKMFQALARDRLDRLNASPSSTPWTYFRVYSALFMVLSTDLCWIKLSLMIYNTVGSSVYLLLLFEPCGIAFETLQALLIHGFQLLDMWINHLAVKNSDCQRSKFYDSMTAGSLLEWKGLLNRNLGFFLDMATLVMALGHYLHIWWLHGMAFHLVDAVLFLNIRALLSSILKRIKGYIKLRVALGALHAALLDATSEELRDYDDECAICREPMAKAKRLHCNHLFHLGCLRSWLDQGLNEVYSCPTCRKPLFVGRTESEANPSRGEVSSDEHLARQFERQNNSVHALTTGMFPTETPNFTESDPWRLAFLNGISSSHLFLMPYRNSEVDPSWLQTWSDQGVDVVGSSAGSRSVGLGQVQLMMRHLASVGEGSAQTTLDDASWGLWPMNPSQASTSSTYVPPGAGGRTGGLHLRTVSRAANNMASILAMAETVREVLPHVPDEIIFQDLQRTNSVSVTVNNLLQM
Protein: Genome polyprotein 2 (Q9IWA2)
Organism: Wheat yellow mosaic virus
Interaction partners:
Sequence:
MASTSSNIYYMDGDPRWPTRDPGAPITRDALPQRISEAWNTVIIRHMLSDGDDQDSILGRDGLPATRFNAYSGLLPTFVQSLGLPVNRLRLHAPVSAIEAPLCVDTSYVVHGLYMSNGTHAYEATRLQPVRTFIAFNFANGYCYLNFFIPMSFQISGANVEAFSRFIEQLPDVLGAYPTLGNLLKTAIYLMRIFPEILDAPIPIIAKRPGVAQFHVTDNRGLPPTWFSMMCGSVSSFVTLLLHNLGNELLNGIVGSAEETGQYTNWNFEHDHWITSKFITLEDYYTTMSSALNVDYRTKGGCEALYDLFSDLGYSNMVRRRKRFPESTQGLSSFYFHLSDRAPFEAIQAFLSVLREIINSDDYDSPYRNIRTRLINLSSLPYDNPDACFTRNIFEDENKLVWNFEFYKVVTIANNATADHETFFRSHVLPFRSFVKEASNDRYNLPSPFEITTPVKAAPNEAPLVESTTESATTNPSVWWQVAVGLITAILTALLVFFWRCFLSAKKIKFRKKDTFPWFGYSHGGPPPSPPGGPPPGSPRDASYQQVPRTVVRDLSFDEDDDLQSVDLEEAGIRFKSLITTIERGNLQELQAVIPEHISDLNVLQSSAHGSGFYTMVSLYLSTLGDAITAFEQRNDISPATIQLLRTLELQLEARHLRFNEAGTPTHILQRSISASVGRAIIRLTQSALLASGEGFRTRMASTLQRIADERSNNLTSFDARALDMTSELFQSIEAALDSDSSDIVPLLANAEASLQVYNNFFGVNYVSTTLLALRRELILRSAEGRVGEQPTGISEESNEELVQKSMQKLDKEIELFQAQIDSQRRVAEITESSNLRENILQPINTVANIAMAGAFLRGGARSRLPGVLPQAQPHTQAFRPFTGRAHHLTTTGRVQRFLRRPGH
Protein: Inner membrane protein YdgC (P0ACX0)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YjbT
- Putative dehydratase subunit YjiM
- UPF0509 protein YciZ
Sequence:
MGLVIKAALGALVVLLIGVLAKTKNYYIAGLIPLFPTFALIAHYIVASERGIEALRATIIFSMWSIIPYFVYLVSLWYFTGMMRLPAAFVGSVACWGISAWVLIICWIKLH
Protein: Succinate dehydrogenase assembly factor (F4KBT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MATRKALINVHRIIRSTAVVGRSSIIPAAANRSYPIIFRNGVDLGARFFCENTASAQNFDIDLSNEENKRRTINRLLYRSKQRGFLELDLVLGNWVEENVNSMDENGVKSLIHVLNLVESEATKLLENPDLWKWLTEQEQPPEAVSSNPVFSALHEKVMKNLNKHAAPETRAAAGQPWVRGWDDFKRGRDAPISGNQ
Protein: Dihydroorotate dehydrogenase (fumarate) (DHOD) (DHODase) (DHOdehase) (EC 1.3.98.1) (Dihydroorotate oxidase) (Q57U83)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Orotidine 5'-phosphate decarboxylase
- Predicted S. cerevisiae Got1 homologue
- Dihydroorotase, putative
- GMP synthase
- Nitrate reductase, putative
- Transmembrane protein
- Guanine deaminase
- Inosine-5'-monophosphate dehydrogenase
- aspartate carbamoyltransferase
- Carbamoyl phosphate synthase arginine-specific large chain
Sequence:
MSLKVNILGHEFSNPFMNAAGVLCTTEEDLRRMTESESGSLIGKSCTLAPRTGNPEPRYFGLPLGSINSMGLPNLGVDFYLSYAAQTHDYSRKPLFLSMSGLSVEESVEMVKKLAPITKEKGTILELNLSCPNVPGKPQVGYDFDTTRTYLQKVSEAYGLPFGVKMPPYFDIAHFDMAAAVLNDFPLVKFITCVNSIGNGLVIDPANETVVIKPKQGFGGLGGKYVLPTALANVNAFFRRCPDKLVFGCGGVYSGEEAFLHILAGASMVQVGTALHDEGPIIFARLNKELQEIMTNKGYKTLDEFRGRVKTMD
Protein: Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma (PI3K-C2-gamma) (PtdIns-3-kinase C2 subunit gamma) (EC 2.7.1.137) (EC 2.7.1.154) (Phosphoinositide 3-kinase-C2-gamma) (O75747)
Organism: Homo sapiens (Human)
Function: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers (By similarity). May play a role in SDF1A-stimulated chemotaxis (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:O70167}; Peripheral membrane protein {ECO:0000250|UniProtKB:O70167}.
Interaction partners:
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Inositol polyphosphate 4-phosphatase type II
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Inositol polyphosphate-4-phosphatase type I A
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
Sequence:
MAYSWQTDPNPNESHEKQYEHQEFLFVNQPHSSSQVSLGFDQIVDEISGKIPHYESEIDENTFFVPTAPKWDSTGHSLNEAHQISLNEFTSKSRELSWHQVSKAPAIGFSPSVLPKPQNTNKECSWGSPIGKHHGADDSRFSILAPSFTSLDKINLEKELENENHNYHIGFESSIPPTNSSFSSDFMPKEENKRSGHVNIVEPSLMLLKGSLQPGMWESTWQKNIESIGCSIQLVEVPQSSNTSLASFCNKVKKIRERYHAADVNFNSGKIWSTTTAFPYQLFSKTKFNIHIFIDNSTQPLHFMPCANYLVKDLIAEILHFCTNDQLLPKDHILSVCGSEEFLQNDHCLGSHKMFQKDKSVIQLHLQKSREAPGKLSRKHEEDHSQFYLNQLLEFMHIWKVSRQCLLTLIRKYDFHLKYLLKTQENVYNIIEEVKKICSVLGCVETKQITDAVNELSLILQRKGENFYQSSETSAKGLIEKVTTELSTSIYQLINVYCNSFYADFQPVNVPRCTSYLNPGLPSHLSFTVYAAHNIPETWVHSYKAFSFTCWLTYAGKKLCQVRNYRNIPDKKLFFFLVNWNETINFPLEIKSLPRESMLTVKLFGIACATNNANLLAWTCLPLFPKEKSILGSMLFSMTLQSEPPVEMITPGVWDVSQPSPVTLQIDFPATGWEYMKPDSEENRSNLEEPLKECIKHIARLSQKQTPLLLSEEKKRYLWFYRFYCNNENCSLPLVLGSAPGWDERTVSEMHTILRRWTFSQPLEALGLLTSSFPDQEIRKVAVQQLDNLLNDELLEYLPQLVQAVKFEWNLESPLVQLLLHRSLQSIQVAHRLYWLLKNAENEAYFKSWYQKLLAALQFCAGKALNDEFSKEQKLIKILGDIGERVKSASDHQRQEVLKKEIGRLEEFFQDVNTCHLPLNPALCIKGIDHDACSYFTSNALPLKITFINANPMGKNISIIFKAGDDLRQDMLVLQLIQVMDNIWLQEGLDMQMIIYRCLSTGKDQGLVQMVPDAVTLAKIHRHSGLIGPLKENTIKKWFSQHNHLKADYEKALRNFFYSCAGWCVVTFILGVCDRHNDNIMLTKSGHMFHIDFGKFLGHAQTFGGIKRDRAPFIFTSEMEYFITEGGKNPQHFQDFVELCCRAYNIIRKHSQLLLNLLEMMLYAGLPELSGIQDLKYVYNNLRPQDTDLEATSHFTKKIKESLECFPVKLNNLIHTLAQMSAISPAKSTSQTFPQESCLLSTTRSIERATILGFSKKSSNLYLIQVTHSNNETSLTEKSFEQFSKLHSQLQKQFASLTLPEFPHWWHLPFTNSDHRRFRDLNHYMEQILNVSHEVTNSDCVLSFFLSEAVQQTVEESSPVYLGEKFPDKKPKVQLVISYEDVKLTILVKHMKNIHLPDGSAPSAHVEFYLLPYPSEVRRRKTKSVPKCTDPTYNEIVVYDEVTELQGHVLMLIVKSKTVFVGAINIRLCSVPLDKEKWYPLGNSII
Protein: Protein BTG4 (BTG family member 4) (Protein PC3b) (O70552)
Organism: Mus musculus (Mouse)
Function: Adapter protein that bridges CNOT7, a catalytic subunit of the CCR4-NOT complex, to EIF4E, and facilitates maternal mRNAs decay during the maturation of oocytes and in the fertilized egg. It is therefore required for the maternal-zygotic transition (MZT), zygotic cleavage and initiation of embryonic development.
Interaction partners:
- CCR4-NOT transcription complex subunit 7
- CCR4-NOT transcription complex subunit 8
- Embryonic polyadenylate-binding protein 2
- CCR4-NOT transcription complex subunit 6-like
Sequence:
MRDEIATAVFFVTRLVKKHEKLSTQQIETFALKLMTILFEKYRGHWHPDCPSKGQAFRCIRINNNENKDPVLERACAESNVNFFHLGLPKEMTIWVDPYEVCCRYGEKKHPFTIASFKGRWENWELAQHVSCAVNRATGDCSSGTSSDEESCSREAQIIPKVNNPKSVYQVENFKQSLQPWFCLPRRKHLADGRGFLPGAACHPVPKSSKWCRPASRRVDRYHWVNAQLFSGQTAPGEPGEEALSSLKQK
Protein: TPR repeat-containing thioredoxin TTL4 (Tetratricopeptide repeat thioredoxin-like 4) (Q84JR9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in osmotic and salt stress tolerance. May play a role in the control of meristematic cell size during osmotic stress.
Interaction partners:
- Chromatin structure-remodeling complex protein SYD
- Probable CCR4-associated factor 1 homolog 7
- Endoplasmin homolog
- SH3 domain-containing protein
- Heat shock protein 90-1
- Heat shock protein 90-4
- Heat shock protein 90-3
- Heat shock protein 90-5, chloroplastic
- Heat shock protein 90-2
- Heat shock protein 90-6, mitochondrial
Sequence:
MSHYRRHSLEPSITSKFRDSLSFQRDDDVINKPDFRELDFGSPLRPRGSSSAAATPAASGSSSSSSGSASGKPAVTSQFARRSHSGELSGLSQTSPVKPGSVNRNLKPGHRRSASAGTPLIYSGLGFSPVNNNNNSSRGGGSGATSPNPGVLPTGNICPSGRILKTGMATRASVRPETLCTGTANYGHGNIIRTGGKVSHATKAAAEMSDSEEVKKAGNVMYRKGNYAEALALYDRAISLSPENPAYRSNRAAALAASGRLEEAVKECLEAVRCDPSYARAHQRLASLYLRLGEAENARRHLCVSGQCPDQADLQRLQTLEKHLRLCTEARKIGDWRTVISEIDAAIANGADSSPQLVACKAEAFLRLHQIKDSDLCISSIPRLDHHHTQPPEKLFGIVCDAYVLCVQAQVDMALGRFENAIVKVERAMTIDHSNSPEVVSVLNNVKNVAKARTRGNELFSSGRYSEASVAYGDGLKLDAFNSVLYCNRAACWFKLGMWEKSVDDCNQALRIQPSYTKALLRRAASYGKLGRWEDAVRDYEVLRKELPGDSEVAESLQRARNALSNKSEEPKYLGFNNEVEEVSTLDKFKTATSLPGISVFHFKSSSNRQSEAISPFVNTLCLRYPLVHFFKVDVEESLALAKAESIKKIPTFKIYKKGEKVKEMVCPSHQLLEDSVTHFLL
Protein: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase Pin1) (PPIase Pin1) (Rotamase Pin1) (Q13526)
Organism: Homo sapiens (Human)
Function: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN. May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR). Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and expression of pro-inflammatory genes in dendritic cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:16476580, ECO:0000269|PubMed:23623683}. Nucleus speckle {ECO:0000269|PubMed:21497122}. Cytoplasm {ECO:0000269|PubMed:21497122}. Note=Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122). {ECO:0000269|PubMed:16476580}.
Interaction partners:
- Interferon regulatory factor 3
- Homeodomain-interacting protein kinase 2
- Cellular tumor antigen p53
- DNA-directed RNA polymerase II subunit RPB1
- 14-3-3 protein sigma
- Myc proto-oncogene protein
- Protein PML
- Serine/threonine-protein kinase PLK1
- Neutrophil cytosol factor 1
- Neutrophil cytosol factor 4
Sequence:
MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE