wanglab/gogpt-training-data huggingface dataset:
Protein: Nicotinic acetylcholine receptor alpha6, isoform D (Q7KTF7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MDSPLPASLSLFVLLIFLAIIKESCQGPHEKRLLNHLLSTYNTLERPVANESEPLEVKFGLTLQQIIDVDEKNQILTTNAWLNLDEKNQLLITNLWLSLEWNDYNLRWNETEYGGVKDLRITPNKLWKPDVLMYNSADEGFDGTYHTNIVVKHNGSCLYVPPGIFKSTCKIDITWFPFDDQHCEMKFGSWTYDGNQLDLVLNSEDGGDLSDFITNGEWYLLAMPGKKNTIVYACCPEPYVDITFTIQIRRRTLYYFFNLIVPCVLISSMALLGFTLPPDSGEKLTLGVTILLSLTVFLNLVAETLPQVSDAIPLLGTYFNCIMFMVASSVVLTVVVLNYHHRTADIHEMPPWIKSVFLQWLPWILRMGRPGRKITRKTILLSNRMKELELKERSSKSLLANVLDIDDDFRHTISGSQTAIGSSASFGRPTTVEEHHTAIGCNHKDLHLILKELQFITARMRKADDEAELIGDWKFAAMVVDRFCLIVFTLFTIIATVTVLLSAPHIIVQ
Protein: Dopamine dehydroxylase (EC 1.1.-.-) (A0A369NIV7)
Organism: Eggerthella lenta (Eubacterium lentum)
Function: Involved in drug metabolism, as part of an interspecies gut bacterial pathway for Levodopa (L-dopa) metabolism, acting on dopamine produced by Enterecoccus L-dopa decarboxylase. Removes the para hydroxyl group of dopamine to produce m-tyramine (3-tyramine). It is possible that dopamine dehydroxylation influences the multiple side effects of L-dopa administration linked to dopamine production in the treatment of Parkinson's disease.
Interaction partners:
Sequence:
MGNLTMSRRTFVKTAAITGAAAAAFGASTHTALAEETYSSVSGNDTVAVKTCCRGCGKMECGVKVIVQNGRAIRVEGDEGAFQSMGNCCTKSQSSIQAAYHPDRLHYPMKRTNPKGEEPGWQRISWDEAMQSIVDNFMDIKAKHGGEAIACQVGTSRIWCMHSESILKNMLETPNNVEAWQICKGPRHFATTMVSQFAMSWMETITRPKVYVQWGGASELSNYDDSCRTTVDVASRADVHISVDPRMANMGKEADYWQHLRPGTDGALALAWTNVIIEKKLYDELYVKKWTNAPFLVCEDMEPSGFPTVRTDGSYWDVKTALLKESDIKEGGSPYKFLVYDNNWEKLKAEGVEHEYGAFTWFNADQEGVIDETGGFWEGENYDSEKARQGREAAQDNLLPGQTQGWLPDPMPFDPAIDPALEGEFEITLKDGKTVKVKPVWEHYKARAAEYKPEVAAEITGIPASEIEAAATAYGTRIDPSTGYGNGGIQYMLAVEHFCSAIQNCRAFDNLVGITGNMDTPGGNRGPTIVPIDGDLQGFSAWAPGATTPPEEVNRKQIGIDKFPLLGWWQYWCDSHSLWDAVITGDPYPVRALWNESGNFMSQTNTTRAWEALCSLDFYVDLNLWHTPQNDTADIILPVAHWIELNSPRASQGSAGAMGATVKCVQPPAEAKYDPEIVMDLARRMNWKWTDEPGNEWPDINWQLDDSIKLLTDDELTYTTWHVENGKPTFERHGVPMAEVTPKYKTWDEYVKAFQEHGWWQAKDIEPRNWGTYRRYQTGAMRARDRVWGRLDYTAGKGIGDWKPGWFTPTMKQEIWSTVMESHHPDHPEWRLPTYTEPPHGPKDGDRIKEYPLTATTGRRIPVYFHSEHRQLPWCRELWPVPRVEINPKTAAEYGIEQGDWVWIETEWGKIREVADLYYGVKEDVINLEHTWWYPEVKDAGHGWQFSQVNQLIDHYAQDPHSGTSNLRAYQVKIYKATPENSPFNNPVPCDSTGTPIIHTSDDPRLKEWLPTYEGRE
Protein: 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase (D8FRQ0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLYNMRDKSLEAINQKYGLKTDQIKCYFHYQPSFYHLHVHFINLKYDAPASTTMSAILLDDVINNLELNPEHYKKSTLTFTRKNGDKLMEMFREALKN
Protein: Mitochondrial import inner membrane translocase subunit TIM22 (Q382K7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU367038}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU367038}.
Interaction partners:
- J domain-containing protein
- Pre-mRNA-splicing factor SLU7
- Mitochondrial carrier protein, putative
- GrpE protein homolog
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MTTLLDPQPQIDPSQKAMMVLKDSTITPAAMNVVGGYVMGFGFSLFGAMISAESTTQRMGTADFFRYSLKTAHRLGFSFAYFGFLFGGIEVALEKRRGRKDVWNATLSGGLLGGVYGCRYYKAPGLVGGTLGGAAVSLMLERVMDALGLAQR
Protein: Leghemoglobin reductase (EC 1.6.2.6) (Ferric leghemoglobin reductase) (FLbR) (Q9SPB1)
Organism: Vigna unguiculata (Cowpea)
Function: Reduces ferric leghemoglobin (Lb) to ferrous Lb.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:10729615}.
Interaction partners:
Sequence:
MAMASLARRKAYAVVSSSRSSVFLTSLRGFASGSDENDVVVIGGGPGGYVAAIKASQLGLKTTCIEKRGTLGGTCLNVGCIPSKALLHSSHMYHEAKHSFANHGIKLSSVEVDLAGMMAQKDKAVSNLTKGIEGLFKKNKVNYVKGYGKFVSPSEVSVDTIDGGNTVVKGKHIIIATGSDVKSLPGVTIDEKKIVSSTGALALTEIPKKLVVIGAGYIGLEMGSVWGRLGSEVTVVEFASDIVPTMDAEVRKQFQRSLEKQGMKFQLKTKVVGVDTSGDGVKLTLEPAAGGDQTILETDVVLVSAGRTPFTAGLGLDKIGVETDKIRRILVNERFTTNVSGVYAIGDVIPGPMLAHKAEEDGVACVEFIAGKVGHVDYDKVPGVVYTTPEVAYVGKTEEQVKALGVEYRVGKFPFMANSRAKAIDNAEGLVKILAEKETDKILGVHIMAPNAGELIHEAAIALQYDASSEDIARVCHAHPTMSEAVKEAAMATYDKPHSHMKSWLLLHSLLFIFVQQFTMTWR
Protein: Carbonic anhydrase 14 (A0A8I6GAJ9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLFFVLLLKVTWILAADGGRYIWVCPHGQDHWPASYPECGGNAQSPIDIQTDGVIFDPDLPTVQPHGYDQLGTEPLDLHNNGHTVQLSLPPTLHLGGLPRKYTAAQLHLHWGQKGTLKGSEHQINSEATAAELHVVHYDSESYGSLSEAAQKPQGLAVLGILIEVGETENPAYDHILSHLHEVRYKDQKTSVPPFNVRELLPQQLEQFFRYNGSLTTPPCYQSVLWTVFNRRAQISMGQLEKLQETLSSTEEDPSEPLVQNYRVPQPLNQRTIFASFIQGDLQGEMLGLGMGISAGCLCLLLTIYFIAQKIRRKRLGNRKSVVFTSARATTEA
Protein: Transcription factor Spi-B (Q01892)
Organism: Homo sapiens (Human)
Function: Sequence specific transcriptional activator which binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a lymphoid-specific enhancer. Promotes development of plasmacytoid dendritic cells (pDCs), also known as type 2 DC precursors (pre-DC2) or natural interferon (IFN)-producing cells. These cells have the capacity to produce large amounts of interferon and block viral replication. May be required for B-cell receptor (BCR) signaling, which is necessary for normal B-cell development and antigenic stimulation.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:12393575}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:12393575}.
Interaction partners:
- Interferon regulatory factor 4
- POU domain class 2-associating factor 1
- Interferon regulatory factor 8
- Interferon regulatory factor 7
- Paired box protein Pax-5
- B-lymphocyte antigen CD19
- Zinc finger protein Aiolos
- Tumor necrosis factor receptor superfamily member 13C
- Transcription factor COE1
Sequence:
MLALEAAQLDGPHFSCLYPDGVFYDLDSCKHSSYPDSEGAPDSLWDWTVAPPVPATPYEAFDPAAAAFSHPQAAQLCYEPPTYSPAGNLELAPSLEAPGPGLPAYPTENFASQTLVPPAYAPYPSPVLSEEEDLPLDSPALEVSDSESDEALVAGPEGKGSEAGTRKKLRLYQFLLGLLTRGDMRECVWWVEPGAGVFQFSSKHKELLARRWGQQKGNRKRMTYQKLARALRNYAKTGEIRKVKRKLTYQFDSALLPAVRRA
Protein: Transforming growth factor-beta-induced protein ig-h3 (Beta ig-h3) (Kerato-epithelin) (RGD-containing collagen-associated protein) (RGD-CAP) (O11780)
Organism: Sus scrofa (Pig)
Function: Plays a role in cell adhesion (By similarity). May play a role in cell-collagen interactions.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q15582}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:9061001}. Note=May be associated both with microfibrils and with the cell surface. {ECO:0000250|UniProtKB:Q15582}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
Sequence:
MALLGRLLPLALALALGPAATHAGPAKSPYQLVLQHSRLRGRQHGPNVCAVQKLIGTNKKYFTNCKQWYQRKICGKSTVISYECCPGYEKVPGEKGCPAVLPLSNLYETLGVVGSTTTQLYTDRTEKLRPEMEGPGSFTIFAPSNEAWASLPAEVLDSLVSNVNIELLNALRYHMVDRRVLTDELKHGMALTSMYQNSNIQIHHYPNGIVTVNCARLLKADHHATNGVVHLIDKVISTVTNNIQQIIEIEDTFETLRAAVAASGLNTLLEGDGQYTLLAPSNEAFEKIPAETLNRILGDPEALRDLLNNHILKSAMCAEAIVAGLSLETLEGTTLEVGCSGDMLTINGKPIISNKDVLATNGVIHFIDELLIPDSAKTLFELAAESDVSTAVDLFRQAGLGSHLSGNERLTLLAPMNSVFKDGTPRIDARTKNLLLNHMIKDQLASKYLYHGQTLDTLGGKKLRVFVYRNSLCIENSCIAAHDKRGRYGTLFTMDRMLTPPMGTVMDVLKGDNRFSMLVAAIQSAGLTETLNREGVYTVFAPTNEAFQALPLGERNKLLGNAKELANILKYHVGDEILVSGGIGALVRLKSLQGDKLEVSSKNSLVTVNKEPVAEADIMATNGVVHTINTVLRPPANKPQERGDELADSALEIFKQASAFSRATQSSVKLAPVYQRLLERMKH
Protein: Methylesterase 4 (AtMES4) (EC 3.1.1.-) (Alpha/beta fold hydrolase/esterase 4) (O80474)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methylesterase shown to have carboxylesterase activity and methyl salicylate (MeSA) esterase activity in vitro.
Interaction partners:
- Probable UDP-arabinopyranose mutase 4
- Probable carboxylesterase 1
- Transcription repressor MYB5
Sequence:
MEKNNKKRFVLVHGLCHGAWCWYKVKTHLEAVGHCVTAVDLAASGINMTRLEEIQTLKDYCKPLLELLNSLGSDDDKVILVAHSMGGIPAALASDIFPSKIATIVFLTAFMPDTRNLPAYVYQKLIRSVPQEGWLDTVFGTYGKHECPLEFALFGPKFMAKNLYQLSPVQDLELAKMLVRVNPIITNNLAGTRSFSEEGYGTVTRIYIVCGEDMAVPEDYQWWMIKNFPPKEVMEIKCADHMAMFSKPHKLCALLVEIACKYA
Protein: Uncharacterized protein (Q389B3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MANFVRKGAMGRINAERLYAFNKTLKKDTLRERGYWEVSKDSHPINRWSYRRWKQRKEELSVFEDKLEKVPVDQKFKIKKLLTVANISVLGPIMILLYFAFCYLRYRLWGITPIDGAGAVVRGVQNLPRPPGY
Protein: Actinin alpha 4 (H7C144)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVGTLRPDEKAIMTYVSCFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKKQTGSMDSDDFRALLISTGYSLGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL
Protein: 78 kDa glucose-regulated protein (Binding-immunoglobulin protein) (Heat shock protein 70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (B5X397)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- DnaJ homolog subfamily C member 10
- DnaJ homolog subfamily C member 10
- Hypoxia up-regulated protein 1
- Hypoxia up-regulated protein 1
- Translocation protein SEC63 homolog
- DnaJ homolog subfamily B member 11
- Mesencephalic astrocyte-derived neurotrophic factor-like
- ARMET
- Nucleotide exchange factor SIL1
- Eukaryotic translation initiation factor 2-alpha kinase 3
Sequence:
MRLLCVVLLVASSVFADDEDKRESVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTAEGERLIGDAAKNQLTSNPENTVFDAKRLIGRAWTDSAVQHDIKYFPFKVIEKKSKPHIQVDIGGGQLKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGVIAGLNVMRIINEPTAAAIAYGLDKKDGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRGLSAQHQARIEIESFFDGEDFSETLTRAKFEELNMDLFRSTMKPVQKVMEDSDLKKTDIDEIVLVGGSTRIPKVQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGEEDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEDIERMVNDAERFADEDKKLKERIDARNELESYAYSLKNQIGDKEKLGGKLSAEDKETIEKAVEEKIEWMESHQEAELEDFQAKKKELEEVVQPIVSKLYGSAGGPPPEGGEEGEADQGDRDEL
Protein: Tight junction protein 2 (Tight junction protein ZO-2) (Zona occludens protein 2) (Zonula occludens protein 2) (Q95168)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Plays a role in tight junctions and adherens junctions (By similarity). Acts as a positive regulator of RANKL-induced osteoclast differentiation, potentially via mediating downstream transcriptional activity (By similarity).
Subcellular location: Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9Z0U1}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Cell junction, tight junction {ECO:0000269|PubMed:39112699}. Note=Also nuclear under environmental stress conditions and in migratory endothelial cells and subconfluent epithelial cell cultures. Localizes to tight junctions during initial stages of their formation (PubMed:39112699). {ECO:0000250, ECO:0000269|PubMed:39112699}.
Interaction partners:
- Tight junction protein 1
- Afadin, adherens junction formation factor.
- F11 receptor.
- Occludin
- Rap guanine nucleotide exchange factor 2
- WW domain containing transcription regulator 1.
- Claudin
- Claudin
- Gap junction alpha-1 protein
- Claudin
Sequence:
MEELIWEQYTVTLQKDSKRGFGIAVSGGRDNPHFENGETSIVISDVLPGGPADGLLQENDRVVMVNGTPMEDVLHSFAVQQLRKSGKIAAIVVKRPRKVQLAPPQGSLPVDEDDRAFEVMDEFDGRSARSGYSERSRRSSHGGRSRSWEDSPERGRPHERAWSQERERSRGRSLERGLDHDDDYRRPRERSRGRSLERGLDHDDDYGRPGERSHGMSTDRGYDRGYDRGYDRGYDRTYSPEAEYGRRTQPDARHAGSRSRSREHLRSRSPSPELRGRPDHAGQPDSDRPIGVLLMKSKANEEYGLRLGSQIFIKQMTRTALATKDGNLHEGDIILKINGTVTENMSLTDARKLIEKSRGKLQLVVLRDSKQTLINIPSLNDSDSEIEDISEIESNRSFSPEERRQQYSDYDYHSSNEKLKERPNSREDMQNRWSRMGATPTPFKSMGDIASVVGTENSKEPRYQEEPPAPQPKAAPRTFLRPSPEDEAIYGPNTKMVRFKKGDSVGLRLAGGNDVGIFVAGIQEGTSAEQEGLQEGDQILKVNTQDFRGLVREDAVLYLLEIPKGEMVTILAQSRADVYRDILACGRGDSFFIRSHFECEKETPQSLAFSRGEVFRVVDTLYDGKLGHWLAVRIGNELEKGLIPNKSRAEQMASVQNAQRDNAGDRADFWRMRGQRSGMKKNLRKSREDLTAAVSVSTKFPAYERVLLREAGFKRPVVLFGPIADIALEKLANELPDLFQTAKTEPKDAGSEKSSGVVRLNTVRQIIEQDKHALLDVTPKAVDLLNYTQWFPIVIFFNPDSRQGVKTMRQRLNPTSNKSSRKLYDQANKLKKTCAHLFTATINLNSANDSWFGSLKDTIQHQQGEAVWVSEGKMEGMDDDPEDRMSYLTAMGADYLSCDSRLISDFEDTDGEGGAYTDNELDEPAEEPLVSSITRSSEPVQHEESIRKPSPEPRAQMRRAASRDQLRDSSPPPAFKPEPPKAKTQNREESFDISRSHDYKSNPSAVAGNEVSGASTRSCPPPIAAKPSFGRSILKPSTPVPSPESEEVGEGSEEQEGAPKSVLGKVKIFEKMDHKARLQRMQELQEAQNARIEIAQKHPDIYAVPIKTHKPDPGLSQHTSSRPPEPQKGPSRLYQDPRGSYGSDAEEEEYRQQLSEHSKRGYYSQPSRYRDTEL
Protein: ECA polysaccharide chain length modulation protein (P0AG01)
Organism: Escherichia coli O157:H7
Function: Modulates the polysaccharide chain length of enterobacterial common antigen (ECA).
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02025, ECO:0000269|PubMed:25307743}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02025}.
Interaction partners:
- Probable ECA polymerase
- Lipid III flippase
- Probable ECA polymerase
- Lipid III flippase
- Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
- Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
- UDP-N-acetyl-D-mannosamine dehydrogenase
- UDP-N-acetyl-D-mannosamine dehydrogenase
- TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
- TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
Sequence:
MTQPMPGKPAEDAENELDIRGLFRTLWAGKLWIIGMGLAFALIALAYTFFARQEWSSTAITDRPTVNMLGGYYSQQQFLRNLDVRSNMASADQPSVMDEAYKEFVMQLASWDTRREFWLQTDYYKQRMVGNSKADAALLDEMINNIQFIPGDFTRAVNDSVKLIAETAPDANNLLRQYVAFASQRAASHLNDELKGAWAARTIQMKAQVKRQEEVAKAIYDRRMNSIEQALKIAEQHNISRSATDVPAEELPDSEMFLLGRPMLQARLENLQAVGPAFDLDYDQNRAMLNTLNVGPTLDPRFQTYRYLRTPEEPVKRDSPRRAFLMIMWGIVGGLIGAGVALTRRCSK
Protein: Fucose mutarotase (EC 5.1.3.29) (Q8R2K1)
Organism: Mus musculus (Mouse)
Function: Involved in the interconversion between alpha- and beta-L-fucoses. L-Fucose (6-deoxy-L-galactose) exists as alpha-L-fucose (29.5%) and beta-L-fucose (70.5%), the beta-form is metabolized through the salvage pathway. GDP-L-fucose formed either by the de novo or salvage pathways is transported into the endoplasmic reticulum, where it serves as a substrate for N- and O-glycosylations by fucosyltransferases. Fucosylated structures expressed on cell surfaces or secreted in biological fluids are believed to play a critical role in cell-cell adhesion and recognition processes.
Interaction partners:
- DENN domain-containing protein 10
Sequence:
MVALKGIPKVLSPELLFALARMGHGDEIVLADANFPTSSICQCGPVEIRADGLDIPQLLEAVLRLLPLDTYVESPAAVMDLVPSDKEKGLQTPIWKRYESLLLEADCKKTLMKLERFEFYERAKKAFAVVATGEMALYGNIILKKGTLDLGPS
Protein: Unconventional myosin heavy chain 6 (P91443)
Organism: Caenorhabditis elegans
Function: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13402}.
Interaction partners:
- SH3 domain-containing protein
- Transmembrane channel-like protein 2
- Actin
- PAT complex subunit CCDC47
- Twinfilin
- Netrin receptor unc-40
Sequence:
MVLVSKGDFIWIEPGKTEGSIPIGARVIDQDHGRLKVIDDLGNEQWLSADRRVRLMHPTSVQGVEDMCQLGDFHESAILRNLFIRYREKLIYAYTGSILIAVNPYMDIAIYTADEIRMYKRKRIGELPPHIFAIADNAYTNMRREKKNQSVIISGESGAGKTESTKLVLQFLATISGQHSWIEQQVLEANPVLEAFGNAKTIRNDNSSRFGKYIDVHFNESGSIEGAKIEQYLLEKSRIVTQSENERNYHIFYCLLAGLSREEKSELELGTAADYYYLIQGKTLTAEGRDDAADLAEIRSAMRVLMINEQEIGSIFKLLASLLHIGNIRFRQNTNDNMESVDVADPSTLVRIAKLLQLHEQNLLDAITTKSLVTREERVISRLNGQQAVDARDALAKAIYGKLFIHIVRRVNDAIYKPSQSRRTSIGILDIFGFENFESNSFEQLCINFANETLQQFFVHHVFKMEQKEYDEEHINWRHIKFVDNQATVDLIAQRPLNILSLIDEESIFPKGTDKTMLLKLHSTHGRNELYLQPKSELQRAFGVTHFAGNVFYNTRGFLEKNRDSFSADLSVLISSSKMPFLARLFDDIEYDTSSRKKVTVGNQFRRSLEQLMSQLTQTHPFFIRCIKPNEMKRALVMDRDLVLRQLRYSGMMETIKIRRSGYPIRHDYYPFVFRYRVLVSSIQGPVNRIDLHDAAKKICHMILGTNADYQLGKTKVFLKDKHDLVLEQEYYRILKDKAIVIQKNVRRWLVRKDFEKQRQAAVTIQTAWRGFDQRKRYRQIISGFSRLQAVLRSRQLVSHYQTLRKTIIQFQAVCRGSLVRRQVGEKRKRGEKAPLTEVSSTASVISDSHEELVGHLFDFLPSDGKDSGNENDSADSSRRGSYSRLHTSPVMPPANIPRVDSYVDEDLSKYQFGKYAATFFQAQATATHVKKPLKTALLTHTEPSAQLAALTAWTTILRFMGDLADVKPGSTNGSEVYDKTPVMIKLYATLGKKFSAHDLEEAMLSSEYGGAKTLKKGMGRKLISMTLKRKGKINGSDTSSISSDSVYSSFNAMLENKPMTSLDKLHYIIGLGILREDLRDEIYCQLCKQLSNNPSKLSAARGWILLSLCVGCFAPSERFIKYLFCFIRERGPAGTGYSKYIEDRLRRTQVNGTRHQPPSYVELQANKSQKPVVLAVTFMDGSVKTLCADSATTAAELCKQLAEKVGLTNSFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEQGRQERNAPWRLFFRKEIFSPWHDPRDDPVSTNLIYQQVIRGIKYGEYRCDKDEELAAICAQQYYIDEGTMDVNKLENNLPSYLPDFEMSGKEMALEKWTQTIMHQYRKKFTGRLPSQIEVKENVVSVAKTKWPLLFSRFYEALKFAGPPLPKNEVIIAVNWTGVYVVDDREHVMLEFSFPEISTAYYGKGKRSTTDTCTVRTVVGDEYTFQSPNADDITNLIVMFLEGLKKRSRYLVAIKSQKGDEKNNFLEFEKGDLLILVNEFTGNTLLTESVVKGENSRTCLFGLIRAENVYVLPTLVKPSKNTLQIFPKDMDLSLDLFNNNKQVTVVDYNAEPYTLENFAEDNFNSQVKRVGSQISLMTLRKKESQIECWRFSREHIDQPLLKKLNGREDACRGAIEIFAAIMKYMGDEPSKRSRLGTHLTDHIFKLPISMEALRDELYCQLVKQLTLNPSIMSEERGWELLWMATGLFAPSAALAKEISHFLKSRPHPIALDCQNRMQKLAKGGSRKYPPHLVEVEAIQHKTTQIFHKVFFPDNTDEAIEVDSATRARDFCHKIGYRLGLKSSDGFSLFVKIKDKVLAVPESEFFFDYVRSLSDWVHTNHATQKDATMIPINYQVYFMRKLWYNFVAGADPQADIIFHYHQESQKYLLGYHKTTKNDVIELAALILRSMTKDGKNAPLAQIPQLLDEIIPKDSLKMYSASEWRKTISNAYARIEHLKSDQAKIEFLNYICRWPTFGSAFFPVSQYSDLNLPDRLLLAINQTGVNIYHLDTKNLLVQYPFNVICNWTSGNTYFNMTVGNMLKGNEGKKLLLDTTVGYKMDDLLTSYISLLISNQNNHPSKTREVAL
Protein: ELAV-like protein (A0A2R8Q8X4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAVRRGHIRYLKVCEVQNQGNDRDSHKGASSIKEVYDMPNGYEDPMGDEPSDAKTNLIINYLPQNMSQEELRSLFSSIGEVESAKLIRDKMAGHSLGYGFVNYVNPSDAERAINTLNGLRLQSKTIKVSYARPSSDGIKDANLYISGLPKTMTQKNVEDMFTQYGRIINSRILVDQASGLSRGVAFIRFDKRSEAEEAIKDLNGSKPSGASEPITVKFAANPNQSKNSQLLSQLYHTQSRRFGGPVHHQPQRFRFSPMSVDHSVSSMNVASSSSSGWCIFVYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTSKCKGFGFVTMTNYEEAAMAISSLNGYRLGDKVLQVSFKSSKSHK
Protein: Kelch-like protein 34 (Q8N239)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSYFLSYCKAHGGALLTGYQALRAEGFLCDVTLETEGSEFPAHRSLLACSSDYFRALFKSHTQESRARVIHLHVPSAAGLQRLLDFIYTAWLSLSMDTVEDTLEAASYLQVTEALGLCGRYLERQLAPENCCFAANVAARFGLAHTLDAAERCIVSHLQELLARGAGPAGLLELNPTSLRAVLGAPDVARVPEARLLGLALAWLRQEPTTERLAHCTELLERVRFGLVPADVLRRVYSGSGLVLPARVKGLIIQALNYHTTPSRQPLMQGEQTSIRSPQTRILLVGGRRAREVVIEEVAAPQRAARGQVAAPEPEEEEEELEEEEEEEEWELTQNVVAFDVYNHRWRSLTQLPTPLLGHSVCTAGNFLFVLGGESPSGSASSPLADDSRVVTAQVHRYDPRFHAWTEVPAMREARAHFWCGAVGERLLAVGGLGAGGEVLASVEMYDLRRDRWTAAGALPRALHGHAGAVGDRGVVYISGGKAGRGEGGASSLRDLYVLGPEEQVWSKKAPMGTARFGHHMAVLRGAVFAFLGRYEPFSEIERYDPGADQWTRLRPLPYDRFCYGLAVVEETALLLGGLKWRDSRQVPTRNVVGYDLDLDRWEDIGCALPWAWSGLRCAVLQLAEGGDDEREGEVGEALDLVLG
Protein: Uncharacterized protein (Q385B1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEEIIELCALCTSEEGHMDFVLGSVLTFMLQRTAQVALPRMSALERGSLTLRLISAGGLQNETCRHFVFEKLCPPYNAALLLRLSHELYLRPTERMTAFSRPNSSESPTRLKHSLPLFSLVRGAKDASRSQPPVDFRSTDVSELLSALLDSWNPAHPTSLSLGELPPGLATFLAFQYPLRILVMLQKDVVEPFVPASWRNTWHQLCFEGSGRGSVDSLHNLLVGGMCEGFWPALRRVLVNPLLGGEKGLKEKEGDGDQFDVLEGTTVLALHAVFRLWLGELRQMWSALGGGVVVSESGGHSAQNPSFCDTLAGGLLLLEQDGGLEGCETVALCAPHALLLVLYDGYCLASQVVRHALDHPNVALLGPSFADLESDGGPLLGELGVKSGSAFFAALALRLPVSQLYIAGRVWQLLETIVSNKARGKENDEHVAVLRSRLQAMLSSFVYSNLKLGTTRSSELSVGGATPVTQSPSSAAGLRADETPRATLRLKRLRVTEPSSQPGTTTGGDGGGGLNASHAVPGGQDIASAVPLLCETLIEFALSELSQPVIPAQHHSSAAAVRASGNEESLGGTRLVLLTPPHIKGVLNLLSPTSSQLPSFCLTPVCDVSCVLMSVLLYRRCATLHQWLLNEKRAEVRATVATRLTRRTRQWGRFLAPLGLFRYVPVADVLLPQCLQAMEGKSTSMATDLMPATDAAVVEFCGAVRVCIVQHTR
Protein: Transcriptional regulator WhiB5 (P71592)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A transcription factor that is probably redox-responsive. Probably plays a role in immunomodulation and reactivation after chronic infection. Its induction results in transcription of a number of genes including sigM, and the genes for 2 type VII secretion systems ESX-2 and ESX-4. Seems to negatively regulate its own expression. The apo-form has been shown to act as a protein disulfide reductase. The apo- but not holo-form probably binds DNA.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Mycosin-4
- ESX-4 secretion system protein eccD4
- Hypothetical alanine and valine rich protein
- Uncharacterized HTH-type transcriptional regulator Rv0023
- Uncharacterized protein Rv0025
Sequence:
MAHPCATDPELWFGYPDDDGSDGAAKARAYERSATQARIQCLRRCPLLQQRRCAQHAVEHRVEYGVWAGIKLPGGQYRKREQLAAAHDVLRRIAGGEINSRQLPDNAALLARNEGLEVTPVPGVVVHLPIAQVGPQPAA
Protein: Clusterin (H0YLK8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MEACKDSRIGGMMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCR
Protein: Mnt, isoform J (M9NDN0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGIGGIGVLLEAAQFLEQHEKLPQAGGGGGSALGVGVALPQQQQQTVHCKSNSIINNNNSSQHNRNSSSSSNGIIATPPFTNGNGNGTVGVGNASAIFNVSVNANGNGLSNGHSSPRSQLAAAATAHDYEYSAAGVANGHSEGRPHVSAARDQQDHPQHQQHANHMQIQQHYGYMRSNIGGVIYGLHKDSADSAASSACGAGAGAAAVGMSIASSAPAAGSQLSAHHHTGHGGRRRTTSSNSNGAGTREVHNKLEKERRAQLKECYDLLKKVLPMGDEDRKKTSNLTILDTAHKYVNSLSHEVCEQEAKIEKLAKQKIELQKRLKQLSLRRESPPTDQQIIPQADKAVCLATTATTAPPTAASGHNGTTILFDAGNACATGQQLTTVINKTNGGATAAASSKHNGNHTGGATTTLTPAMGIMTIKNGNGSNGNMLAISPTGGHNHQLHQHHNGSPAGSPSGIGATTGATITRGSPTPSTPSPSPSSSSSGVSLSTSFMGGSSSSSSSSSSSSSSSSSSSSSSPTQQQQIITPTATARSVGLKFHGGAGAAVPAGGGSVNGFHQADKDRNYTFLRLSAGTTAQ
Protein: ORC1-type DNA replication protein 2 (Q9UXF8)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds both single-stranded and double-stranded DNA, with a preference for molecules that contain a bubble, a fork, or a tail. Has a weak ATPase activity. Stimulates the binding of the MCM helicase to the origin DNA, but strongly inhibits ATPase and DNA helicase activities of MCM. Also regulates the DNA polymerase and the nuclease activities of PolB1.
Interaction partners:
- Minichromosome maintenance protein MCM
- DNA primase large subunit PriL
- DNA primase small subunit PriS
- DNA polymerase 1
- Single-stranded DNA binding protein Ssb
- DNA polymerase 2
- DNA primase DnaG
- Flap endonuclease 1
- THUMP domain-containing protein
Sequence:
MVSAKDILSDSLRSSVLIIKHKDKLSPDYVPENLPHREEKIKELGFIFKDLLAGDAKDSERVVILGRTGTGKTATVRLFGKNFEDIAEREYGVKVKYVHINCYRHRTLYLISQEIANALKLPIPSRGLSAQEVFKMIHEYLDRRNIHLIVALDEFGHFLNTANTEEIYFLVRLYDEISAIIKRISYIFIVNESHSIYKLDRSIRDHIARRLIEFPPYKSMELYDILKYRVDEAFNDNAVDDEVLQFISNTYGYDKGGNGNARIAIETLSLAGEIAEKEGSPVVLLDHAKKANSTINPEIQEIIDSLSYLDLHQLILLKALIRALNKTKADEITMGTLEEEYISLSREFNEEPRRHTQVYEYLRKLKVIGIINTRQSGKGMRGRTTLVSLSLPLDKRLDDYIMQQIMVRLKSRA