wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar protein sorting-associated protein 41 homolog (P93043)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for vacuolar assembly and vacuolar traffic.
Interaction partners:
- Vacuolar protein-sorting-associated protein 33 homolog
- Vacuolar protein-sorting-associated protein 11 homolog
- Vacuolar sorting protein 39
- Vacuolar sorting protein 18
- Protein VACUOLELESS1
- Vacuolar sorting protein 3
- Vacuolar fusion protein MON1 homolog
- Vesicle transport v-SNARE 11
- Syntaxin-22
- Vacuolar fusion protein CCZ1 homolog A
Sequence:
MAAVPPENGVDGDDEREEEEEDEEEEEEEEEEENGDEAEEEPRLKYQRMGGNVPALLSNDAASCIAVAARMIALGTHDGTVRILDLLGNQVKEFRAHTAPVNDINFDTEGEYIGSCSDDGSVVINSLFTDDEKMKFDYHRPMKAISLDPDYTKKQSKRFVAGGLAGHLYMNSKKWFGNKDQVLHSGEGPIHSVKWRGSLIAWANDVGVKVYDTAKDQRVTFIEKPRGSPRPEALLPHLVWQDDTLLVIGWGTSVKIASIKSDQQQTGTFRQIQMSSLTQVDIVASFQTSYYISGIAPFGDSLVILAYIPIEGDGEKEFSSTTTLSRQGNAQRPEIRIVSWNNDELTMDALPVHGFEHYKAKDYSLAHAPFPGSSYAGGQWAAGDEPLYYIVSPKDVVIAKPRDAEDHINWLLQHGFHEKALAAVEASEGRTELIDKVGAGYLDHLIVERKYAEAASLCPKLLRGSASAWERWVFHFAQLRQLPVLVPYMPTDNPRLKDTVYEVALVALATNPSYHKELLSAVKSWPRSVYSALTVISAIEPQLNTSSMTDALKEALAELYVIDGQYQKAFSLYADLLKPEVFDFIEKYSLHEAIRGKVVQLMLLDCKRATVLFIQNRDLIPPSEVVPQLLKAGKNPQVLKAGKKCDSRYYLYLYLHALFEVSHDTGKDFHDMQVELYAEYDTKMLLPFLRSSQHYKLEKAYELCVKKDFLREQVFVLGRMGNAKQALAVIINKLGDIEEAVEFVSMQHDDDLWEELIKQCLNKPEMVGLLLEHTVGNLDPLYIVNMVPNGLEIPRLRDRLVKIVTDYRTETSLRHGCNDILKTDIVNLLVKCFNEARRGVCLSHEDDDSRAKREDNNRSSFSQRMVVDKSLSIKMTEVKSKTRGDTRCCMCFDPVSIRGDTVVVFFCCHAYHETCLMDAAFSNNNHKTTKGSSGYEYSYDNGVDEEEEDEEEDEDGDGDRPGRSRLRCILCTTAAAASAR
Protein: Transmembrane protein 184A (Q6PFI3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNETTLRILSASSDKNMDNVPLPSYSLLSNNTDLLNKTVIRSANGTEVVADDQIFLSTATAQALSGIFVWSALILTCHQIYLHLRSYTVPNEQRYIIRILFIVPIYAFDSWLSLLFITNDQYYVYFDSVRDCYEAFVIYNFLSLSFEYLGGESAIMSEIRGKPIQSSCLYGTCCLVGMSYSIGFLRFCKQATLQFCVVKPIMAVITILLQAFGKYHDGDFNVTGGYLYITIIYNFSVSLALYALFLFYFATSDLLRPFEPVLKFLTIKSVIFLSFWQGMVLAILERCGVIPEAQFIDGHEVGAGTVAAGWQNFIICIEMFFASIALRYAFTSSVYREKKNEAPENVAPMHGISSGLKETINPGDMVQDAIHNFSPAYQQYTQQSTQEVVQPSANGKPGISTSKSTKKSDKVMLIDTDDEF
Protein: Casein kinase II subunit beta (CK II beta) (Q5ACW5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Casein kinase II subunit beta
- Casein kinase II subunit alpha
- Casein kinase II subunit alpha
- Ribosomal RNA-processing protein 7
- U3 small nucleolar RNA-associated protein 22
- rRNA biogenesis protein RRP36
- rRNA-processing protein
- SnoRNA-binding rRNA-processing protein
- U3 small nucleolar ribonucleoprotein protein IMP4
- Ribosome biosynthesis protein
Sequence:
MPSDPEEDYIPWIQQFCELFGHDYFVQVSQDFIEDDFNLTGLSSQVPYYREALYTILDYQVETAEDHNTDNTTTNTSNNNDSRNGTSKRNASELPNKALLAHSAELLYGLIHARYIVSKQGLTAMASKFERNDFGSCPRYFCDGMHLIPVGSTDVPGQETVRLFCPCCNDIYIPSSSRYLNIDGAFFGTTFPGLLVKMFPEIENQCRIRITKFSQNDFGLKLFGFKINELSATGPRMKWLRMHPKTEDEKQEYDSCEYNVPISYLDEDEEMEEDDEEEDEVEEEDDDRTMASE
Protein: Oxysterol-binding protein-related protein 3C (OSBP-related protein 3C) (Q93Y40)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the transport of sterols.
Interaction partners:
Sequence:
MGSPKKNENKGFFAAMTSGFSMFGTAVSRSVNGVQGNEGVEVINPEGGKEDAEEEAQKGRWKDEERDSYWKMMQKYIGSDITSMVTLPVVIFEPMTMLQKMAEIMEYSHLLDQADECEDPYLRLVYASSWAISVYYAFQRTWKPFNPILGETYEMVNHGGISFISEQVSHHPPMSAGHAENEHFIYDITSKLKTKLLGNSVDVYPVGRTRVTLKKDGVVLDLVPPLTKIHNLIFGRTWVDSPGEMVMTNLTTGDKVVLYFQPCGWFGSGRYEVDGYVYSAAEEPKIMMTGKWNEKMSYQPCDAEGEPLPGTELKEVWHLADVPKNDNFQYTHFAHKINSFDTAPAKLLASDSRIRPDRYSLEQGDLSKAGSEKHSLEERQRAEKRTRETKGQKFTPRWFDLTDEITPTPWGDIEVYQYNGKYNEHRDTAESSSSASNETDLKSIEFNPWQYGNISTE
Protein: Solute carrier family 15 member 1 (Intestinal H(+)/peptide cotransporter) (Oligopeptide transporter, small intestine isoform) (Peptide transporter 1) (P46059)
Organism: Homo sapiens (Human)
Function: Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Primarily responsible for the absorption of dietary di- and tripeptides from the small intestinal lumen (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:28408210}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to the apical membrane of enterocytes. {ECO:0000269|PubMed:28408210}.
Interaction partners:
- Sodium/glucose cotransporter 1
- Solute carrier family 2, facilitated glucose transporter member 2
- Excitatory amino acid transporter 3
- ATP-binding cassette sub-family C member 2
- Solute carrier family 22 member 6
Sequence:
MGMSKSHSFFGYPLSIFFIVVNEFCERFSYYGMRAILILYFTNFISWDDNLSTAIYHTFVALCYLTPILGALIADSWLGKFKTIVSLSIVYTIGQAVTSVSSINDLTDHNHDGTPDSLPVHVVLSLIGLALIALGTGGIKPCVSAFGGDQFEEGQEKQRNRFFSIFYLAINAGSLLSTIITPMLRVQQCGIHSKQACYPLAFGVPAALMAVALIVFVLGSGMYKKFKPQGNIMGKVAKCIGFAIKNRFRHRSKAFPKREHWLDWAKEKYDERLISQIKMVTRVMFLYIPLPMFWALFDQQGSRWTLQATTMSGKIGALEIQPDQMQTVNAILIVIMVPIFDAVLYPLIAKCGFNFTSLKKMAVGMVLASMAFVVAAIVQVEIDKTLPVFPKGNEVQIKVLNIGNNTMNISLPGEMVTLGPMSQTNAFMTFDVNKLTRINISSPGSPVTAVTDDFKQGQRHTLLVWAPNHYQVVKDGLNQKPEKGENGIRFVNTFNELITITMSGKVYANISSYNASTYQFFPSGIKGFTISSTEIPPQCQPNFNTFYLEFGSAYTYIVQRKNDSCPEVKVFEDISANTVNMALQIPQYFLLTCGEVVFSVTGLEFSYSQAPSNMKSVLQAGWLLTVAVGNIIVLIVAGAGQFSKQWAEYILFAALLLVVCVIFAIMARFYTYINPAEIEAQFDEDEKKNRLEKSNPYFMSGANSQKQM
Protein: C3/C5 convertase (F1QFC2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MTSMECGLRLKWLILALICPLIAGAPSREGSCPEENLDIAGGSFTLSNGYSDGSYLQYICPDNHYPSISSRRCQFGVWTPKASSRKKAECKKITCPNPRVLENGEVAPYQERYYINDVTTYSCSSDYKFRGSKVRVCQPNGKWNGSTPICGRDYHCPDPGVPPGSSRTGSIFNIDDEVTYHCDSPLTLIGSKVRKCLDDGQWSGTEPQCYADFTYDTAMEAAEAFGNSLTTTLTVQQGFEDDQHGKKISLDRGGKLDIYIAVDASDSIDPKDFGKAKKIIKTLIEKISYYEVSPNYEILMFATDVDQIVKMRDFKTNEKARNISKIFEDLDNFNYDKKGDRTGTNIAKLYLKILDSMSLEQVQNKEDFLQTQHVIIVFTDGQANMGGNPKPKVDLIKNLVIKNNASRENKLDLYVFGVGKDVKKEDMNGLVSEKKDERHFFKLPDLDEVQNTFDLMLDDSTVVGLCGMQQNYDGSNKRSAYPWLAQLSIAQSQISDCMGSLVTSRYILTAAHCFKEGDTPDKITVYLEKNTDVKVEKVFIHPNYSLTAKQSIGIKEFYDFDVALLQLKTPVKMSVNLRPICLPCTKETNRALKLSDSQGTCEKHEQILLSNELVDAAFTSKMDMEKRSPRKIRRITVKLGKYLDACVEDAKKAKGIEVADATEAVTKNFLCSGGNQPQRDDVSCKGESGGATHVDKYGRLIQIGVVSWGVKNLCSKAKLDAVSVSDSRDYHINLLRPDIQSFLKKHLENDKLGHTLTFLP
Protein: Ribosomal protein S12 (Ribosomal protein small subunit 12) (Q2F983)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MPTKNQLIRHGREEKQRTDRTRASDQCPQKQGVCLRVSTRTPKKPNSALRKIAKVRLSNRHDIFAHIPGEGHNSQEHSIVLVRGGRVKDSPGVKSHRIRGVKDLLGIPDRRKGRSKYGAERPKSK
Protein: V0 assembly protein 1 (P53262)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Accessory component of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments. Functions with VMA21 in assembly of the V0 complex.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Single-pass type I membrane protein {ECO:0000269|PubMed:14562095}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18799613}; Single-pass type I membrane protein {ECO:0000269|PubMed:18799613}.
Interaction partners:
- V-type proton ATPase subunit a, vacuolar isoform
- Vacuolar ATPase assembly protein VMA22
- Vacuolar ATPase assembly integral membrane protein VMA21
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d
- V-type proton ATPase subunit c''
- V-type proton ATPase subunit c
- V-type proton ATPase subunit e
- V-type proton ATPase subunit C
- V-type proton ATPase subunit c'
Sequence:
MVFGQLYALFIFTLSCCISKTVQADSSKESSSFISFDKESNWDTISTISSTADVISSVDSAIAVFEFDNFSLLDNLMIDEEYPFFNRFFANDVSLTVHDDSPLNISQSLSPIMEQFTVDELPESASDLLYEYSLDDKSIVLFKFTSDAYDLKKLDEFIDSCLSFLEDKSGDNLTVVINSLGWAFEDEDGDDEYATEETLSHHDNNKGKEGDDDILSSIWTEGLLMCLIVSALLLFILIVALSWISNLDITYGALEKSTNPIKKNN
Protein: Extracellular matrix protein 1 (Secretory component p85) (Q61508)
Organism: Mus musculus (Mouse)
Function: Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Metalloproteinase inhibitor 3
- EGF-containing fibulin-like extracellular matrix protein 1
Sequence:
MGTVSRAALILACLALASAASEGAFKASDQREMTPERLFQHLHEVGYAAPPSPPQTRRLRVDHSVTSLHDPPLFEEQREVQPPSSPEDIPVYEEDWPTFLNPNVDKAGPAVPQEAIPLQKEQPPPQVHIEQKEIDPPAQPQEEIVQKEVKPHTLAGQLPPEPRTWNPARHCQQGRRGVWGHRLDGFPPGRPSPDNLKQICLPERQHVIYGPWNLPQTGYSHLSRQGETLNVLETGYSRCCRCRSDTNRLDCLKLVWEDAMTQFCEAEFSVKTRPHLCCRLRGEERFSCFQKEAPRPDYLLRPCPVHQNGMSSGPQLPFPPGLPTPDNVKNICLLRRFRAVPRNLPATDAIQRQLQALTRLETEFQRCCRQGHNHTCTWKAWEGTLDGYCERELAIKTHPHSCCHYPPSPARDECFAHLAPYPNYDRDILTLDLSRVTPNLMGQLCGSGRVLSKHKQIPGLIQNMTIRCCELPYPEQACCGEEEKLAFIENLCGPRRNSWKDPALCCDLSPEDKQINCFNTNYLRNVALVAGDTGNATGLGEQGPTRGTDANPAPGSKEE
Protein: Uncharacterized protein (Q38CB6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRMSLTTRRPFCPVLLNIGSSRAVTLSHFHAKVCPSITATVKQTIRELDDEASPNHQRRQESCFSSGELRLRPYGFSPERPQLQHESWSCAWHSYLNAVRLRGEVSAAGVAPLPPTATSANSTSHNDDEFFPMTGTLTLPVPVVVPTSNNEPSNETIMMEFFRVDAFIPVRVQMYHVMRRLIKMQAVWNNIVAIGIVVPTHEVEYFISAARAAHASDGERTPHALLSRKPSVLVYDPEGLRFQAPESKRLRK
Protein: Non-specific lipid-transfer protein 10 (LTP 10) (Q9LZV9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity).
Interaction partners:
- Non-specific lipid-transfer protein 15
- At2g45350/F14N22.7
- Non-specific lipid-transfer protein 9
- At3g13230
- Zinc finger
- Uncharacterized protein
- Phosphoglycerate mutase family protein
- GDSL esterase/lipase At1g09390
- GDSL esterase/lipase At5g62930
- At3g15680
Sequence:
MMRVVLPLCLLLASIFAWGSEAAISCNAVQANLYPCVVYVVQGGAIPYSCCNGIRMLSKQATSASDKQGVCRCIKSVVGRVSYSSIYLKKAAALPGKCGVKLPYKIDPSTNCNSIK
Protein: Carbamoyl phosphate synthase small chain, chloroplastic (EC 6.3.5.5) (Carbamoyl phosphate synthetase glutamine chain) (Protein VENOSA 6) (Q9LVW7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the carbamoyl-phosphate synthetase (CPS) composed of a small chain CARA/VEN6 and a large chain CARB/VEN3. Involved in arginine biosynthesis. Required for mesophyll development.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Argininosuccinate synthase, chloroplastic
- Aspartate carbamoyltransferase, chloroplastic
- Ornithine transcarbamylase, chloroplastic
- Amidophosphoribosyltransferase 2, chloroplastic
- Dihydroorotate dehydrogenase
- Uridine 5'-monophosphate synthase
- Argininosuccinate lyase, chloroplastic
- Glutamine synthetase cytosolic isozyme 1-3
- Glutamine synthetase cytosolic isozyme 1-4
Sequence:
MAMATRTLGFVLPTSLSSQPSFDRRGGGFRVSVIRCSTSPLTFPTSGVVEKPWTSYNARLVLEDGSIWPAKSFGAPGTRIAELVFNTSLTGYQEILTDPSYAGQFVLMTNPQIGNTGVNPDDEESGQCFLTGLVIRNLSISTSNWRCTKTLADYLTERDIMGVYDLDTRAITRRLREDGSLIGVLSTEQSKTDDELLQMSRSWDIVGIDLISDVSCKSPYEWVDKTNAEWDFNTNSRDGKSYKVIAYDFGIKQNILRRLSSYGCQITVVPSTFPAAEALKMNPDGILFSNGPGDPSAVPYAVETVKELLGKVPVYGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGQVEISAQNHNYAVDPASLPGGVEVTHVNLNDGSCAGLSFPEMNVMSLQYHPEASPGPHDSDNAFREFIELMKRSKQSS
Protein: Leucine aminopeptidase A (EC 3.4.11.-) (Leucyl aminopeptidase A) (LAPA) (Q2U1F3)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
Subcellular location: Secreted {ECO:0000269|PubMed:19129648, ECO:0000269|PubMed:20803144}.
Interaction partners:
Sequence:
MRFLPCIATLAATASALAIGDHVRSDDQYVLELAPGQTKVVTEAEKWALRAEGKRFFDITERASSLELASNKKQKLAVTYPDSVQHNETVQNLIKSLDKKNFETVLQPFSEFHNRYYKSDNGKKSSEWLQGKIQEIISASGAKGVTVEPFKHSFPQSSLIAKIPGKSDKTIVLGAHQDSINLDSPSEGRAPGADDDGSGVVTILEAFRVLLTDEKVAAGEAPNTVEFHFYAGEEGGLLGSQDIFEQYSQKSRDVKAMLQQDMTGYTKGTTDAGKPESIGIITDNVDENLTKFLKVIVDAYCTIPTVDSKCGYGCSDHASATKYGYPAAFAFESAFGDDSPYIHSADDTIETVNFDHVLQHGRLTLGFAYELAFADSL
Protein: U2A'/phosphoprotein 32 family A C-terminal domain-containing protein (Q38B89)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MILKEETVLRKTNAENLAAVRNLNLWGEGLTDVSIVSRLPRIEVLALAANKLTTLSPFAACTQLEELYLRRNNVASMLEIKYLRHLPKLHTLWLMDNPCARHPHYRQIVILCCRHLRHLDETEVSEKERAEAEKLLPEGMLQEMLESESAEAAVGTANKAQLQNRTPVSERKQPMGEVVQGGAIHETGAGRERGHRVTSSDTSGRGPSSAPERRQGSADDGLAQTAVQVQRAMFSSIMALVPELAVQTIEALQKELAEELCRRGKRLPPVVRDRT
Protein: Zinc finger protein 639 (J3KR68)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNEYPKKRKRKTLHPSRYSDSSGISRIADGFNGIFSDHCYSVCSMRQPDLKYFDNKDDDSDTETSNDLPKFADGIKARNRNQNYLVPSPVLRILDHTAFSTEKSADIVICDEECDSPESVNQQTQEESPIEVHTAEDVPIAVEVHAISEDYDIETENNSSESLQDQTDEEPPAKLCKILDKSQALNVTAQQKWPLLRANSSGLYKCELCEFNSKYFSDLKQHMILKHKRTDSNVCRVCKESFSTNMLLIEHAKLHEEDPYICKYCDYKTVIFENLSQHIADTHFSDHL
Protein: N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (DDAH-1) (Dimethylarginine dimethylaminohydrolase 1) (EC 3.5.3.18) (DDAHI) (Dimethylargininase-1) (Q9CWS0)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
Interaction partners:
- Alanine--glyoxylate aminotransferase 2, mitochondrial
Sequence:
MAGLGHPSAFGRATHAVVRAPPESLCRHALRRSQGEEVDFARAERQHELYVGVLGSKLGLQVVQLPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADSLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDMAANCIYLNIPSKGHVLLHRTPEEYPESAKVYEKLKDHLLIPVSNSEMEKVDGLLTCCSVFINKKIDS
Protein: Zinc transporter foi (Protein fear-of-intimacy) (Protein kastchen) (Q9VSL7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the normal migration of longitudinal and peripheral glial cells. During larval development, required for the migration of the subretinal glia into the eye disk. During embryonic development, also controls the migration of muscle cells toward their attachment sites. Required in the mesoderm for the correct morphogenesis of embryonic gonad and for tracheal branch fusion during tracheal development. Shg may be cooperating with foi to mediate a common mechanism for gonad and tracheal morphogenesis. Acts as a zinc transporter in both yeast and mammalian cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12702650, ECO:0000269|PubMed:15464587, ECO:0000269|PubMed:15509557}; Multi-pass membrane protein {ECO:0000269|PubMed:12702650, ECO:0000269|PubMed:15464587, ECO:0000269|PubMed:15509557}.
Interaction partners:
- GH18858p
- IP18018p
- RE15841p
Sequence:
MARHIMAVCVVCLLCAHRLHCQDHIESLLGPARVTTHNSQDQLNARVYTNLSPSSETTDRRQQRSASGDDDTFNYSISPPSRREKRHAGHEHGPTSESRVPQITQYYLEKLMAQDELMNSSGFDGLLQQLSLHSLASGASEGTCVPGSRLVHHVQPHDHHHAHHHEEEDHSLQLNNCTLIQNGTTSNVICPSLPNNNTHPLGKEAKNFTLSDKDLLHLCPILLYELKAQSGGCIEPAILSDIDTTEELLEAEKDKDIFYVWIYAFISVFACGILGLVGVAIIPFMGSRYYKYIIQYLVALAVGTMTGDALLHLLPHSLAGQDERGMIMKGLGCLGGIIFFYVMEHALTMISEWRKSVEKKETKKPSRAKVMRDPDSSVNNSVAGDKICKQKYSSYPYCYDEITMNNKQSEWMHLPFDVAAGAGGDAPSVAELRNGVGDHDGSNDMAAAAESLISPLHTNCVEMNHHNHNHKHNSHQQNHEGQDSNTIVTDLDGNAVYAVNKAKDKDSRNDHVTVILREHESSHHGHSHRHGHVHSPPETLSAVAWMIIMGDGLHNFTDGMAIGAAFAENIAGGFSTSLAVFCHELPHELGDFAILIKAGMSVKSAVYYNLLTGVLSFIGMIFGIAFGQSQDVAQWMFAVAAGLFIYIALVDMMPEISASHKSLGQFLLQILGMLSGVGIMLLIALYEGDLMSAFGTAGAASHQHAH
Protein: Midline fasciclin, isoform F (Midline fasciclin, isoform G) (Midline fasciclin, isoform M) (Q86B95)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRLWACLLLLGSIQIQAVPFYGDSSSEEVAEFDDSSDSTHESSDNSSSGYDTEFVPLEHQQQPQGRQETAATVPAQTPSGVEQKPFNVDTITTDVNSPNPAIFFQQSFPFFGNEFFNSFGGFGFGAAQEPWWKGPNVCTEKEEDETVASETEAEETVDTFGQERDGVTNVVRSPLFGQFQFSVNSCAEKPNKHVCTKIVNQNGKKKTLTLTRQCCYGYGRPRNADFTTPCEKIDIKDVEATASDMGAKQFLESARTAGELADMLGAGSGKKVTLFVPNDAAFMEYRGHHQQENNVEDAKAEASKPSIYKLHAVLGEVQLEDVPNEKLLQTELPDQKIRINSYQLPAALGLEPYRFAANCVPIEKHDKLSEQALVHTLGGVLKPLTKNLMDIIRERADMSIMRTVLEKTNLSAMLEDDKPVTIFVPTDAAFDKLEPHLRRALKEGRGCASNILKNHLLDLTFCSLATVPGAKTTAYNLLGEPLLLNRTHRAANQTGPTPIYINNLAKIIDADIMGTNGVLHVIDTILPTESALPMTSLMSQKNLTIFQRLLEASGYDDQFDDLDNVTIFAPTDKALQNTEWARMLKEQPELLNHNLDLLEFLNYHVVKPMIKTCDLSEKSLPTVAGSSVRLNLYSTHALFSDVMNRATVNCARLVHFDDESCGSVLHQVDRALAPPKNNMLKLLEANPNYSKFLELVRKANLTQLLSNDSRSLTLLVPKNDIFEELNESGEGSKPADPMALVKTHIVEDVVCCAGIIPTNWPFVRSIESISGQHLRITRDRRPKIENAGVTKCDVVATNGILHEINDIIVPRPQRQQQQRPQLIPPGAGYQPQGDFDVFF
Protein: Possible transcriptional regulatory protein (Probably ArsR-family) (P71941)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable arsenic-transport integral membrane protein ArsC
- Probable transcriptional regulatory protein
- Uncharacterized HTH-type transcriptional regulator Rv0494
- HTH-type transcriptional regulator Rv1931c
- Probable transcriptional regulatory protein
- Probable transcriptional regulatory protein
- Cadmium-induced protein CadI
- Putative antitoxin HigA3
- Uncharacterized HTH-type transcriptional regulator Rv0767c
- HTH-type transcriptional regulator LysG
Sequence:
MSNLHPLPEVASCVVAPLVREPLNPPAAAEMAARFKALADPVRLQLLSSVASRAGGEACVCDISAGVEVSQPTISHHLKVLRDAGLLTSRRRASWVYYAVVPEALTVLSNLLSVHADAAPALGAPA
Protein: Calcium-responsive transactivator (SS18-like protein 1) (Q8BW22)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator which is required for calcium-dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP.
Subcellular location: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes to nuclear bodies. Colocalizes with SGO1 at kinetochore (By similarity). {ECO:0000250}.
Interaction partners:
- Actin-like protein 6B
- Zinc finger protein neuro-d4
- Zinc finger protein DPF3
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF complex subunit SMARCC2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- AT-rich interactive domain-containing protein 1A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF complex subunit SMARCC1
Sequence:
MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILDYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALSQSGSSQGLHPQGSLSDTVSTGLPPASLMQGQIGNGPNHVSMQQTAQSTLPTTSMSLSGSGHGTGPGYSHSGPTSQSVPMQGQGAISNYVSRTNINMQSNPVSMMHQQAATSHYNSAQGGSQHYQGQAPIAMMGQGGQGGSMMGQRPMAPYRPSQQGSSQQYLGQEEYYSEQYSHSQGSAEPMSQQYYPDGHGDYAYQQSSYTEQSYDRSFEDPTQHYYEGGNSQYSQQQAGYQQGTAQQQTYSQQQYPNQQSYPGQQQGYGPAQGAPSQYSSYQQGQGQQYGSYRTSQTGPSAQQQRPYGYEQGQYGNYQQ
Protein: BUB3-interacting and GLEBS motif-containing protein ZNF207 (BuGZ) (49 kDa zinc finger protein) (Zinc finger protein 207) (Q9JMD0)
Organism: Mus musculus (Mouse)
Function: Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly. ZNF207/BuGZ is mainly composed of disordered low-complexity regions and undergoes phase transition or coacervation to form temperature-dependent liquid droplets. Coacervation promotes microtubule bundling and concentrates tubulin, promoting microtubule polymerization and assembly of spindle and spindle matrix by concentrating its building blocks. Also acts as a regulator of mitotic chromosome alignment by mediating the stability and kinetochore loading of BUB3. Mechanisms by which BUB3 is protected are unclear: according to a first report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3. According to another report, the stabilization is independent of the proteasome (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9832628}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O43670}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O43670}. Note=Localizes primarily to the nucleus in interphase, concentrates at kinetochores prior to nuclear envelope breakdown and during early prometaphase, and disappears from kinetochores upon microtubule-binding. {ECO:0000250|UniProtKB:O43670}.
Interaction partners:
- Mitotic checkpoint protein BUB3
- Heterogeneous nuclear ribonucleoprotein M
- Serine/arginine-rich splicing factor 10
- Far upstream element-binding protein 1
- Serine/arginine-rich splicing factor 3
- Splicing factor 3B subunit 1
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Ubiquitin-associated protein 2-like
- Bcl-2-associated transcription factor 1
Sequence:
MGRKKKKQLKPWCWYCNRDFDDEKILIQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMDERRRLLEQKTQESQKKKQQDDSDEYDDDESAASTSFQPQPVQPQQGYIPPMAQPGLPPVPGAPGMPPGIPPLMPGVPPLMPGMPPVMPGMPPGLHHQRKYTQSFCGENIMMPMGGMMPPGPGIPPLMPGMPPGMPPPVPRPGIPPMTQAQAVSAPGILNRPPAPTAAVPAPQPPVTKPLFPSAGQMGTPVTSSSTASSNSESLSASSKALFPSTAQAQAAVQGPVGTDFKPLNSTPAATTTEPPKPTFPAYTQSTASTTSTTNSTAAKPAASITSKPATLTTTSATSKLIHPDEDISLEERRAQLPKYQRNLPRPGQTPIGNPPVGPIGGMMPPQPGLPQQQAMRPPMPPHGQYGGHHQGMPGYLPGAMPPYGQGPPMVPPYQGGPPRPPMGMRPPVMSQGGRY
Protein: Mitotic checkpoint protein BUB3.3 (Protein BUDDING UNINHIBITED BY BENZYMIDAZOL 3.3) (F4I241)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20 (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Accumulates onto both kinetochores and the spindle microtubules in cell arrested in metaphase. Starts to localize at kinetochores in prometaphase I (Pro-MI) stage and maintains the localization until the metaphase I-anaphase I (MI-AI) transition. Associates with unattached kinetochores upon spindle assembly checkpoint (SAC) activation. Present in the phragmoplast midline during the final step of cell division (By similarity). {ECO:0000250}.
Interaction partners:
- Mitotic spindle checkpoint protein MAD2
- Anaphase-promoting complex subunit 4
- Cell division cycle 20.5, cofactor of APC complex
- At1g78070/F28K19_28
- Mitotic spindle checkpoint protein BUBR1
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- At5g05510
- Protein SUPPRESSOR OF FRI 4
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 5
Sequence:
MSGDRLEFENPIEDAVSRLRFSPQSNNLLVASWDSYLRLYDVESSSLSLELNSQAALLDCCFENESTSFTSGSDGFIRRYDLNAGTVDTIGRHDDISTSIVYSYEKGEVISTGFDEKIKFWDTRQRESLVFSTDAGGAVGCVTVSGNNLVVCVDASMHIYDLRNLDEAFQSYASQVEVPIRCITSVPYSRGYAVGSVDGRVAVDFPNTSCSSEIKYSFRCHPKSRNGRLDGVCINAIEFSPCGSGTFVTGDNEGYVISWNAKSRRRLNELPRYSNSIASLAFDHTGELLAIASSHTYQDAKEKEEAPQVFIHRL