wanglab/gogpt-training-data huggingface dataset:
Protein: Protein DPCD (Q384D8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- EGF-like domain-containing protein
- BRCT domain-containing protein
- 14-3-3-like protein, putative
- 14-3-3-like protein, putative
Sequence:
MSVTLSEPKSSVIVNGRRRITSKFVDGGEMIEEYDVITDDLLLRKYRSRTTLGGFSAWEVEVGNEASTRNLDKELVVETSGSPEVVKQDALEFYVFRIRNLPYAKEVFSVAVEHSKPTDMGEIVVRTSNKKYFKRLSIPDMNRRNLKLDPAQLSFDVQHNTLIIRYKKPLVVLAAESAAKKERASLPAKRIDDADSRTSCNQQ
Protein: Chromobox protein homolog 7 (Q8VDS3)
Organism: Mus musculus (Mouse)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3) (By similarity). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3). Trimethylation at 'Lys-27' (H3K27me3) is important for chromatin recruitment. May possibly also bind trimethylated lysine residues in other proteins (in vitro). Binds non-coding, single-stranded RNA and double-stranded RNA. Plays a role in the timely repression of differentiation-specific genes in pluripotent embryonic stem cells to maintain the undifferentiated state. Regulator of cellular lifespan by maintaining the repression of CDKN2A, but not by inducing telomerase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:14647293, ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:20541999}. Chromosome {ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}. Note=Requires trimethylation at 'Lys-27' (H3K27me3) for the localization to chromatin (PubMed:22226355). Localizes to facultative heterochromatin and to the inactivated X chromosome in females (PubMed:16537902). {ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}.
Interaction partners:
- Polycomb complex protein BMI-1
- E3 ubiquitin-protein ligase RING2
- E3 ubiquitin-protein ligase RING1
- Histone-lysine N-methyltransferase EZH2
- Polycomb group RING finger protein 2
- Polycomb protein Suz12
- Chromobox protein homolog 8
- Chromobox protein homolog 2
- Polycomb group RING finger protein 1
- Polycomb group RING finger protein 6
Sequence:
MELSAIGEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVMAYEEKEERDRASGYRKRGPKPRRLLLQESAAPDVVQTPGDWEPMEQAPEEEAEADLTNGPPPWTPTLPSSEVTVTDITANSVTVTFREAQAAEGFFRDRNEKL
Protein: Acetylcholine receptor subunit alpha (P25108)
Organism: Rattus norvegicus (Rat)
Function: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Acetylcholine receptor subunit beta
- Acetylcholine receptor subunit delta
- Acetylcholine receptor subunit epsilon
- Neuronal acetylcholine receptor subunit alpha-9
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit alpha-3
- Neuronal acetylcholine receptor subunit beta-2
- Neuronal acetylcholine receptor subunit beta-4
- Neuronal acetylcholine receptor subunit beta-3
- Neuronal acetylcholine receptor subunit alpha-5
Sequence:
MELTAVLLLLGLCSAGTVLGSEHETRLVAKLFKDYSSVVRPVGDHREIVQVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDVVLYNNADGDFAIVKFTKVLLDYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKEARGWKHWVFYSCCPNTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTSLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHIMPEWVRKVFIDTIPNIMFFSTMKRPSRDKQEKRIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGVKYIAETMKSDQESNNASEEWKYVAMVMDHILLGVFMLVCLIGTLAVFAGRLIELHQQG
Protein: Expressed protein (SPFH/Band 7/PHB domain-containing membrane-associated protein family) (Q9ZQ87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648}.
Interaction partners:
- At5g54100
- SPFH/Band 7/PHB domain-containing membrane-associated protein family
- Prohibitin-4, mitochondrial
- Protein OS-9 homolog
- Prohibitin-2, mitochondrial
- ATP-dependent zinc metalloprotease FTSH 10, mitochondrial
- ATP-dependent zinc metalloprotease FTSH 3, mitochondrial
Sequence:
MDAQQRRTDIPRAPPVGEPGGDISSILIAFGVFAAIAALVMFPSSLVHQVPEGHVGAYWRGGALLNIITEPGFHLKLPFITNYEPVQVTLQTDQVRDIPCGTKGGVLITFEKIEVVNRLRKDFVYDTLLNYGVNYDNTWIYDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRYAPGIEILSVRVTKPKIPESVRRNFEQMEEERTKVLIAIEKQRVAEKEAETKKIMAISEAEKNANVSKILMQQKLTEKDSSRREADIENQMYLDRQKSLADADYYRVLREAEANKLKLTPEFLELKFIDAIARNTKIFFGDKVPNMVLDQRLLGNFLNHSTKDKDGSLEMATDT
Protein: Electrogenic aspartate/glutamate antiporter SLC25A13, mitochondrial (Calcium-binding mitochondrial carrier protein Aralar2) (ARALAR-related gene 2) (ARALAR2) (Citrin) (Mitochondrial aspartate glutamate carrier 2) (Solute carrier family 25 member 13) (Q9UJS0)
Organism: Homo sapiens (Human)
Function: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle. Also mediates the uptake of L-cysteinesulfinate by mitochondria in exchange of L-glutamate and proton. Can also exchange L-cysteinesulfinate with aspartate in their anionic form without any proton translocation.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10642534, ECO:0000269|PubMed:11566871}; Multi-pass membrane protein {ECO:0000269|PubMed:11566871}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim13
- Argininosuccinate synthase
- Mitochondrial import inner membrane translocase subunit Tim8 A
- Mitochondrial import inner membrane translocase subunit Tim23
- Electrogenic aspartate/glutamate antiporter SLC25A12, mitochondrial
- Non-selective voltage-gated ion channel VDAC1
- Mitochondrial import inner membrane translocase subunit Tim22
- Mitochondrial import inner membrane translocase subunit Tim9
Sequence:
MAAAKVALTKRADPAELRTIFLKYASIEKNGEFFMSPNDFVTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALFMVAFQLFDKAGKGEVTFEDVKQVFGQTTIHQHIPFNWDSEFVQLHFGKERKRHLTYAEFTQFLLEIQLEHAKQAFVQRDNARTGRVTAIDFRDIMVTIRPHVLTPFVEECLVAAAGGTTSHQVSFSYFNGFNSLLNNMELIRKIYSTLAGTRKDVEVTKEEFVLAAQKFGQVTPMEVDILFQLADLYEPRGRMTLADIERIAPLEEGTLPFNLAEAQRQKASGDSARPVLLQVAESAYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELMYKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKLTVNDFVRDKFMHKDGSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDLGFFGIYKGAKACFLRDIPFSAIYFPCYAHVKASFANEDGQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGVTLLTYELLQRWFYIDFGGVKPMGSEPVPKSRINLPAPNPDHVGGYKLAVATFAGIENKFGLYLPLFKPSVSTSKAIGGGP
Protein: Paired box 8 (G3V3F3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDSCVATKSLSPGHTLIPSSAVTPPESPQSDSLGSTYSINGLLGIAQPGSDKRKMDDSDQDSCRLSIDSQSSSSGPRKHLRTDAFSQHHLEPLECPFERQHYPEAYASPSHTKGEQ
Protein: Propanediol dehydratase small subunit (EC 4.2.1.28) (Diol dehydratase small subunit) (DDH small subunit) (Propanediol utilization protein PduE) (O31042)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol (1,2-PD) to propionaldehyde. Required for S.typhimurium growth on 1,2-PD as the sole carbon and energy source. Localized in the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation.
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:10498708, ECO:0000269|PubMed:11844753, ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:21821773}. Note=Probably located inside the BMC shell. {ECO:0000269|PubMed:10498708}.
Interaction partners:
- Propanediol dehydratase medium subunit
- Propanediol dehydratase large subunit
- Propanediol dehydratase-reactivating factor small subunit
- Propanal dehydrogenase
- Bacterial microcompartment shell protein PduB
- Propanediol dehydratase-reactivating factor large subunit
- 1-propanol dehydrogenase PduQ
- Corrinoid adenosyltransferase PduO
- Bacterial microcompartment shell protein PduK
- Phosphate propanoyltransferase
Sequence:
MNTDAIESMVRDVLSRMNSLQGDAPAAAPAAGGTSRSAKVSDYPLANKHPEWVKTATNKTLDDFTLENVLSNKVTAQDMRITPETLRLQASIAKDAGRDRLAMNFERAAELTAVPDDRILEIYNALRPYRSTKEELLAIADDLENRYQAKICAAFVREAAGLYVERKKLKGDD
Protein: Pleiomorphic adenoma gene-like 1 (Q3UQW2)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAPFRCQKCGKSFVTLEKFTIHNYSHSRERPFKCSKAECGKAFVSKYKLMRHMATHSPQKIHQCTHCEKTFNRKDHLKNHLQTHDPNKISYACDDCGKKYHTMLGYKRHLALHSASNGDLTCGVCTLELGSTEVLLDHLKSHAEEKANQAPREKKYQCDHCDRCFYTRKDVRRHLVVHTGCKDFLCQFCAQRFGRKDHLTRHTKKTHSQELMQENMQAGDYQSNFQLIAPSTSFQIKVDPMPPFQLGAAPENGLDGGLPPEVHGLVLAAPEEAPQPMPPLEPLEPLEPLEPLEPMQSLEPLQPLEPMQPLEPMQPLEPMQPLEPLEPLEPMQPLEPMQPLEPMQPMLPMQPMQPMQPMQPMLPMQPMLPMQPMQPMQPMLPMPEPSFTLHPGVVPTSPPPIILQEHKYNPVPTSYAPFVGMPVKADGKAFCNVGFFEEFPLQEPQAPLKFNPCFEMPMEGFGKVTLSKELLVDAVNIAIPASLEISSLLGFWQLPPPTPQNGFVNSTIPVGPGEPLPHRITCLAQQQPPPLPPPPPLPLPQPLPVPQPLPQPQMQPQFQLQIQPQMQPQMQLQPLQLQLPQLLPQLQPQQQPDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEEEQEEAEEEAEEGAEEGAEPEAQAEEEEEEEEAEEPQPEEAQIAGLVYKKWTV
Protein: Zinc-finger homeodomain protein 13 (AtZHD13) (Homeobox protein 27) (AtHB-27) (Q9FMY7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcription factor.
Subcellular location: Nucleus {ECO:0000250}. Note=Interactions with MIF proteins prevent nuclear subcellular location and leads to a scattered repartition throughout the cytoplasm. {ECO:0000250}.
Interaction partners:
- Zinc-finger homeodomain protein 10
- Pathogenesis-related homeodomain protein
Sequence:
MDEIKPKKEENSKRRRNVKPICRETGDHVHYLPTCKTKPKPTRTHHAPPPILDSIFKVTHKPHYYECRKNHAADIGTTAYDGCGEFVSSTGEEDSLNCAACGCHRNFHREELIPENGGVTETVLEVLKISSCQFRRIFCSPYGGGKSEGKKKKKEKESYGGDPIIKDRFGGAEEEEGIVKRLKTKFTAEQTEKMRDYAEKLRWKVRPERQEEVEEFCVEIGVNRKNFRIWMNNHKDKIIIDE
Protein: Cytochrome P450 86A22 (EC 1.14.14.129) (Long-chain acyl-CoA omega-monooxygenase) (B3RFJ6)
Organism: Petunia hybrida (Petunia)
Function: Fatty acyl-CoA omega-hydroxylase essential for the production of omega-hydroxy fatty acids and the biosynthesis of triacylglycerol-/diacylglycerol-based estolide polyesters in the stigma. Substrate preference is 16:0-CoA > 18:1-CoA > 18:0-CoA.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEVSTTMMIVAIVAAYLLWFKSITKSMKGPKGPTMWPVVGSLPGLIENGNRMHEWIADNLRACSGTYQTCICAIPFLARKQLVTVTCDPKNLEHILKVRFDNYPKGPTWQAVFHDLLGEGIFNSDGDTWLFQRKTAALEFTTRTLRQAMGRWVNRAIKNRFCPILEMAQVQGKPVDLQDLLLRLTFDNICGLAFGKDPETLSPELPENNFATSFDRATEATLHRFIMPEFVWKLKKMLGLGLEVSLNNSLKQVDNYMTDVINTRKLELLNHQNGGPQHDDLLSRFMKKKESYSDKFLQHVALNFILAGRDTSSVALSWFFWLVSSNPRVEEKILVEICTILAETRGNDTSKWLEEPLVFEEVDQLMYLKAALSETLRLYPSVPEDSKHVISDDYLPDGTFVPAGSNITYSIYSTGRMKFIWGEDCLEFKPERWMSQDGDKFQVQDTFRFVAFNAGPRICLGKDLAYLQMKSIAAAVLLRHRLAVAPGHKVEQKMSLTLFMKDGLVMNVTPRDLTPILAKIEKFGKVESCAGEHHLINNGIHQPGSIAVNGIAA
Protein: F-box domain-containing protein (Q17896)
Organism: Caenorhabditis elegans
Interaction partners:
- IBR domain-containing protein
- Uncharacterized protein
- DUF19 domain-containing protein
Sequence:
MSWPTLTVRLQQKVIRYLDYESRCNLRICSKDDKDSVDSVKFNPKTLMLYEITSDMSEEKTIVRMQIDTFKMWFIGKNNITKVDKSWNGELVDELSELKQENRYDVIRRYLTRMSLDGIIQAESIKLDDLSFSPPETLKFKCDNLEASYIGNNHDALWMKQFILEFKNLTIIKYHPHEDIGFTYSELKVSNSLNLNCDIGITDKDLLEIKATSLNISSQLITVEGAKKALERFLKRGKKTDTFVLEIRRPENFNAQEHIIPKSLVIRKIIRRGETEDEYYGKIFRGFENENGVQDVRDFNSSLMGDKLIVSCSVYEKSETPCQLYPFYYSYG
Protein: IS1538, resolvase (P95116)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MNLATWAERNGVAPGTAYRWFRAGLLSVMARRVGRLILVDEPAGDAGMRSPTAVYARVSSADQKADLDRQVARVTAWATAQQMPVDKVVTEVGSAFNEHRRKFLSLLRDPSVHRIVVEHRDRFCRLGSKYVQAAFAAQGRELVVVDSAEVDDDLVRDMTEILTSMCARLYGKRAAENRTKRALAAAAGEDHEAA
Protein: Vacuolar protein sorting-associated protein 35 (Q8IIQ6)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 26
- Phosphoinositide-binding protein, putative
- Sortilin
- GTPase-activating protein, putative
- Vacuolar protein sorting-associated protein 9, putative
- Ras-related protein RAB7
Sequence:
MSTYKDNNNHNNHNSNMNTIDQKKFLDECIFVVKEQSFYMKQALENGSLRDTLKYASNMLCELRTSHLSPKYYYELYMLIFNELQHLDNFISDKKKHKKKFIDIYESVQHAGNIIPRLYLLIIVGRNYIKNKDIKAKYILKDMTELCKGVQHPLRGLFLRYFLIQMCKDRIPDTGSEYEEAGGGDINDAFEFLLTNFYESLKLWSRMNDKVLKVPNMIQDDNTMNSKIKILKEKMDVKMLVGSILVRMSQLEGMTKQYYIENCLPKILLYLSNINDCLIQQYIFESIVQVFSDECHIYSLEILLNAILKMNTSIDFKSILITLLKRLRSFIEANNKCDLPKDIDIFNLFYDHLVVYVNRTLDTYTKVNYNDSINRSPNEDHHGYTHNDLSKGKAKDIINNNDNNNDDNNNNKDNDDNNNNNNNNNNNNNNNNNYNYNHNNNQDRYNISKGNVQNGHIKIENMNQTNNDLNNNNIINNMGHINTNDLNKNNTGKNCTIVNTDEFVNNVVKMLQVIYEFIFLCIRIYDDDIIISKLFGLPYTIVSNVNMNNDTICEEIISIIVLPFNYLGLSALNARNMQTLLNSITEKHKKKLSLDIIDAIIECKKKYITYEDVEKILKYISYIFHEKDKKNKNNDEDIFNLENNNSAYTCEKICKFFHIITNTKNIEEKYNICMLFYKYISNSTYLVHLLPTIIFTLLHVVTQITKLGQEDHFNQNDDKNNNMNTIDTIDSNNNNNDNNSNCNNDNSNIDSNHTMDNEKKEDFINSSDSYNIYPNDNDKQNLNNYLHNNQNNFILDEKKINQYNIYVKNIFKFIHTNLLTVASQMPILTFKLFLYSAIVVNNYNSFVQTHEFLTFDNLEAICYEFITQPLIIYEEDINISAQQFDCIVWIVGILCTHINLLDNENYNNIALKLTQHANKLLKKKDQCIGVLKCSHLYWENKKYRNSNKVIECLQKSIKNAEIAIQSNNDNIILFTYMLDKYLYYYEAQNIDVSEETLHYLIDICQDYYNKTNDDTNFKQEYKKVIKYVHDKQKNSNVFQKINIDTSILRS
Protein: Zinc fingers and homeoboxes protein 1 (Q9UKY1)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor. Increases DNMT3B-mediated repressive transcriptional activity when DNMT3B is tethered to DNA. May link molecule between DNMT3B and other co-repressor proteins.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:12237128, ECO:0000269|PubMed:17056598}. Note=Colocalized in the nucleus with DNMT3B.
Interaction partners:
- Nuclear transcription factor Y subunit alpha
- DNA
- Zinc finger MYND domain-containing protein 11
- Nuclear transcription factor Y subunit gamma
Sequence:
MASRRKSTTPCMVLASEQDPDLELISDLDEGPPVLTPVENTRAESISSDEEVHESVDSDNQQNKKVEGGYECKYCTFQTPDLNMFTFHVDSEHPNVVLNSSYVCVECNFLTKRYDALSEHNLKYHPGEENFKLTMVKRNNQTIFEQTINDLTFDGSFVKEENAEQAESTEVSSSGISISKTPIMKMMKNKVENKRIAVHHNSVEDVPEEKENEIKPDREEIVENPSSSASESNTSTSIVNRIHPSTASTVVTPAAVLPGLAQVITAVSAQQNSNLIPKVLIPVNSIPTYNAALDNNPLLLNTYNKFPYPTMSEITVLSAQAKYTEEQIKIWFSAQRLKHGVSWTPEEVEEARRKQFNGTVHTVPQTITVIPTHISTGSNGLPSILQTCQIVGQPGLVLTQVAGTNTLPVTAPIALTVAGVPSQNNIQKSQVPAAQPTAETKPATAAVPTSQSVKHETALVNPDSFGIRAKKTKEQLAELKVSYLKNQFPHDSEIIRLMKITGLTKGEIKKWFSDTRYNQRNSKSNQCLHLNNDSSTTIIIDSSDETTESPTVGTAQPKQSWNPFPDFTPQKFKEKTAEQLRVLQASFLNSSVLTDEELNRLRAQTKLTRREIDAWFTEKKKSKALKEEKMEIDESNAGSSKEEAGETSPADESGAPKSGSTGKICKKTPEQLHMLKSAFVRTQWPSPEEYDKLAKESGLARTDIVSWFGDTRYAWKNGNLKWYYYYQSANSSSMNGLSSLRKRGRGRPKGRGRGRPRGRPRGSKRINNWDRGPSLIKFKTGTAILKDYYLKHKFLNEQDLDELVNKSHMGYEQVREWFAERQRRSELGIELFEENEEEDEVIDDQEEDEEETDDSDTWEPPRHVKRKLSKSDD
Protein: Protocadherin 11 X-linked (A0A0A6YWK0)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MDLLSGTYIFAVLLACVVFQSGAQEKNYTVREEMPENVLIGDLLKDLNLSLIPDKSLTTPMQFKLVYKTGDVPLIRIEEGTGEIFTTGARIDREKLCAGIVLDARCFYEVEVAVLPDEIFRLVKIRFLIEDINDNAPLFPTTVINISIPENSAINSRYSLPAAIDPDIGINGVQNYQLIKSQNIFGLDVIETPEGDKMPQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVADTNDNHPIFIEKEIEVSIPENAPIGSSVTQLHATDADIGENARIHFYFSNLVSNIAKRLFHLNTTTGLITVKEPLDREESPSHKLLVLATDGGSTPARATVLVNVTDINDNVPSIDIRYIVNPTNGTVLLSENAPLNTKIALITVMDKDSEHNGRVTCFTDHEVPFRLRPVFSNQFLLETAAFLDFESTREYAIKLLAADAGKPPLNQSSMLLIKVKDENDNAPVFTQSFISLSVPENNSPGAQLTKISATDADSGQNAEISYMLGFDAPPEFNLDQRTGILTAVKKLDREKQEKYYFTVLAQDNGIPPLMSNATVFVTVLDQNDNSPIFTHNEYNFYVPESLPKHGTVGLITVTDPDYGENSAVTLSILDVNDQFTIDPQSGVIRPNISFDRERQESYTFYVKAEDGGRVSRSSTARVTINVVDVNDNKPIFIDPPSNYSFEWVLPSTNPGTVVFKVVAIDDDIGMNAEVLYSIVGGNTKGLFMIEQTSGNITLKEKCMVSDLGLHRVIVKANDLGQPDSLFNVVNVNFFINESVPNATLIYELVRRSIDAPANQNTETTSASSPTTDYVKIMVAIVAGTITVVLVIFITAVVRCRQPPHLKASQKNKQNSEWVTPNPENRQMIMMKKKKKKKKKHPPKNLLLNFVTIEEAKPDDGENERNSVTLDLPIELEEQTMGKYNWGTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKHHIIQELPLDNTFVGCDSISKCSSSSSDPYSVSECSYPVTTFKAPVSVHIRPTEPRTSTIEICSEI
Protein: Lipoma-preferred partner homolog (Q8BFW7)
Organism: Mus musculus (Mouse)
Function: May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell junction {ECO:0000250}. Note=Found in the nucleus, in the cytoplasm and at cell adhesion sites. {ECO:0000250}.
Interaction partners:
- LIM and SH3 domain protein 1
Sequence:
MSHPSWLPPKSTGEPLGHVPARMETTHSFGNPSISVSTQQPPKKYAPVVAPKPKYNPYKQPGGEGDLLPPPPPPLEDPGTIPPGPGHFPPPPPLDEGAFKVQQGNPGGKTLEERRSSLDAEIDSLTSILADLECSSPYKPRPPQGSASSIASPPVSTPVTGHKRMVIPQQPPLTATKKSATKPQPAPQAAPIPVTPIGTLKPQPQPVPASYTTASTSSRPTFNVQVKSAQPSPHYMAGPSSGQIYGPGPRGYNNQPVPVSGQCPPPPTCVGTDYAYIPPSGHPPESGYGYTSNQGRYYEPYYAAGPSYGGRSEGDTAYGQQVQPNTWKREAAYAPPASGNQNHPGMYPVSGPKKTYITDPVSAPCAPPLQPKGGYPGPMGPPSIPPSFRPEDELEHLTKKMLYDMENPPADDYFGRCARCGENVVGEGTGCTAMDQVFHVDCFTCIVCDVKLRGQPFYAVEKKAYCEPCYINTLEQCSVCSKPIMERILRATGKAYHPHCFTCVMCHRSLDGIPFTVDACGLIHCIEDFHKKFAPRCSVCKEPIMPAPGQEETVRIVALDRDFHVHCYRCEDCGGLLSEGDNQGCYPLDGHILCKTCNSARIRVLTAKASTDL
Protein: Carbamoyl phosphate synthase pyrimidine-specific small chain (EC 6.3.5.5) (Carbamoyl phosphate synthetase glutamine chain 2) (P25993)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Orotidine 5'-phosphate decarboxylase
- Dihydroorotate dehydrogenase B
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase arginine-specific large chain
- Orotate phosphoribosyltransferase
- Carbamoyl phosphate synthase pyrimidine-specific large chain
- Dihydroorotase
- Dihydroorotate dehydrogenase B
- Uracil permease
- Ornithine carbamoyltransferase
Sequence:
MKRRLVLENGAVFEGEAFGSLEHNMGEVVFNTGMTGYQEILSDPSYCGQIVTLTYPLIGNYGINRDDFESITPFVKGLIIKELCELPSNWRSAYTLDEYLKMKNIPGLQGIDTRKLTRMIRTAGALKGTFASSDEDIEAVLKRLNETELPRNQVSQVSAKTAYPSPGRGKRIVLVDFGMKHGILRELNKRKCDVIVVPYNITAEEVLQLKPDGIMLSNGPGDPKDVPEAIEMIKGVLGKVPLFGICLGHQLFALACGANTEKMKFGHRGSNHPVKELATGKVALTSQNHGYTVSSISKTELEVTHIAINDDTIEGLKHKTLPAFTVQYHPEASPGPEDANHLFDRFIEMIETTEKEGEAVCQNA
Protein: 1,3,6,8-tetrahydroxynaphthalene synthase (THNS) (EC 2.3.1.233) (1,3,6,8-tetrahydroxynaphthalene synthesis polyketide synthase type III) (Q54240)
Organism: Streptomyces griseus
Function: Involved in the biosynthesis of melanin but also various secondary metabolites containing a naphthoquinone ring. Catalyzes the iterative condensation of five CoA-linked malonyl units to form a pentaketide intermediate. THNS subsequently catalyzes the dual intramolecular Claisen and aldol condensations of this linear intermediate to produce the fused ring of 1,3,6,8-tetrahydroxynaphthalene (THN).
Interaction partners:
Sequence:
MATLCRPAIAVPEHVITMQQTLDLARETHAGHPQRDLVLRLIQNTGVQTRHLVQPIEKTLAHPGFEVRNQVYEAEAKTRVPEVVRRALANAETEPSEIDLIVYVSCTGFMMPSLTAWIINSMGFRPETRQLPIAQLGCAAGGAAINRAHDFCVAYPDSNVLIVSCEFCSLCYQPTDIGVGSLLSNGLFGDALSAAVVRGQGGTGMRLERNGSHLVPDTEDWISYAVRDTGFHFQLDKRVPGTMEMLAPVLLDLVDLHGWSVPNMDFFIVHAGGPRILDDLCHFLDLPPEMFRYSRATLTERGNIASSVVFDALARLFDDGGAAESAQGLIAGFGPGITAEVAVGSWAKEGLGADVGRDLDELELTAGVALSG
Protein: Neuronal-specific septin-3 (Q9Z1S5)
Organism: Mus musculus (Mouse)
Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Synapse {ECO:0000250}.
Interaction partners:
- Septin-7
- Septin-5
- Septin-6
- Septin-4
- Septin-11
- Septin-8
- Septin-9
- Septin-2
- Septin 12
- Septin-1
Sequence:
MSKGLPEARTDAAMSELVPEPRPKPAVPMKPVSINSNLLGYIGIDTIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRQESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVIRTHLQDLKEVTHNIHYETYRAKRLNDNGGLPPVSVDTEESHDSNP
Protein: Frizzled-8 (Fz-8) (Xfz8) (O93274)
Organism: Xenopus laevis (African clawed frog)
Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Activation by Wnt8, Wnt5A or Wnt3A induces expression of beta-catenin target genes. Displays an axis-inducing activity.
Subcellular location: Membrane {ECO:0000269|PubMed:10097073}; Multi-pass membrane protein {ECO:0000269|PubMed:10097073}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MESLSLSLLLLVSWLQGSQCAAAKELSCQEITVPLCKDIGYNYTYMPNQFNHDTQDEAGMEVHQFWPLVVIHCSPDLKFFLCSMYTPICLEDYKKPLPPCRSVCERARAGCAPLMRQYGFAWPDRMRCDRLPEQGNPDTLCMDYYNRTEQTTAAPSHPEPPKPPARSVPKGRTRVEPPRSRSRATGCESGCQCRAPMVQVSNERHPLYNRVRTGQIPNCAMPCHNPFFSPEERTFTEFWIGLWSVLCFASTFATVSTFLIDMERFKYPERPIIFLSACYLLVSTGYLIRLIAGHEKVACSRGELDLEHIIHYETTGPALCTLVFLLIYFFGMASSIWWVILSLTWFLAAGMKWGNEAIAGYSQYFHLAAWLVPSIKSIAVLALSSVDGDPVAGICFVGNQNLDNLRGFVLAPLVIYLFIGSMFLLAGFVSLFRIRSVIKQGGTKTDKLEKLMIRIGIFSVLYTVPATIVVACFFYEQHNRQGWEVAHNCNSCQPEMAQPHRPDYAVFMLKYFMCLVVGITSGVWIWSGKTLESWRAFCTRCCWGSKATGGSMYSDVSTGLTWRSGTGSSVSCPKQMPLSQV
Protein: Myb-like domain-containing protein (Q57U75)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRNNRTRCTIDDVNGMLARNAQLRNALQERYKQLKMRYEQLAALRAALSPSRGVTLRKLGVRQETADGAEEVRFLDDYTTGGVGNPPFRDAGIYSAKNIVCYAPVPPTRDELRWKGVTLAFPQLAYVHSLAMLPETANSFSKALQWSREEDSALREQVHAYKGARCGPSFWKALGAPGQSRFEVASHYIRLQQLGLIEPGKNDKTMMWIPEEQRDIALREAVWRHLGDEGGIMAAYVEIISVAARKCVYLSEVTCNESLVFPPYVWVKRTTFNWLTSLLIQKAKAPLVRCEGEFSDDTPLCMHFKSDISLKLSAEDMMACLLAFKGEVFGEVGGLRFIERAFLPKNRTYALKATDFMAKREGKKHKLDEEV
Protein: AT04665p (Q6NQW5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLATTSPISYRQLPLRLFQIGPKFRDELKTRFGLMRAKEFLMKDMYSFDVSEETAMETYTVVNAAYDRLFKQLEVPFVKVNAATGIMGGSVSHEYHYVSPVGEDNLLQCSSCGFAGNSEVVKAPASCPSCNSSDLKEVRGVEVAHTFLLGDKYSKPLGATFLNTTGKPQSLVMGCYGIGITRVIAAALEVLSSDHELRWPKLLAPYDVCLIGPKQGSKEQPEAEVIENELLLNVGEICGHQELLHDDRKELTIGKRLLEAKRLGHPLTIVVGAKSVRLDSPKLEVHTSKGETYELDFSETLKLVAEHSQHKKSLERGCFQSETEESKSRSVGHQV