wanglab/gogpt-training-data huggingface dataset:
Protein: RIMS-binding protein 2 (RIM-BP2) (Q9JIR1)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the synaptic transmission as bifunctional linker that interacts simultaneously with RIMS1, RIMS2, CACNA1D and CACNA1B.
Subcellular location: Cell membrane {ECO:0000250}. Synapse {ECO:0000250}. Note=Synaptic plasma membrane. {ECO:0000250}.
Interaction partners:
- Regulating synaptic membrane exocytosis protein 2
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- ELKS/Rab6-interacting/CAST family member 1
Sequence:
MREAAERRQQLELEHEQALAILNAKQQEIQLLQQSKVRELEEKCRVQSEQFNLLSRDLEKFRQHAGSIDLLGSNSVALLDVPLAPGKPFSQYMNGLATSIHKGHEGPTGHYSVIGDYIPLSGDKLESPCVKPSFLLRSSSPRCRFESEMDDDRSSNKSKHSSSGKVHLCVARYSYNPFDGPNENPEAELPLTAGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVDFIQDNESRFAGTLGSEQDQNFLNHSGISLERDSILHLHSPTQVDSGITDNGGGTLDVNIDDIGEDIVPYPRKITLIKQLAKSVIVGWEPPAVPPGWGTVSSYNVLVDKETRMSLALGRRTKALIEKLNTAACTYRISVQCVTSRGNSDELQCTLLVGKDVVVAPSQLRVDNITQISAQLSWLPTNSNYSHIIFLNEEELDIVKAARYKYQFFNLRPNMAYKVKVLAQPHQMPWQLPLEQREKDEACVEFSTLPAGPPAPPQDVTVQAGATTASVQVSWKPPALTPTGLSNGANVTGYGVYAKGQRVAEVIAPTANGAAVELVRLRSLEAKAVSVRTLSAQGESMDSALAAIPPDLLVPPAPHPRTAPPPKPLTSDMDTKDLGPHVKVDESWEQSRPPGPAHGHMLEPPDMHSTGPGRRSPSPSRILPQPQGAPVSTTVAKAMAREAAQRVAETSKLEKRSLFLEQSSAGPYANSDEEDGYASPEVKRRGTSVDDFLKGSELGQQPHCCHGDEYHTESSRGSDLSDIMEEDEEELYSEMQLEDGGRRRPSGTSHNALKILGNSALMGRGDRMEHVSRRYSHSGGGPQRHRPMAPSIDEYTGRDHLSPDFYDESETDPGAEELPARIFVALFDYDPLTMSPNPDAAEEELPFKEGQIIKVYGDKDADGFYRGETCARLGLIPCNMVSEIHADDEEMMDQLLRQGFLPLNTPVEKIERSRRSGRGHSVPTRRMVALYDYDPRESSPNVDVEAELLFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEEVPDDVEVHLSDAPPHYSHDPPMRTKAKRVSQPP
Protein: MOB kinase activator 2 (HCCA2) (Mob2 homolog) (Mps one binder kinase activator-like 2) (Q70IA6)
Organism: Homo sapiens (Human)
Function: Stimulates the autophosphorylation and kinase activity of STK38 and STK38L.
Subcellular location: Nucleus {ECO:0000269|PubMed:15067004}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15067004}.
Interaction partners:
- Serine/threonine-protein kinase 38-like
- Serine/threonine-protein kinase 38
- MOB-like protein phocein
Sequence:
MDWLMGKSKAKPNGKKPAAEERKAYLEPEHTKARITDFQFKELVVLPREIDLNEWLASNTTTFFHHINLQYSTISEFCTGETCQTMAVCNTQYYWYDERGKKVKCTAPQYVDFVMSSVQKLVTDEDVFPTKYGREFPSSFESLVRKICRHLFHVLAHIYWAHFKETLALELHGHLNTLYVHFILFAREFNLLDPKETAIMDDLTEVLCSGAGGVHSGGSGDGAGSGGPGAQNHVKER
Protein: Lysophospholipid acyltransferase (LPLAT) (EC 2.3.1.23) (EC 2.3.1.51) (EC 2.3.1.n6) (EC 2.3.1.n7) (1-acyl-sn-glycerol-3-phosphate acyltransferase) (AGPAT) (Lysophosphatidic acid acyltransferase) (LPAAT) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lysophosphatidylserine acyltransferase) (LPSAT) (Sphingolipid compensation protein 4) (Q08548)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Broad specificity membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of various lysophospholipids. Preferentially acylates lysophosphocholine (LPC), but also lysophosphoethanolamine (LPE), lysophosphatidylglycerol (LPG), lysophosphatidic acid (LPA), lysophosphoethanolamine (LPE), lysophosphoinositol (LPI), and lysophosphoserine (LPS). Prefers an acyl residue to an alkyl residue at the sn-1 position of lysophospholipid acceptors. Accepts acyl chains in acyl-CoA from C-2 to C-20, and shows strong preference for unsaturated acyl-CoAs with 16-20 carbons. Together with SLC1, plays a central role in phosphatidic acid (PA) biosynthesis. PA is the intermediate, from which all glycerophospholipids are synthesized. Can also introduce an acyl chain at the sn-1 position of the lysophosphatidylcholine analog 1-hydroxy-2-hexadecyl-sn-glycero-3-phosphocholine (HHPC).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17890783}; Multi-pass membrane protein.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Glycerol-3-phosphate O-acyltransferase 1
- Glycerol-3-phosphate O-acyltransferase 2
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Lysophosphatidic acid:oleoyl-CoA acyltransferase 1
- Phosphatidylserine decarboxylase proenzyme 2
- Choline/ethanolaminephosphotransferase 1
- Phosphatidic acid phosphohydrolase 1
- Phosphatidylethanolamine N-methyltransferase
- Phosphatidate cytidylyltransferase
Sequence:
MYNPVDAVLTKIITNYGIDSFTLRYAICLLGSFPLNAILKRIPEKRIGLKCCFIISMSMFYLFGVLNLVSGFRTLFISTMFTYLISRFYRSKFMPHLNFMFVMGHLAINHIHAQFLNEQTQTTVDITSSQMVLAMKLTSFAWSYYDGSCTSESDFKDLTEHQKSRAVRGHPPLLKFLAYAFFYSTLLTGPSFDYADFDSWLNCEMFRDLPESKKPMRRHHPGERRQIPKNGKLALWKVVQGLAWMILSTLGMKHFPVKYVLDKDGFPTRSFIFRIHYLFLLGFIHRFKYYAAWTISEGSCILCGLGYNGYDSKTQKIRWDRVRNIDIWTVETAQNTREMLEAWNMNTNKWLKYSVYLRVTKKGKKPGFRSTLFTFLTSAFWHGTRPGYYLTFATGALYQTCGKIYRRNFRPIFLREDGVTPLPSKKIYDLVGIYAIKLAFGYMVQPFIILDLKPSLMVWGSVYFYVHIIVAFSFFLFRGPYAKQVTEFFKSKQPKEIFIRKQKKLEKDISASSPNLGGILKAKIEHEKGKTAEEEEMNLGIPPIELEKWDNAKEDWEDFCKDYKEWRNKNGLEIEEENLSKAFERFKQEFSNAASGSGERVRKMSFSGYSPKPISKKEE
Protein: ADP-ribosylation factor 5 (P84084)
Organism: Mus musculus (Mouse)
Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular location: Golgi apparatus. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P84085}. Membrane {ECO:0000250|UniProtKB:P84085}; Lipid-anchor {ECO:0000250|UniProtKB:P84085}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Coatomer subunit beta
- ADP-ribosylation factor GTPase-activating protein 1
- ADP-ribosylation factor GTPase-activating protein 2
- Coatomer subunit beta'
- ADP-ribosylation factor 4
- Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- Rab11 family-interacting protein 3
- ADP-ribosylation factor GTPase-activating protein 3
- RAB6-interacting golgin
Sequence:
MGLTVSALFSRIFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVQESADELQKMLQEDELRDAVLLVFANKQDMPNAMPVSELTDKLGLQHLRSRTWYVQATCATQGTGLYDGLDWLSHELSKR
Protein: Protein REVEILLE 2 (MYB family transcription factor Circadian 1) (F4K5X6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Positive regulator for cold-responsive gene expression and cold tolerance. Part of a regulatory feedback loop that controls a subset of the circadian outputs and modulates the central oscillator. Negatively self-regulates its own expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Gb|AAD18119.1
- Two-component response regulator-like APRR5
- TRF-like 6
- Two-component response regulator-like APRR1
- At2g42780/F7D19.22
Sequence:
MAMQERCESLCSDELISSSDAFYLKTRKPYTITKQREKWTEAEHEKFVEALKLYGRAWRRIEEHVGTKTAVQIRSHAQKFFTKVARDFGVSSESIEIPPPRPKRKPMHPYPRKLVIPDAKEMVYAELTGSKLIQDEDNRSPTSVLSAHGSDGLGSIGSNSPNSSSAELSSHTEESLSLEAETKQSLKLFGKTFVVGDYNSSMSCDDSEDGKKKLYSETQSLQCSSSTSENAETEVVVSEFKRSERSAFSQLKSSVTEMNNMRGFMPYKKRVKVEENIDNVKLSYPLW
Protein: RE23033p (Q5BIC7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MTKSALKSAFYKNQAPISEQNRSQIVSRMSLLRTILLIIISIHFKLAHADQVVLLDTTREATLEWTRYPYGPQAQTPGWVEESFTDFVKGINWRSYVVCDVAYHNVNNWLWSPFIDRGSANRLYIEIQFTIRDCSLFPGNALSCKETFSLLFYEFDAATREPPPWQTDSYRLIARIAAGEGRFNQNSDVDINTEVKSIAVNKKGVYFAFRDQGACISVLAVKVYYITCPAVTENFAHFNETPTGREITIIEKQNGTCVDNAEPYETPTYLCKGDGKWTILTGGCRCKAGYEPNYTNKTCTECPLGTFKSPEVTKCTPCPPNSNASKTGSPFCKCASGFYRHPNDGRHMPCYSPPAAPTNLTLLFVDQTSAIISWSAPAKNESFSSETNSKIYHSDIVYKIKCNICSPNVVYNPSTDTFNETKITLTNLEPVTTYTVQIHAINSVSHINEFKRHSNESSLVAVSDIVFSNTSLLNIPLDLNEVKTGQAEIVFTTESVLLSTVFNLRILAITNKDADLEWDKPVQSDFPLEFYEVRWFPKVELDAINKSALNTKETKAHIVGLLENTEYGFQVRCKTNNGFGSYSNMIYAQTLQSVGSVYDDSVQIRFIAGAIVTGVLFLVIFIIATVYFMRSKHQDDLDKKSTNHLPLPLDYASNEVNSMDTTPIVKKLHLNVTTPLFGNSRSYVDPHTYEDPNQAIREFAREIDANYITIEAIIGVENLAMYVVVD
Protein: Bone morphogenetic protein 1 (BMP-1) (EC 3.4.24.19) (Mammalian tolloid protein) (mTld) (Procollagen C-proteinase) (PCP) (P98063)
Organism: Mus musculus (Mouse)
Function: Metalloprotease that plays key roles in regulating the formation of the extracellular matrix (ECM) via processing of various precursor proteins into mature functional enzymes or structural proteins. Thereby participates in several developmental and physiological processes such as cartilage and bone formation, muscle growth and homeostasis, wound healing and tissue repair. Roles in ECM formation include cleavage of the C-terminal propeptides from procollagens such as procollagen I, II and III or the proteolytic activation of the enzyme lysyl oxidase LOX, necessary to formation of covalent cross-links in collagen and elastic fibers. Additional substrates include matricellular thrombospondin-1/THBS1 whose cleavage leads to cell adhesion disruption and TGF-beta activation (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:20181949}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20181949}. Secreted {ECO:0000250|UniProtKB:P13497}. Note=Co-localizes with POSTN in the Golgi.
Interaction partners:
- Periostin
- Chordin
- Inactive rhomboid protein 2
- Protein-lysine 6-oxidase
- Collagen alpha-1
- Fibronectin
- Apolipoprotein A-I
- Complement C1r-A subcomponent
- Complement C1r-B subcomponent
- Biglycan
Sequence:
MPGVARPPLPLLSLPLLLLLLLLPRAGRPLDLADYTYDLGEEDAPELLNYKDPCKAAAFLGDIALDEEDLRAFQVQQAAVLRQQTARRPSIKAAGNSSALGGQGTSGQPQRESRGRWRGRPRSRRAATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPSIGQRTRLSKGDIAQARKLYKCPACGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSMDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGGKLPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEAICGGDVKKDNGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSNLIGRYCGYEKPDDIKSTSSRLWLKFVSDGSINKAGFAVNFFKEVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRCEAACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCKEAGCEHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFVEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLATGNRMFLRFYSDNSVQRKGFQASHSTECGGQVRADVKTKDLYSHAQFGDNNYPGGVDCEWVIVAEEGYGVELVFQTFEVEEETDCGYDYIELFDGYDSTAPRLGRYCGSGPPEEVYSAGDSVLVKFHSDDTISKKGFHLRYTSTKFQDTLHSRK
Protein: DNA-cytosine methyltransferase (EC 2.1.1.37) (Type II methyltransferase M.EcoKDcm) (M.EcoKDcm) (P0AED9)
Organism: Escherichia coli (strain K12)
Function: This methylase recognizes the double-stranded sequence 5'-CCWGG-3', methylates C-2 on both strands.
Interaction partners:
- DNA mismatch endonuclease Vsr
- S-adenosylmethionine synthase
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
- S-adenosylmethionine decarboxylase proenzyme
- DNA adenine methyltransferase YhdJ
- Uncharacterized protein YedJ
Sequence:
MQENISVTDSYSTGNAAQAMLEKLLQIYDVKTLVAQLNGVGENHWSAAILKRALANDSAWHRLSEKEFAHLQTLLPKPPAHHPHYAFRFIDLFAGIGGIRRGFESIGGQCVFTSEWNKHAVRTYKANHYCDPATHHFNEDIRDITLSHKEGVSDEAAAEHIRQHIPEHDVLLAGFPCQPFSLAGVSKKNSLGRAHGFACDTQGTLFFDVVRIIDARRPAMFVLENVKNLKSHDQGKTFRIIMQTLDELGYDVADAEDNGPDDPKIIDGKHFLPQHRERIVLVGFRRDLNLKADFTLRDISECFPAQRVTLAQLLDPMVEAKYILTPVLWKYLYRYAKKHQARGNGFGYGMVYPNNPQSVTRTLSARYYKDGAEILIDRGWDMATGEKDFDDPLNQQHRPRRLTPRECARLMGFEAPGEAKFRIPVSDTQAYRQFGNSVVVPVFAAVAKLLEPKIKQAVALRQQEAQHGRRSR
Protein: Exportin-5 (Exp5) (Ran-binding protein 21) (Q924C1)
Organism: Mus musculus (Mouse)
Function: Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi) (By similarity). Mediates nuclear export of ADAR/ADAR1 in a RanGTP-dependent manner (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9HAV4}. Cytoplasm {ECO:0000250|UniProtKB:Q9HAV4}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q9HAV4}.
Interaction partners:
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran, testis-specific isoform
- GTP-binding nuclear protein Ran
- Endoribonuclease Dicer
- Protein argonaute-2
- Ribonuclease 3
- Microprocessor complex subunit DGCR8
- RISC-loading complex subunit TARBP2
- Protein argonaute-1
- Protein argonaute-4
Sequence:
MEMEQVNALCEELVKAVTVMMDPSSTQRYRLEALKFCEEFKEKCPICVPCGLKLAEKTQIAIVRHFGLQILEHVVKFRWNSMSRLEKVYLKNSVMELIANGTLRILEEENHIKDVLSRIVVEMIKREWPQHWPDMLMELDTLFRQGETQRELVMFILLRLAEDVVTFQTLPTQRRRDIQQTLTQNMERILNFLLNTLQENVNKYQQMKTDSSQEAEAQANCRVSVAALNTLAGYIDWVSLNHITAENCKLVETLCLLLNEQELQLGAAECLLIAVSRKGKLEDRKRLMILFGDVAMHYILSAAQTADGGGLVEKHYLFLKRLCQVLCALGNLLCALLALDANIQTPINFGMYLESFLAFTTHPSQFLRSSTHMTWGALFRHEVLSRDPALLAVIPKYLRASMTNLVKMGFPSKTDSPSCEYSRFDFDSDEDFNAFFNSSRAQHGEVVRCVCRLDPKTSFQMAAEWLKYQLSASIDTGPVNSCSTAGTGEGGFCSIFSPSYVQWEAMTFFLESVINQMFRTLDKEELPVSDGIELLQLVLNFEIKDPLVLSCVLTNVSALFPFVTYKPAFLPQVFSKLFSFVTFESVGESKAPRTRAVRNVRRHACSSINKMCRDYPDLVLPNFDMLYSHVKQLLSNELLLTQMEKCALMEALVLVSNQFKDYERQKLFLEELMAPVVNIWLSEEMCRALSDIDSFIAYVGADLKSCDPAVEDPCGLNRARMSFCVYSILGVMRRTSWPSDLEEAKAGGFVVGYTPSGNPIFRNPCTEQILRLLDNLLALVRTHNTLYTPEMLTKMAEPFTKALDIVESEKTAILGLPQPLLEFNDHPVYRTTLERMQRFFGILYENCYHILGKAGPSMQQDFYTVEDLASQLLGSAFVNLNNIPDFRLRSMLRVFVKPLVLFCPSEHYETLISPILGPLFTYLHMRLSQKWHVINQRSILCGEDEIAEDNPESQEMLEEQLVRMLTREAMDLIMACCVSKKTADHTAAPTADGDDEEMMATEVAPSSVVELTDLGKCLMKHEDVCTALLITAFNSLTWKDTLSCQRATTQLCWPLLKQVMSGTLLADAVTWLFTSVLKGLQMHGQHDGCMASLVHLAFQIYEALRPRYLEIRAVMEQIPEINKESLDQFDCKLLNPSLQKAADKRRKDHFKRLIAGCIGKPLGEQFRKEVHIKNLPWLFKKPKPMLETEVLDSEEGGLATIFEP
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (Q6FPV9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Transcription factor
- protein-tyrosine-phosphatase
- mitogen-activated protein kinase kinase
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- mitogen-activated protein kinase kinase
- Tyrosine-protein phosphatase CDC14
- mitogen-activated protein kinase kinase
- GTP-binding protein RHO1
Sequence:
MDVERQTFKVFNQDFTIDKRFELIKEIGHGAYGIVCSARFTEASEETTVAIKKVTNIFSKTLLCKRSLRELKLLRHFRGHKNITCLYDMDIVFYPDGSINGLYLYEELMECDMHQIIKSGQALTDAHYQSFTYQILCGLKYIHSADVLHRDLKPGNLLVNADCQLKICDFGLARGYSENPEENNQFLTEYVATRWYRAPEIMLSYQGYTKAIDIWSTGCILAEFLGGKPLFKGKDYVDQLNRILQVLGTPPDETLRRVGSKNVQDYIHQLGYIQKIPFSELFPNANEDALDLLEGMLAFDPQKRITVDKALEHPYLTIWHDPADEPECNEKFEFSFESVNEMEDLKRMVVDEVQSFREFVRQPLMDDKSQEDEQQQGSPENYQQTSPTNISPQRLHNNGSHDLLQEPEFLTQTPNQNSTIPDQLQESFVGIHSDNLPEHDTDFPPRPQENILASPMGLPSASDRNSMNNDSFLDLERELEFGLDRRYL
Protein: Beta-agarase B (EC 3.2.1.81) (Q9RGX8)
Organism: Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
Function: Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place. Also tolerant to hybrid substrates containing C6-sulfate groups at the -4, +1, and +3 positions.
Subcellular location: Cell outer membrane {ECO:0000305|PubMed:15456406}; Lipid-anchor {ECO:0000305|PubMed:15456406}.
Interaction partners:
Sequence:
MYLIYLRLVFCCALLLGCGDNSKFDSATDLPVEQEQEQETEQEGEPEESSEQDLVEEVDWKDIPVPADAGPNMKWEFQEISDNFEYEAPADNKGSEFLEKWDDFYHNAWAGPGLTEWKRDRSYVADGELKMWATRKPGSDKINMGCITSKTRVVYPVYIEARAKVMNSTLASDVWLLSADDTQEIDILEAYGADYSESAGKDHSYFSKKVHISHHVFIRDPFQDYQPKDAGSWFEDGTVWNKEFHRFGVYWRDPWHLEYYIDGVLVRTVSGKDIIDPKHFTNTTDPGNTEIDTRTGLNKEMDIIINTEDQTWRSSPASGLQSNTYTPTDNELSNIENNTFGVDWIRIYKPVEK
Protein: Eyes absent homolog (EC 3.1.3.48) (Q66HX1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Centromere protein U
- Sine oculis homeobox homolog 1a
Sequence:
MAAYGQTQYSPALQPAGPYTPYTHHTQGYSMTSYNIKTEDGLSHSPGQSSLLGYTPNFSGTPPGQTLYSYSHGGSISSGIFQGANSITGSTPFSPAQQDFSTYSSYSQSQYSPYYNTHYNSPYITASNITPSAITTAIPYQHTDHPAVSTNHSPESHTAEYQAPTSPPTPGKDQDGAPPRRSADGKLRGRKRASDPVPPLDSDIERVFVWDLDETIIIFHSLLTGTFSTRFGKDSGKAVSLGLWMEEMIFNLADSRLFFNDLEECDQVHIDDVASDDNGQDLSTYNFGTDGFQTPAGGGSLCLGSGVHGGVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGSPKREEWLQLRREMEVLTDLWLTQALKALALINSRPNCVNVLVTTTQLIPALSKVLLYGLGGAFPIENIYSATKTGKESCFERVTQRFGRRAVYVVVGDGIEEETVAKKKNMPFWRVTCRADLEALSHALELDYL
Protein: 3-isopropylmalate dehydratase (EC 4.2.1.33) (Alpha-IPM isomerase) (IPMI) (Isopropylmalate isomerase) (P07264)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Interaction partners:
- 2-isopropylmalate synthase
- 3-isopropylmalate dehydrogenase
- 2-isopropylmalate synthase 2, mitochondrial
- Dihydroxy-acid dehydratase, mitochondrial
- Ketol-acid reductoisomerase, mitochondrial
- Acetolactate synthase catalytic subunit, mitochondrial
- Regulatory protein LEU3
- Acetolactate synthase small subunit, mitochondrial
- Homocitrate synthase, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
Sequence:
MVYTPSKGPRTLYDKVFDAHVVHQDENGSFLLYIDRHLVHEVTSPQAFEGLENAGRKVRRVDCTLATVDHNIPTESRKNFKSLDTFIKQTDSRLQVKTLENNVKQFGVPYFGMSDARQGIVHTIGPEEGFTLPGTTVVCGDSHTSTHGAFGSLAFGIGTSEVEHVLATQTIIQAKSKNMRITVNGKLSPGITSKDLILYIIGLIGTAGGTGCVIEFAGEAIEALSMEARMSMCNMAIEAGARAGMIKPDETTFQYTKGRPLAPKGAEWEKAVAYWKTLKTDEGAKFDHEINIEAVDVIPTITWGTSPQDALPITGSVPDPKNVTDPIKKSGMERALAYMGLEPNTPLKSIKVDKVFIGSCTNGRIEDLRSAAAVVRGQKLASNIKLAMVVPGSGLVKKQAEAEGLDKIFQEAGFEWREAGCSICLGMNPDILDAYERCASTSNRNFEGRQGALSRTHLMSPAMAAAAGIAGHFVDIREFEYKDQDQSSPKVEVTSEDEKELESAAYDHAEPVQPEDAPQDIANDELKDIPVKSDDTPAKPSSSGMKPFLTLEGISAPLDKANVDTDAIIPKQFLKTIKRTGLKKGLFYEWRFRKDDQGKDQETDFVLNVEPWREAEILVVTGDNFGCGSSREHAPWALKDFGIKSIIAPSYGDIFYNNSFKNGLLPIRLDQQIIIDKLIPIANKGGKLCVDLPNQKILDSDGNVLVDHFEIEPFRKHCLVNGLDDIGITLQKEEYISRYEALRREKYSFLEGGSKLLKFDNVPKRKAVTTTFDKVHQDW
Protein: Kinesin, putative (Q582P0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSMHRDLLRIRRQTSNLVSSPSPPSSRASPRARVSSARGEQRQGASEAVHVAVRVRPLSVNEAGQDVIVSMDPSAKKIFVRNRGEEQQEFPFELPVWSCGGNALNGSPPVSQAALYKMVGQPLLDHAFEGFNSTLMVYGSTGSGKTYTMMGDMDGGFLGEDEDVLNDGEEGIVPRLCREMFQKIRDRSVSLSDGGTLTWDVHASYVEVYCEKISDLLNNGAPVTIREVITDNEAHFALNGAQRVNVRNSAEILHLLKIGNRHRKTASTAMNERSSRSHAIFVVELTEMLVVRGPDGECVGAPGKFLTVRLVDLAGSERVGEAGMSGQLFKEGVDINCSLFTLGMVIEALSDPSRRHMRPPYRDSTLTKILKDAFGGNSKTTMICTIAPTEAQRVHTVQTLQYGLKARRIVNKPCAKRGPSAKELRKASEEMLSLRQKRRERQPQGTGLEESYADLRRAGDGGLHNGGALRHSESSSEGKETSLGGSNFATDEERDRYRRKMEELEEEIERARARYREQGRELQNIRRESAAEAEVRLRALEAQFNEKENHLKRKGHEIQRKHRDAESRLKEFKNFSEERISDLLRAQGELKDKLHEKELAVGQRERELQEAQSRAEEEVSRLHQRMMQQERKWLERHKALEAEICAQEDKMRDRLRDAMERMRNVEEVAARRESELHRKWLDAQQATRELHHKLAESEAEKARQISQDRRETTKRESELAHKLEETERGRKALEREAVSLKTELDVLKEDYEMLAKNSREGCDAEARLLPLEEELKRREERLQQREEQAQASLDEVLKKQEELDRLHLAVIAKADAIEKDAVAALRERESRLQKREDELKSLEHELEARSAVLDVEAKYKSMEYDTKESGAEALASRERRATELLQDELQEALQRVHLDMKQREEKFDRMEDDIKRCREQLENLYNERDEMLRRASTSSAGRSCVFDSPLPVPPRGCRRCRSGTSWPSNCSTMGTGEENDASLSGRQFSPNQSSASQQEPRCSENGVEGGRSSELRPISALAGESVCLWLKNMLITMEERSRGLLEDLCYHEYSVLERMTSIGSLFSFGENAPNTRSPEVAARVVDRTSVSACSDHLRGGFRLGSICGVVPHDAPCVPSLMHTEADCGLRDAASEHEQLAQRIVAFERLQHQREVEFQQKDEQIREYLVEVEAMDRERMAMYRLKEEEHEAAAAQLQMAKREFDHRVNCMQQTLFCRGAQQHAESIVLQEAAERENIFRLFNIQLHKIFAHERNMAHHTNCVDLLRQREEVITLEEAQLQKRISQLKDEEDEWKRRRSTEETQILTYLLELQNEDMLRKQAIGEKGSREDTAKYCEDAELGVAGLCNVMHRVRDHTQKCELAVQKMESELEQQADAEKVLEEREAAVERRRRELSTSMESRERSLLDREMELEELTRRLKGDIQKRELAIQKMESELEQQADAEKVLEEREAAVERRRRELSTSMESRERSLLEQEVDLRKLSTKAGDNCRKRPGSRVAHNQEGSYYVDIKKLLEVCGFQLPGGKVEFPDGADTPIELTDNLIDVIESLRRQLKVWIQKYRVLKSDEKLECERCLWQNNRGATVCRCCGNAQLV
Protein: Chromatin structure-remodeling complex subunit RSC9 (RSC complex subunit RSC9) (Remodel the structure of chromatin complex subunit 9) (Q03124)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit plays a role in transcriptional response to stress. It is involved in both repression and activation of mRNAs regulated by the target of rapamycin (TOR) kinases, and in the synthesis of rRNA.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858, ECO:0000269|PubMed:11931764, ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.
Interaction partners:
- Chromatin structure-remodeling complex protein RSC3
- Chromatin structure-remodeling complex subunit RSC7
- Nuclear protein STH1/NPS1
- Chromatin structure-remodeling complex protein RSC58
- Chromatin structure-remodeling complex subunit SFH1
- Actin-like protein ARP9
- Actin-related protein 7
- Chromatin structure-remodeling complex protein RSC8
- Chromatin structure-remodeling complex protein RSC6
- Chromatin structure-remodeling complex subunit RSC4
Sequence:
MNSLASNTPLNGTPVSEAPATSSEPVNMFETMVANPIKVSRLQSNGVLTGPAANTKSIHYSLANFNVFQSLPKETARGVDDLTRMEMALLSGIPEEIKWSLKKYLTYSNKAPYMISLRTLPDLLPLFKTFILPLERIVEGLNKSSICDSKAMDSLQMGLNALLILRNLAQDTDSVQILVKDREIKSFILFILKKFQCVATGDNKWQLYEGNATFFNELTHYTLDLMEAISSYIAPAMKDDHYFQTLVSILNYTKDRYMVISILRSLSRLLVRSKANEESAADNLDHKTLSLIVSFLLLECDSELIIASLDFLYQYILPGSQRITELFKSKECSLILEATLPNLLSYNIATPDYHLLQKHKIRLIKRLKPPAPKEPPNLSEDLFQQLFKLNEPLRSTAWLRCCFEPVQEAEFTQISLWRSYESKFGQPVRESGRKLLPAVEFIKNVSNAFNNAAAIVITDPVTGKKRFVIKGIQPRFKALGIADGERESQVPISALKSKFLNDSKEITPARQNSIPEVKFPQELSDVSKVACTFLCLLSNDTDDGAGSAFCQRIRPLVLHKLADIPPLTLALSEYMENTSGL
Protein: Vacuolar basic amino acid transporter 2 (P38358)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transporter required for vacuolar uptake of histidine, arginine and lysine and to a lesser extent tyrosine.
Subcellular location: Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Uncharacterized membrane protein YJL163C
- Low affinity ammonium transporter
- Vacuolar amino acid transporter 4
Sequence:
MSISNWITTAYLITSTSFQPLYGSFSDALGRRNCLFFANGAFTIGCLACGFSKNIYMLSFMRALTGIGGGGLITLSTIVNSDVIPSSKRGIFQAFQNLLLGFGAICGASFGGTIASSIGWRWCFLIQVPISVISSILMNYYVPNQKEYNRQNSSIFQNPGKILRDIDVMGSILIITGLTLQLLYLSLGCSTSKLSWTSPSVLLLLVGSVIILLLFILHERKTSARAIIPMELVNSSYSVVVLSISILVGFASYAYLFTLPLFFQIVLGDSTAKAGLRLTIPSLFTPVGSLITGFSMSKYNCLRLLLYIGISLMFLGNFLFLFIEKTSPNWLIGLFLIPANLGQGITFPTTLFTFIFMFSKSDQATATSTLYLFRSIGSVWGVAISAGVIQLSFAGLLRSNLKGLLDENKIKKLIVQLSANSSYIGSLHGEVKNTVIKSFDEATKRAHLMSTLLSSLALILCILKDNLAKPKTRR