wanglab/gogpt-training-data huggingface dataset:
Protein: Core-2/I-branching beta-1,6-N-acetylglucosaminyltransferase family protein (F21B7.14) (Glycosyltransferase) (Putative glycosylation enzyme) (Q9LR71)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MRKLYRKLVSFRDPFARVKRHVSSHSGFRAFSDRKWLFPFLASLIMSITLLILLISGQFDNFFGEEDQLPVDVVSESNDYFVESDFKQSMNSTADVNPEPPRLAYLISGTKGDSHRMMRTLQAVYHPRNQYVLHLDLEAPPRERMELAMSVKTDPTFREMENVRVMAQSNLVTYKGPTMIACTLQAVSILLRESLHWDWFLNLSASDYPLVTQDDLLYVFSNLSRNVNFIENMQLTGWKLNQRAKSIIVDPALYLSKKSDIAWTTQRRSLPNSFRLFTGSAWIMLTRSFLEYCIWGWDNFPRTILMYYTNFVSSPEGYFHTVICNSKEFINTAIGHDLHYIAWDSPPKQHPRSLSLKDFDNMVKSKAPFARKFHKNDPALDKIDKELLGRTHRFAPGGWCVGSSANGNDQCSVQGDDSVLKPGPGSERLQELVQTLSSEEFRRKQCS
Protein: 2-hydroxyisoflavanone synthase (2HI synthase) (EC 1.14.14.87) (CYP Ge-8) (Cytochrome P450 93C2) (Isoflavonoid synthase) (Q9SXS3)
Organism: Glycyrrhiza echinata (Licorice)
Function: 2-hydroxyisoflavanone synthase, which catalyzes the hydroxylation associated with 1,2-aryl migration of flavanones. Converts liquiritigenin and naringenin into highly unstable precursors of the isoflavones daidzein and genistein. Acts only on substrates with (2S)-chirality.
Subcellular location: Microsome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLVELAITLLVIALFIHLRPTLSAKSKSLRHLPNPPSPKPRLPFVGHLHLLDKPLLHYSLIDLSKRYGPLYSLYFGSMPTVVASTPELFKLFLQTHEASSFNTRFQTSAIRRLTYDNSVAMVPFGPYWKFIRKLIMNDLLNATTVNKLRPLRSQEIRKVLRVMAQSAESQVPLNVTEELLKWTNSTISRMMLGEAEEIRDIARDVLKIFGEYSLTDFIWPLKKLKVGQYEKRIDDIFNRFDPVIERVIKKRQEIRKKRKERNGEIEEGEQSVVFLDTLLDFAEDETMEIKITKEQIKGLVVDFFSAGTDSTAVATDWALSELINNPRVFQKAREEIDAVVGKDRLVDEADVQNLPYIRSIVKETFRMHPPLPVVKRKCVQECEVDGYVIPEGALILFNVWAVGRDPKYWDRPTEFRPERFLENVGEGDQAVDLRGQHFQLLPFGSGRRMCPGVNLATAGMATLLASVIQCFDLSVVGPQGKILKGNDAKVSMEERAGLTVPRAHNLICVPVARSSAVPKLFSS
Protein: SIVA1 apoptosis inducing factor (H0YJN1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLIGPDGRLIRSLGQASEADPSGVASIACSSCVRAVDGKAVCGQCERALCGQCVRTCWGCGSVACTLCGLVDCSDMYEKVLCTSCAMFET
Protein: FXYD domain-containing ion transport regulator 4 (Channel-inducing factor) (CHIF) (Q9D2W0)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q63113}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q63113}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q63113}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q63113}. Note=Detected in the basolateral membrane of collecting duct principal cells. {ECO:0000250|UniProtKB:Q63113}.
Interaction partners:
- Phospholemman
- Sodium/potassium-transporting ATPase subunit gamma
- FXYD domain-containing ion transport regulator 7
- Sodium/potassium-transporting ATPase subunit beta-3
- Sodium/potassium-transporting ATPase subunit alpha-1
- Sodium/potassium-transporting ATPase subunit alpha-4
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit alpha-3
- Phospholamban
Sequence:
MEEITCAFLLLLAGLPALEASDPVDKDSPFYYDWESLQLGGLIFGGLLCIAGIAMALSGKCKCRRTHKPSSLPGKATPLIIPGSANTC
Protein: Protein TIC 20-v, chloroplastic (Translocon at the inner envelope membrane of chloroplasts 20-V) (AtTIC20-v) (Q9FM67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in protein precursor import into chloroplasts. Not redundant with TIC20-I, TIC20-II or TIC20-IV.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:21395885}; Multi-pass membrane protein {ECO:0000269|PubMed:21395885}.
Interaction partners:
- Protein TIC 20-I, chloroplastic
- Protein TIC 20-IV, chloroplastic
- Outer envelope pore protein 24A, chloroplastic
Sequence:
MAIISQFFAPLPSLTGTLTLTGRSFLPLNLDTQFPKPRLSRDRAATLVLQSKGDDSVDASDRIISAVCYFYPFFDGIQYGKFIITQYQPFQILIQPLFPAIRAFKSFPFNGFLIFITLYFVVVRNPNFSRYVRFNTMQAIVLDVLLIFPDLLERSFNPRDGFGLDVVMSLDSTVFLFLLVSLIYGFSACLFGLTPRLPLVAEAADRQVL
Protein: Uncharacterized protein (Q57TV8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWRRTPTLASCLSAAQALVPSTWRSAPSGWFLVPQSNTTEGDELCVAKLFLFLNHAAQYMFLGKVMALAEEIQCVPRLEWFYAELYFTLPPTPAAERLACYMNDQERLRCGLRNQSRGTSASGLLWSKELNKRVEERATEDFCWLLTDDQRKTEKFLQETYIQWHHRADYLVTRKSREKREFRQDLTLHQVIQEGQERKRRMQRRRSRDESREVNIAAGKESEWDNFTHDVLPRDLREALDRESDGMEDVRISRAGTATGGWNRGYRTHPNFR
Protein: DDHD domain containing 2 (H0YF17)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XEIFFAFGSPIGMFLTVRGLKRIDPNYRFPTCKGFFNIYHPFDPVAYRIEPMVVPGVEFEPMLIPHHKGRKRMHLELREGLTRMSMDLKNNLLGSLRMAWKSFTRAPYPALQASETPEETEAEPESTSEKPSDVNTEETSVAVKEEVLPINVGMLNGGQRIDYVLQEKPIESFNEYLFALQSHLCYWESEDTVLLVLKEIYQTQGIFLDQPLQ
Protein: Rifin (Q9NFA9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHCINILLFALPLNILVNTHKKTSITPLHTPKRPTTRLLCECELYSPANYDNDPQMKEVMENFIKQTQERFYEYDERMKTTRQKCKEQCEKDIQKIILKDKLEKELMDKFATLHTDIQSDAIPTCVCEKSIADKMEKGCLRCAGVLGGGVMPGMGLIDGSLLGAISVLQPLEIAAAKDAAIAKATDAAIEAGINTVVSKIKGLLASFTEKEVLVDLTKIVTPSTYNNGAILHKSAMALANKSCDFEGRGINSSFCNTLYNGEKTTFEPFAKAGIAEYNATYTLQKEALETANVDMVKATYASYQTAIIASIVAIVVIVLIMVIIYKILRYRRKKKMKKKLQYIKLLKE
Protein: Uncharacterized protein (Q381V3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAALRSVRSKQQVNKFCSVGSALLGDAVCFSIKEWDNTLRTLEAARCDPLLLPPLASLPTSAVCEAVRHYHNVYMKASQLIVLRPLHWRKWQEGLCEFMDHTNNNGTDGGNSSNGSSTTLHTGCCELEVLCGAFLSQQREQFVVAFWGTVDSCSLRLKLLVSRFPHEDEIISVSPVAGDGMDGNGADLEEVRIAAEESADDMGEGAILLRKRYFRELYSFQRLACESAHLFGFYASVGKAERLWLTDTLLLERHEEAAEVLIRRSFKRDFDVPSLELVSGELLEDYKSFEVNESKQRVLLKRAGDTLKGLWCILAHDKFVKHQSQSKLQQKGVEEEYECGVEEEERSCGTDATALKFPEELVRCISCKAVRSVTAFATAVQSIVECNPSSPPSANLERLEFLLSLLLRWFEAYTGERHRGDIPLFLDTDLWEFLLQRHTELLKWVMSAYCSGETDVDYNSAVEAVQFVCLSVLRCLDVYKAAVVSKRCEESVKDKLKCVAGNTVAEWLKHTAIGAFLRGIRRACSDLCASGTRFCLSIPLMLIVVRSSVVESRLLLLCHGISCAVDVRQLLLPMVDLGFKEMSQLDKNADGTLLTSWVGSMTSVLNSLRRTLRVHGAEHAPADDFVCELHRHYLSLQRLSPAAVSDIVTDAWTDFLSSGFVVEGGLRGSRRVSLFSVSSERRSALHGAQQMVNGTHVDVGHEERDYKRLRKE
Protein: Hexose transporter HXT9 (P40885)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable glucose transporter.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Carbon catabolite-derepressing protein kinase
- ATP-dependent permease PDR15
- Protein SNQ2
- ATP-dependent permease PDR10
- Pleiotropic ABC efflux transporter of multiple drugs
- Transcription factor PDR3
- Transcription factor PDR1
- Oligomycin resistance ATP-dependent permease YOR1
- Oligo-1,6-glucosidase IMA3
- DNA damage-inducible protein 1
Sequence:
MSGVNNTSANDLSTTESNSNSVANAPSVKTEHNDSKNSLNLDATEPPIDLPQKPLSAYTTVAILCLMIAFGGFIFGWDTGTISGFVNLSDFIRRFGQKNDKGTYYLSKVRMGLIVSIFNIGCAIGGIVLSKVGDIYGRRIGLITVTAIYVVGILIQITSINKWYQYFIGRIISGLGVGGIAVLSPMLISEVAPKQIRGTLVQLYQLMCTMGIFLGYCTNYGTKNYHNATQWRVGLGLCFAWTTFMVSGMMFVPESPRYLIEVGKDEEAKRSLSKSNKVSVDDPALLAEYDTIKAGIELEKLAGNASWSELLSTKTKVFQRVLMGVMIQSLQQLTGDNYFFYYGTTIFKSVGLKDSFQTSIIIGVVNFFSSFIAVYTIERFGRRTCLLWGAASMLCCFAVFASVGVTKLWPQGSSHQDITSQGAGNCMIVFTMFFIFSFATTWAGGCYVIVSETFPLRVKSRGMAIATAANWMWGFLISFFTPFITGAINFYYGYVFLGCLVFAYFYVFFFVPETKGLTLEEVNTMWLEGVPAWKSASWVPPERRTADYDADAIDHDDRPIYKRFFSS
Protein: Ras-related protein Rab-31 (EC 3.6.5.2) (GTP-binding protein Rab0) (Q6GQP4)
Organism: Rattus norvegicus (Rat)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Required for the integrity and for normal function of the Golgi apparatus and the trans-Golgi network. Plays a role in insulin-stimulated translocation of GLUT4 to the cell membrane. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium (By similarity). Plays a role in M6PR transport from the trans-Golgi network to endosomes. Plays a role in the internalization of EGFR from the cell membrane into endosomes.
Subcellular location: Early endosome {ECO:0000250|UniProtKB:Q13636}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q13636}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q13636}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Rapidly recruited to phagosomes containing S.aureus or M.tuberculosis. {ECO:0000250|UniProtKB:Q13636}.
Interaction partners:
- DCC-interacting protein 13-alpha
- Rab5 GDP/GTP exchange factor
- Geranylgeranyl transferase type-2 subunit alpha
- DCC-interacting protein 13-beta
- GTPase-activating protein and VPS9 domain-containing protein 1
- Ras and Rab interactor 3
- Rab GDP dissociation inhibitor alpha
- Rab GDP dissociation inhibitor beta
Sequence:
MMAIRELKVCLLGDTGVGKSSIVCRFVQDHFDHNISPTIGASFMTKTVPCGNELHKFLIWDTAGQERFHSLAPMYYRGSAAAVIVYDITKQDSFHTLKKWVKELKEHGPENIVMAIAGNKCDLSDIREVPLKDAKEYAESIGALVVETSAKNAINIEELFQGISRQIPPLDPHENGNSGGIKLGNQSLQAGRRCC
Protein: Cytochrome P450 11B1, mitochondrial (CYPXIB1) (Cytochrome P450(11 beta)-DS) (Cytochrome P450C11) (Steroid 11-beta-hydroxylase, CYP11B1) (EC 1.14.15.4) (P15393)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase involved in the biosynthesis of adrenal corticoids. Catalyzes the hydroxylation of carbon hydrogen bond at 11-beta position of 11-deoxycortisol and 11-deoxycorticosterone/21-hydroxyprogesterone yielding cortisol or corticosterone, respectively. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14137}.
Interaction partners:
Sequence:
MALRVTADVWLARPWQCLHRTRALGTTAKVAPKTLKPFEAIPQYSRNKWLKMIQILREQGQENLHLEMHQAFQELGPIFRHSAGGAQIVSVMLPEDAEKLHQVESILPHRMPLEPWVAHRELRGLRRGVFLLNGADWRFNRLQLNPNMLSPKAIQSFVPFVDVVARDFVENLKKRMLENVHGSMSINIQSNMFNYTMEASHFVISGERLGLTGHDLKPESVTFTHALHSMFKSTTQLMFLPKSLTRWTSTRVWKEHFDSWDIISEYVTKCIKNVYRELAEGRQQSWSVISEMVAQSTLSMDAIHANSMELIAGSVDTTAISLVMTLFELARNPDVQQALRQESLAAEASIVANPQKAMSDLPLLRAALKETLRLYPVGSFVERIVHSDLVLQNYHVPAGTFVIIYLYSMGRNPAVFPRPERYMPQRWLERKRSFQHLAFGFGVRQCLGRRLAEVEMLLLLHHMLKTFQVETLRQEDMQMVFRFLLMPSSSPFLTFRPVS
Protein: Acyl-CoA-binding domain-containing protein 7 (Q8N6N7)
Organism: Homo sapiens (Human)
Function: Binds medium- and long-chain acyl-CoA esters.
Interaction partners:
Sequence:
MALQADFDRAAEDVRKLKARPDDGELKELYGLYKQAIVGDINIACPGMLDLKGKAKWEAWNLKKGLSTEDATSAYISKAKELIEKYGI
Protein: Keratin-associated protein 19-7 (Q3SYF9)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
Sequence:
MSYSGSYYGGLGYGCGGFGGLGYGYSCGCGSFRRLGYGCGYGGYRYSCCHPSCYGGYWSSGFY
Protein: Protein FAM13C (Q8NE31)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFSCFCFSLQDNSFSSTTVTECDEDPVSLHEDQTDCSSLRDENNKENYPDAGALVEEHAPPSWEPQQQNVEATVLVDSVLRPSMGNFKSRKPKSIFKAESGRSHGESQETEHVVSSQSECQVRAGTPAHESPQNNAFKCQETVRLQPRIDQRTAISPKDAFETRQDLNEEEAAQVHGVKDPAPASTQSVLADGTDSADPSPVHKDGQNEADSAPEDLHSVGTSRLLYHITDGDNPLLSPRCSIFSQSQRFNLDPESAPSPPSTQQFMMPRSSSRCSCGDGKEPQTITQLTKHIQSLKRKIRKFEEKFEQEKKYRPSHGDKTSNPEVLKWMNDLAKGRKQLKELKLKLSEEQGSAPKGPPRNLLCEQPTVPRENGKPEAAGPEPSSSGEETPDAALTCLKERREQLPPQEDSKVTKQDKNLIKPLYDRYRIIKQILSTPSLIPTIQEEEDSDEDRPQGSQQPSLADPASHLPVGDHLTYSNETEPVRALLPDEKKEVKPPALSMSNLHEATMPVLLDHLRETRADKKRLRKALREFEEQFFKQTGRSPQKEDRIPMADEYYEYKHIKAKLRLLEVLISKQDVAKTI
Protein: MKIAA0846 protein (Q69ZX7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
RTMGSNGLGKAATLDELLSTCIEMFDDNGDLNDSYLPRIVLLMHRWYLSSTELAGKLLCMYRNASGESCDEFRLKICYFMRYWILKFPAEFNLDLGLIRMTEEFREVASQLGHEKHISLMDISSVPSYDWMRRVTQRKKVSKRGKACLLFDHLEPIELAEHLTFLEHKSFRRISFTDYQSYVIHGCLENNPTLERSIALFNGISKWVQLMVLSKPSAQQRAEVITKFINVAQKLLQLKNFNTLMAVVGGLSHSSISRLKDTHSHLSSEVTKNWNEMTELVSSNGNYCNYRKAFADCDGFKIPILGVHLKDLIAVHVIFPDWMEENKVNVVKMHQLSVTLSELVSLQNASHHLEPNMDLINLLTLSLDLYHTEDDIYKLSLVLEPRNSKSQPTSPTTPNKPVVPLEWASEVVPKPDPTIINKHIRKLVESVFRNYDHDHDGYISQEDFESIAANFPFLDSFCVLDKDQDGLISKDEMMAYFLRAKSQLHCKMGPGFIHNFQEMNYLKPTFCEHCAGFLWGIIKQGYKCKDCGANCHKQCKDLLVLACRRLARAPSLSSNPGSLPGSPALPPVQDEVFEFPGVTAGHRDLDSRAITLVTGSSRKISVRLQRATTSQATQTEPVWSEAVWGDSGSHTFPKMKSKFHDKAAKDKGFAKWENEKPTVQAGVDVVDRGTAFEPDQDDGQDEAKQGGEDG
Protein: Phosphate import ATP-binding protein PstB 2 (EC 7.3.2.1) (ABC phosphate transporter 2) (Phosphate-transporting ATPase 2) (P9WQK9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ABC transporter complex PstSACB involved in phosphate import (Probable). Responsible for energy coupling to the transport system.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01702}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01702}.
Interaction partners:
- Phosphate transport system permease protein PstC 1
- Phosphate-binding protein PstS 1
- Phosphate transport system permease protein PstA 2
- Phosphate transport system permease protein PstA 1
- Phosphate transport system permease protein PstC 2
- Phosphate-binding protein PstS 2
- Phosphate-specific transport system accessory protein PhoU homolog 1
- Phosphate-binding protein PstS 3
- Phosphate-specific transport system accessory protein PhoU homolog 2
- Phosphate import ATP-binding protein PstB 1
Sequence:
MACERLGGQSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGDVKDAKRGN
Protein: Primase C-terminal 2 domain-containing protein (Q57XD4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRITLPSQQVSKRLVAKLASMSGVKGATATNAKGNDAASQAMEAPAVVPPSRETPKSTLPRVGARAAVPVGGAGVHSDALRQGTLRAATPIKPSVAAAAASVYETRINAPAPNIRNGEADGQQLPQKKTLRRRKRLIRVSTRRRVRQNTAKVPEDMEEEPIVEDVEDPFVDQEEHEEEPVAAAPREKRQQPRPERVKGRPEAKTVDRQPEIKKTEPSPAASYAAYEHDRISGTSLHGKTPMIKAFRIEDVLAACTPSDGVFARRLPQGGCQFFAWPGTPLAVASSAVANMPETIRTVHAIFGREKTPMDLVLDIDCPVPQEHWSMSKVRPFQKKVLDDVMNVIVEEIEAIGEEIESQVVLQSPNLKKVSFHVHTKLKDAAFEDYNSLHGFLHQFHKRIPAVDLQIYRSNGMLRMHRCMKENHTSAIVVFEDKDWNIGFPDGIVPDAKAALHSACIREEGTYSRLLHFDPPRNFPTAFENSGANGSGAAEDKKIKVLLPRTEREAVENASRWLREGTREADVDEWRSWIRLGINAYRVAYHFRDAMTLQRPALEELLDAWVEASKKCPAKFKPGVCEARWATFDINRLSKFDDNEWWPSYQRIGRTAMLNEAADAANRGGANGIPPQGA
Protein: Holocytochrome-c1 synthase (EC 4.4.1.17) (Cytochrome c1 heme lyase) (CC1HL) (Q00873)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C1 apoprotein to produce the mature functional cytochrome.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:1499554}. Note=Partially exposed to the intermembrane space. {ECO:0000305|PubMed:1499554}.
Interaction partners:
- Protoheme IX farnesyltransferase, mitochondrial
- Holocytochrome-c synthase
- Cytochrome c1, heme protein, mitochondrial
- Heme A synthase COX15
- Ferrochelatase, mitochondrial
- Cytochrome c isoform 2
- Cytochrome c isoform 1
- Mitochondrial chaperone BCS1
Sequence:
MMSSDQQGKCPVDEETKKLWLREHGNEAHPGATAPGNQLECSANPQDNDKTPEYHTTVDLSQSREVSTIPRTNSDRNWIYPSEKQFYEAMMKKNWDPNSDDMKVVVPLHNSINERVWNYIKSWEDKQGGEACGGIKLTNFKGDSKKLTPRAWFRSRILHLAKPFDRHDWQIDRCGKTVDYVIDFYSTDLNDANSQQQPLIYLDVRPKLNSFEGFRLRFWKSLGF
Protein: GH12756p (Zinc-finger protein at 72D, isoform A) (Q9VUY6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MANNNYAGFNYGGTQYNTGQVSYPAVTNATYANAAAYQNAAVAAGQGGYGGAAGAGAGATSGPGAGGYGGYGDYRSAMQYDATKTFYQQSPASYNASGSTASVSKTHYSAPPVKNQVKGKMDKSNGGPKPPSSAPPAGNNYSGYDTALYNAASMYVAQQHQGNPNQKPNGGANNWYQRKMGATIPGATAIRGMRPKAPPRPQQLHYCEVCKISCAGPQTYREHLEGQKHKKREASLKMSASANSATQNRGNNYHCELCDVTCTGTDAYAAHVRGAKHQKVVKLHQKLGKPIPSEEPKKMGKINFVPAAAGGAGVAKTEGGANESDAAGDLDDNLDDSLGENTDNIKPVGGEYIEEVKDEEGKILSFNCKLCDCKFNDPNAKEMHMKGRRHRLQYKRKVQPDLVVDFKPTPRQRRLAEARANRAMMSSHRGGDDHDGGYWEEQRNRQYNEEYDYNNWMSRSFGGAQRFGRMGNGPPPHFGMMPGGNVRRPESTDDRHAIARHAEIYPKEEELQTIQRIVSHTERALKLVSDALAEQPSDAGAANKKDKAEKPSEKDGRDNQIFSFQKDADNGGNVVRILKGVMRVGYLAKGLLLHGDNAVELVVLCAEKPTSGLLQRVANVLPDKLKEVAASLSAG
Protein: Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 2) (Cell division protein kinase 1) (Never in mitosis protein X) (Q00646)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles.
Interaction partners:
- G2/mitotic-specific cyclin-B
- Cyclin dependent kinase inhibitor Pho81, putative
- M-phase inducer phosphatase
- Protein kinase domain-containing protein
- Cyclin-dependent kinases regulatory subunit
- Cell division control protein
- Nucleoporin NSP1
- C2H2 transcription factor
- Histone H1
- G2/mitotic-specific cyclin
Sequence:
MENYQKIEKIGEGTYGVVYKARELTHPNRIVALKKIRLEAEDEGVPSTAIREISLLKEMNDPNIVRLLNIVHADGHKLYLVFEFLDLDLKKYMEALPVSEGGRGRALPDGSTLSRNLGLGDAMVKKFMAQLIEGIRFCHSHRVLHRDLKPQNLLIDRDGNLKLADFGLARAFGVPLRTYTHEVVTLWYRSPEILLGGRQYSTGVDMWSCGAIFAEMCTRKPLFPGDSEIDEIFKIFRILGTPDETIWPGVTSFPDFKPTFPKWKREDIQNVVPGLEEDGLDLLEALLEYDPARRISAKQACMHPYFQHGSSYYSGRARRNGFH
Protein: Similarity to unknown protein (Q9FGY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT3g07470/F21O3_18
Sequence:
MVTEAMKAKAEVYHGDKTCREKFGSLLSEIGLPNRLLSNKEIKECGYVKDTGFVWLKHKEKKKEDQKRRYQDLLRFDNVVVCFEDEVTAYFEPNRIKKLTGVKAKEFMVWISLGEIQVNRSSGLITFKTEVGLLSKSLPLSVFEDVHGDDHDLKEKPKKELKLNKTKIYLY
Protein: Processive diacylglycerol beta-glycosyltransferase (EC 2.4.1.-) (Beta-monoglycosyldiacylglycerol synthase) (Beta-MGS) (MGlyDAG synthase) (Diglycosyldiacylglycerol synthase) (Beta-DGS) (DGlyDAG synthase) (Glycosyl-beta-1,6-galactosyldiacylglycerol synthase) (UDP-galactose:1,2-diacylglycerol 3-beta-D-galactosyltransferase) (UDP-glucose:1,2-diacylglycerol 3-beta-D-glucosyltransferase) (P75302)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Processive glycosyltransferase involved in the biosynthesis of both the non-bilayer-prone beta-monoglycosyldiacylglycerol and the bilayer-forming membrane lipid glucosyl-galactosyldiacylglycerol and digalactosyl-diacylglycerol. These components contribute to regulate the properties and stability of the membrane. Catalyzes sequentially the transfers of glucosyl or galactosyl residues from UDP-Glc or UDP-Gal to diacylglycerol (DAG) acceptor to form the corresponding beta-glycosyl-DAG (3-O-(beta-D-glycopyranosyl)-1,2-diacyl-sn-glycerol). Then, only beta-galactosyl-DAG (3-O-(beta-D-galactopyranosyl)-1,2-diacyl-sn-glycerol) can act as acceptor to give the beta-glycosyl-beta-galactosyl-DAG product (3-O-(beta-D-glycopyranosyl-(1->6)-D-galactopyranosyl)-1,2-diacyl-sn-glycerol). It can also use alpha-Gal-beta-Gal-DAG, ceramide (Cer) and beta-Gal-Cer as sugar acceptors. The enzyme is supposed to be mainly a galactosyltransferase, with higher glycosyltransferase activity for the addition of the second glycosyl on beta-Gal-DAG as acceptor. The main glycolipid produced in vivo is beta-Glc-beta-Gal-DAG with a beta-1,6 linkage.
Subcellular location: Cell membrane {ECO:0000250}.
Interaction partners:
- Uncharacterized glycosyltransferase MG060 homolog
- Uncharacterized glycosyltransferase MG025 homolog
Sequence:
MNKLISILVPCYQSQPFLDRFFKSLLKQDWNGVKVIFFNDNKPDPTYEILKQFQQAHPQLAIEVHCGEKNVGVGGSRDQLINYVDTPYFYFVDPDDEFSDPNCFKAIVETIQGENFDIAVLNSIVYLQMLKNDFLIKHIPLKNIFQGKVKLNPDNTVNHLHYIQNNDQYIWNIVINTAFFKALDLQFVNRFIEDIAVWFPIMFKAQKVLWIDVNGVNYYLRPNSASTQKNSIKLLSFIEAYERLYFHLKKVGKLADFIDPNNKIESRFWRRQAFIWFSFINVSWMKAEFEQTKSVLQKLFDFMEANGIYDRVFTNKHHGIYLLWVNRLKHFKKLVQAQPHL
Protein: mRNA export factor ICP27 homolog (H2A0V8)
Organism: Murid herpesvirus 1 (MuHV-1) (Mouse cytomegalovirus)
Subcellular location: Virion tegument {ECO:0000256|ARBA:ARBA00004535}.
Interaction partners:
Sequence:
MLRTGVKRRLGPFAGYDEDDAATGGVSRRSKYSQQQSQHYYYGHNQSSYRDSGASHPNWKRNAHLMPPPLSSPSSPPPQYDKNIAALTHLNKKLDCLGPDDLECLKAMIRIREARAQGRRPEPSSAPSILESSLVSSNNSNNNTTLSLGGGGGGDYHRQTSPDIRDYTTGSLGLCMFPMDLPDPIKLLENRYTDNDRHAPAVVTHDELINTNYLLLFRKHFDALPPEELRVLVQDRTFAINNAPSLDVVAAMADENLTYVKFHRVHNLPVNPKDLYMSTLGLIKYATFNKLNLGELSCLLDSPGGGGSDREYHILRQIANKPASPCRKGGSSAAAAAASFDVLRRPPLSFKHPLQQALALIASFARIVGVIRRRSLRHSGPFFIRDFDDTGATDSYRCGMISELIFDYLRGHRCQNEVCRVKLKKLLQPYTSTLFFCAYNNTRKHPNGTYRREGRQKRRAPDATPNIPRLAYRRSTTTSPEVEPAPPSRMTSSNSPRVDSRGGDRRGDSSSTSNNHHRHHTRRARTRSTHDSSSSGSRRRSSATDGRRSRRGSRRGEAQRESNGHHSSKSPSTVSSTTVHGQNGARGDSAPSRKSQQSQQQPETTSKESSKTAAMPPPPSPCSPSPASRERRTSKSPSSSPRPHDPPPDEPADAEKELATAGDEDEGVRSPGECSVATRRGSSADESSDSSSSSSDSSSSSDEEESDVEDCRELDLQSKRLEEALEERCERDFEADDEEFAEPIEEDDLHCSLDMEEDIEDEPLDPETESVWTASVTPLAAPPSIRILDHEPGDAEEEEESDTDFYDETDQPLNKRIHLRSATPTDDVIMECDLSYSEMDSD
Protein: Endophilin-A3 (EEN-B2) (Endophilin-3) (SH3 domain protein 2C) (SH3 domain-containing GRB2-like protein 3) (Q99963)
Organism: Homo sapiens (Human)
Function: Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O35180}. Early endosome membrane {ECO:0000250|UniProtKB:O35180}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35180}. Note=Associated with postsynaptic endosomes in hippocampal neurons. Associated with presynaptic endosomes in olfactory neurons. {ECO:0000250|UniProtKB:O35180}.
Interaction partners:
- Huntingtin
- Activity-regulated cytoskeleton-associated protein
- Dynamin-2
- Synaptojanin-1
- Endophilin-A2
- Endophilin-A1
- E3 ubiquitin-protein ligase CBL
- Ataxin-2
- Epidermal growth factor receptor
- Synaptojanin-2
Sequence:
MSVAGLKKQFHKASQLFSEKISGAEGTKLDDEFLDMERKIDVTNKVVAEILSKTTEYLQPNPAYRAKLGMLNTVSKIRGQVKTTGYPQTEGLLGDCMLKYGKELGEDSTFGNALIEVGESMKLMAEVKDSLDINVKQTFIDPLQLLQDKDLKEIGHHLKKLEGRRLDYDYKKKRVGKIPDEEVRQAVEKFEESKELAERSMFNFLENDVEQVSQLAVFIEAALDYHRQSTEILQELQSKLQMRISAASSVPRREYKPRPVKRSSSELNGVSTTSVVKTTGSNIPMDQPCCRGLYDFEPENQGELGFKEGDIITLTNQIDENWYEGMIHGESGFFPINYVEVIVPLPQ
Protein: Origin recognition complex subunit 4 (F1QRE0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR007858}.
Interaction partners:
- Origin recognition complex subunit 1
- Origin recognition complex, subunit 2.
- Cell division control protein
- Origin recognition complex subunit 6
- Origin recognition complex subunit 5
- Origin recognition complex subunit 3
- Chromatin licensing and DNA replication factor 1
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM4
- DNA helicase
Sequence:
MSKRRPAALSDVQCVSLVQELLRERLCHQKLPDQPIGLDSQYKHLLELLRRTAVHGESNSVLIVGPRGSGKTMLLGCVLRELMSLKEVQKNVLLVELNGLLQTDDKIALKEITRQLHLENVVGDKVFGSFAENLAFLLEALKKGDKSSSRPVLFLLDEFDLFAHHKNQTLLYNLLDVSQSAQTPVAVVGLTCRLDVLELLEKRVKSRFSHRQIHLFSSLSFSQYVDVVRLQLSLPQDFPDHRFSSQWNQSVTKLCEDKSVLEVLKRSFNSSKDFRSLYSLLFMAVSRVSVSHSTLCEADFLESGRLISADSKANVLHGLSILELCLIIAMKHLNDTYDGEPFNFQMVHNEFKKFIQRKSHSIHKFEKPVVMKAFEHLLQLELVRPVDSGVCKVQREYQLMRLMLEHGQVMEALQRYPQCPTDVKQWALSAFA