wanglab/gogpt-training-data huggingface dataset:
Protein: Homeobox protein SIX6a (SIX homeobox 6a) (Sine oculis-related homeobox 6a) (Q7T3G8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MFQLPILNFSPQQVAGVCETLEESGDVERLGRFLWSLPVAPSACDVLGKNESVLRARAVVAFHAGNFRELYHILENHKFTKDSHAKLQALWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRHLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQQQVLSGGSVRSLGDDDTTVDRLGPASSPEVSLSSKAATSAISITSSDSECDI
Protein: AP-2 complex subunit mu (Adaptin medium chain APM4) (Clathrin assembly protein complex 2 mu medium chain) (Clathrin coat assembly protein AP50) (Clathrin coat-associated protein AP50) (Mu2-adaptin) (Plasma membrane adaptor AP-2 50 kDa protein) (Q99186)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.
Subcellular location: Membrane, clathrin-coated pit. Cytoplasmic vesicle, clathrin-coated vesicle membrane.
Interaction partners:
- AP-2 complex subunit beta
- AP-2 complex subunit sigma
- AP-2 complex subunit alpha
- AP-1 complex subunit beta-1
- Putative ATP-dependent RNA helicase YLR419W
- AP-3 complex subunit delta
- Clathrin heavy chain
- AP-1 complex subunit gamma-1
- Transcription activator MSS11
- Factor-induced gene 2 protein
Sequence:
MISGVLVYSSRGELVLNKFFKNSLKRSISDIFRVQVINNLDVRSPVLTLGSTTFHHIRSRHGDNLWLVTITRSNANSAAIWEFLYKLDAVMNAYRLDREEALKEEFMIVHEMLDIMLGGNGIPIDTELNSVIAQMSVKPVRNMGGLLDSPDGNDVLSSSSSPTSSAGELHFPKFLTKRSSSFLGQGDSTSDFYDNNKITWRPKGIIHKKDEVFLYVNERINILVSRDGSILKSYVDGTIDITTHLSGTPICRFGLNDSLGMQSEDEKKWLAQQQRHSGSDFGNKNFIPKAAAGSVLLEDCKFHECVSLDKFNRNHIIEFVPPDGSMELMKYHVRDNINLPFKVTPIVTHSTRDNEIDYRITLKSLFPGKLSAKDVVLHIPVPPSTVDCKISVSNGHCKFVPEENAMIWRFNKYNGLTENTLSAVTVSTSDTTQLNLQQWTRPPISLEFEVMMFSNSGLVVRYFTISGKDSKHRAVKWIKYISKAGSYEVRY
Protein: Protein ABIL3 (Abl interactor-like protein 3) (AtABIL3) (Q6NMC6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 5B
- Filament-like plant protein 4
- Actin-related protein 2/3 complex subunit 5A
- Putative calcium-transporting ATPase 7, plasma membrane-type
- Protein SCAR2
- Protein PIR
- Cyclin-T1-4
- MYB-like transcription factor TCL2
- Protein BRANCHLESS TRICHOME
- Actin-related protein 3
Sequence:
MSAAATMPMPREASNYDEISMQQSMLFSDSLKDLKNLRTQLYSAAEYFELSYTNDEQKQIVVETLKDYAIKALVNTVDHLGSVTYKVNDFVDEKVDEVAGTELRVSCIEQRLRMCQEYMDHEGRSQQSLVIDTPKFHKRYFLPSGEIKRGGNLAKLKNVEGSFDGEDDWNQFRNAVRATIRETPPPPVRKPILQSPSQRKPQRSATFSFSSIATAPKKEQDKRAVSPHRFPLLRSGSVAIRPSSISRPTTPSKSRAVTPTPKRYPSEPRRSASVRVAFEKEAQKEPEHQQQPSKSKRLLKALLSRRKTKKDDTLYTYLDEY
Protein: Tetratricopeptide repeat (TPR)-like superfamily protein (Q8VZ31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 26S proteasome regulatory subunit S10B homolog B
- T-complex protein 1 subunit zeta 1
- 26S proteasome regulatory particle chain RPT6-like protein
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit theta
Sequence:
MLKSEASLSIYCDSGDGFKSEDPVTGIEENLERTVTIGDAIDGGEFSFAKHKEEDSGEGERGVFEEVIKKLGIGVRDELGFEIERPPSPPMHLAAGLGIDKFDLYGSEIKFDLPGYDDKNCGDYYKGMLEEYPLHPLLLKNYAKFLEYKGDLSGAEEYYHKCTVVEPSDGVALANYGRLVMKLHQDEAKAMSYFERAVQASPDDSIVLAAYASFLWEINADDDDEDDDEDDDESSGQGKDEFEADAAGKGKSSLSKTEDGETLCRYAKAFWSINNDHEKALFYFEKAVEASPNDSIILGEYARFLWEIDE
Protein: Transposon Ty1-ML1 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q04711)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSNYPNISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENLHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: NAD-dependent methanol dehydrogenase (MDH) (MEDH) (EC 1.1.1.244) (Type 3 alcohol dehydrogenase) (P31005)
Organism: Bacillus methanolicus
Function: Catalyzes the oxidation of methanol to yield formaldehyde. It possesses a NADH-dependent formaldehyde reductase activity and cannot use NADP.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:2673121}.
Interaction partners:
Sequence:
MTNFFIPPASVIGRGAVKEVGTRLKQIGAKKALIVTDAFLHSTGLSEEVAKNIREAGLDVAIFPKAQPDPADTQVHEGVDVFKQENCDALVSIGGGSSHDTAKAIGLVAANGGRINDYQGVNSVEKPVVPVVAITTTAGTGSETTSLAVITDSARKVKMPVIDEKITPTVAIVDPELMVKKPAGLTIATGMDALSHAIEAYVAKGATPVTDAFAIQAMKLINEYLPKAVANGEDIEAREAMAYAQYMAGVAFNNGGLGLVHSISHQVGGVYKLQHGICNSVNMPHVCAFNLIAKTERFAHIAELLGENVSGLSTAAAAERAIVALERYNKNFGIPSGYAEMGVKEEDIELLAKNAFEDVCTQSNPRVATVQDIAQIIKNAL
Protein: Probable glutathione-independent glyoxalase SNO4 (EC 4.2.1.130) (Glyoxalase 3 homolog 4) (Heat shock protein 34) (SNZ proximal open reading frame 4) (Q04902)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS) (By similarity). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation.
Subcellular location: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q04432}. Note=Present in processing bodies (P-bodies) and stress granule (SG) foci upon glucose starvation and heat shock. {ECO:0000250|UniProtKB:Q04432}.
Interaction partners:
- NADPH-dependent methylglyoxal reductase GRE2
- D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3
- Hydroxyacylglutathione hydrolase, mitochondrial
- D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2
- Glyoxalase I
- D-lactate dehydrogenase [cytochrome] 1, mitochondrial
- Hydroxyacylglutathione hydrolase, cytoplasmic isozyme
- Catabolic L-serine/threonine dehydratase
- Threonine dehydratase, mitochondrial
- D-serine dehydratase
Sequence:
MTPKRALISLTSYHGPFYKDGAKTGVFVVEILRSFDTFEKHGFEVDFVSETGGFGWDEHYLPKSFIGGEDKMNFETKNSAFNKALARIKTANEVNASDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLFDGLIDIKTTRPLIEGKAITGFPLEGEIALGVDDILRSRKLTTVERVANKNRAKYLAPIHPWDDYSITDGKLVTGVNANSSYSTTIRAINALYS
Protein: Protein mago nashi homolog (P61326)
Organism: Homo sapiens (Human)
Function: Required for pre-mRNA splicing as component of the spliceosome. Plays a redundant role with MAGOHB as core component of the exon junction complex (EJC) and in the nonsense-mediated decay (NMD) pathway. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:19324961}. Nucleus speckle {ECO:0000269|PubMed:19324961}. Cytoplasm {ECO:0000269|PubMed:19324961}. Note=Detected in granule-like structures in the dendroplasm (By similarity). Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (PubMed:19324961). {ECO:0000250, ECO:0000250|UniProtKB:Q27W02, ECO:0000269|PubMed:19324961}.
Interaction partners:
- RNA-binding protein 8A
- Eukaryotic initiation factor 4A-III
- Regulator of nonsense transcripts 3A
- Protein CASC3
- Regulator of nonsense transcripts 3B
- Partner of Y14 and mago
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 3
- Protein mago nashi homolog 2
- Regulator of nonsense transcripts 1
Sequence:
MESDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI
Protein: V-set and immunoglobulin domain-containing protein 1 (Cell surface A33 antigen) (Glycoprotein A34) (Q9D2J4)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MMVFAFWKVFLILNCLAGQVSMVQVTIPDTFVNVTVGSNVTLLCLYTTTEKSLEKLSIQWSFFHNKEMEEPISIYYSEGGQASAIGQFKDRIIGATNPGNASITILHMQPADSGIYICDVNNPPHFVGKNQGLLDVTVLVKPSKPFCTIQGRPEAGHPISLSCLSAFGTPSPLYYWYNIEGNTIVPVKESFNTATGVLVIGNLTNFEQGYYQCTAINSLGNSSCEIDLTSSHPEVGIIIGALVGALIGAAVIICVVYFARNKVKSKQQKNLNSSTELEPMTKVHHPQQSEAISADGVQLEGTLPSSIHAGHNTEPTTTAVLEPEYEPNPPLETTTQPDPEPEGSVPVLAPEAEIQPHPELDPETETEPEPEPEPKPEPEPEPELEPDPQSGVIIEPLSKAGEDTVKA
Protein: SMARCA1 protein (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1) (B7ZLQ5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEQDTAAVAATVAAADATATIVVIEDEQPGPSTSQEEGAAAAATEATAATEKGEKKKEKNVSSFQLKLAAKAPKSEKEMDPEYEEKMKADRAKRFEFLLKQTELFAHFIQPSAQKSPTSPLNMKLGRPRIKKDEKQSLISAGDYRHRRTEQEEDEELLSESRKTSNVCIRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGKMDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHIVSNSGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREDKFLEVEFLGQREAIEAFNAPNSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQQSNKLAKEEMLQMIRHGATHVFASKESELTDEDITTILERGEKKTAEMNERLQKMGESSLRNFRMDIEQSLYKFEGEDYREKQKLGMVEWIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFFPPRLFELLEKEILYYRKTIGYKVPRNPDIPNPALAQREEQKKIDGAEPLTPEETEEKEKLLTQGFTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKGKNYTEEEDRFLICMLHKMGFDRENVYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERERAEKKKRATKTPMSQKRKAESATESSGKKDVKKVKS
Protein: Hemojuvelin (Hemochromatosis type 2 protein) (Hemojuvelin BMP coreceptor) (RGM domain family member C) (Q6ZVN8)
Organism: Homo sapiens (Human)
Function: Acts as a bone morphogenetic protein (BMP) coreceptor. Through enhancement of BMP signaling regulates hepcidin (HAMP) expression and regulates iron homeostasis.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Also released in the extracellular space. {ECO:0000269|PubMed:25156943}.
Interaction partners:
- Transferrin receptor protein 2
- Neogenin
- Bone morphogenetic protein 6
- Hereditary hemochromatosis protein
- Transmembrane protease serine 6
- Bone morphogenetic protein 2
- Transferrin receptor protein 1
- Hepcidin
- Bone morphogenetic protein receptor type-1A
- Activin receptor type-1
Sequence:
MGEPGQSPSPRSSHGSPPTLSTLTLLLLLCGHAHSQCKILRCNAEYVSSTLSLRGGGSSGALRGGGGGGRGGGVGSGGLCRALRSYALCTRRTARTCRGDLAFHSAVHGIEDLMIQHNCSRQGPTAPPPPRGPALPGAGSGLPAPDPCDYEGRFSRLHGRPPGFLHCASFGDPHVRSFHHHFHTCRVQGAWPLLDNDFLFVQATSSPMALGANATATRKLTIIFKNMQECIDQKVYQAEVDNLPVAFEDGSINGGDRPGGSSLSIQTANPGNHVEIQAAYIGTTIIIRQTAGQLSFSIKVAEDVAMAFSAEQDLQLCVGGCPPSQRLSRSERNRRGAITIDTARRLCKEGLPVEDAYFHSCVFDVLISGDPNFTVAAQAALEDARAFLPDLEKLHLFPSDAGVPLSSATLLAPLLSGLFVLWLCIQ
Protein: Cation transporter HKT1;3 (OsHKT1;3) (Cation transporter HKT6) (OsHKT6) (Q6H501)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functions as a highly-selective sodium transporter. Does not seem to function as sodium-potassium cotransporter. May be involved in turgor changes for rolling and unrolling of leaves in response to environmental variations.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25750424}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:25750424}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Os04g0643100 protein
- Probable V-type proton ATPase subunit d
- V-type proton ATPase subunit F
- Vacuolar proton pump subunit B
- Vacuolar proton pump subunit B
Sequence:
MNHCLVVSHKKLQTFRTFAASKFSSFTKSAQKSIKYSFQFIYQNNPLFVHVAYFALISFAGYGSLKVLKPRDKSNTLKDLDVLFTSVSASTVSSMATVEMEDFSSAQLWVLTILMLIGGEVFTSMLGIHFMRAEFGTKESVSTRDHSPCIDIESITSTKFGPSTQGTKVTVSFSELRMENGGHVEPKTIKFLGFVVMGYLLITNLGGSLLIYLYLNLVPSAHKILKRKGIGIIVFSVFTAISSVGNCGFTPVNENMIIFQKNSILLLLILPQILAGNTLFAPCLRLMVWSLEKITGKKDCRYILEYPKAIGYKHLMSTRESVYLTLTVVSLIILQTVLFLSLEWSSVALDGMSNYQKIVSALFQSVNARHAGESVTDLSNLSSAILVLYTIMMYLPGYTSFLPRHDGEDSKTEKINKRKGLLENWIFSHMSYLAIFVMLICITERDSMATDPLNFNVFSILFEVVSAYGNVGFSVGYSCKRLLNHDARCKDASYGFAGKWSDNGKAILIIVMLFGRLKTFNMKGGRAWKLR
Protein: RE25548p (Q8SWU5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPGRKKNHHKNNNNSRARHQRGGQQSKDKQEQQDKEQSPSPTEEKELPYRVEHSDIYGRYLVANRQLEAGETLIREEPLAIGPCVSGDPVCLGCYHPVSLKADQYRCPGCAWPLCGSTCAGLKHRHGHTETECQLYAERRAVAGELLTERAGPAEVRDLYELVMIVRILLLRQHDPEQFALIARMESHTEERRQNAVLWRHYEEKVVQRLRVTWQLEDLEAEQVHEVCGILDVNCFEIGQNGAKARTLYPSAFLLAHDCTPNTAHTDDPSSFEILLRTSRRVREREALTLGYAYTLQGTLKRRAFMHEGKLFWCCCRRCSDPRELGTDCSALVCATCRTGSVRAVDPLQQTGDWACDRCAHKMGATEVERQLDRINNDLEDIDVHDIPGLENFLLRCVCIHGS
Protein: Mu-cyrtautoxin-As1a (Mu-CUTX-As1a) (Aptotoxin III) (Aps III) (Aptotoxin-3) (Aps-3) (Paralytic peptide III) (PP III) (P49268)
Organism: Apomastus schlingeri (Trap-door spider) (Aptostichus schlingeri)
Function: The recombinant mu-cyrtautoxin-As1a potently and voltage-independently blocks voltage-gated sodium channels (Nav) of insects. It acts by pluging the outer vestibule of the channel. It acts in combination with a weak (30%) voltage-independent block of insect voltage-gated calcium (Cav) channels (low-voltage and high-voltage channels). Tested on DUM neurons, it inhibits sodium currents with an IC(50) of 540 nM (and a Hill coefficient >1, reflecting an incomplete block at higher concentrations). In vivo, it induces flaccid paralysis in adult Australian sheep blowfly Lucilia cuprina. It is both paralytic and lethal, when injected into lepidopteran larvae. It is a slower acting toxin, being lethal at 24 hours, but not paralytic at 1 hour post-injection.
Subcellular location: Secreted {ECO:0000269|PubMed:1440641}.
Interaction partners:
Sequence:
CNSKGTPCTNADECCGGKCAYNVWNCIGGGCSKTCGY
Protein: Sec translocon accessory complex subunit YajC (P9WL75)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein translocase subunit SecA 1
- Protein translocase subunit SecD
- Protein translocase subunit SecE
- Signal recognition particle receptor FtsY
- Signal recognition particle protein
- Probable protein-export membrane protein SecG
- Protein translocase subunit SecA 2
- Protein translocase subunit SecY
- 4-aminobutyrate aminotransferase
- Membrane protein insertase YidC
Sequence:
MESFVLFLPFLLIMGGFMYFASRRQRRAMQATIDLHDSLQPGERVHTTSGLEATIVAIADDTIDLEIAPGVVTTWMKLAIRDRILPDDDIDEELNEDLDKDVDDVAGERRVTNDS
Protein: Peroxisomal biogenesis factor 19 (Peroxin-19) (Peroxisomal farnesylated protein) (A0A0S2Z497)
Organism: Homo sapiens (Human)
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00004405}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004405}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004405}.
Interaction partners:
Sequence:
MAAAEEGCSVGAEADRELEELLESALDDFDKAKPSPAPPSTTTAPDASGPQKRSPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDMTSQQEFTSCLKETLSGLAKNATDLQNSSMSEEELTKAMEGLGMDEGDGEGNILPIMQSIMQNLLSKDVLYPSLKEITEKYPEWLQSHRESLPPEQFEKYQEQHSVMCKICEQFEAETPTDSETTQKARFEMVLDLMQQLQDLGHPPKELAGEMPPGLNFDLDALNLSGPPGASGEQCLIM
Protein: 6-hydroxynicotinate 3-monooxygenase (6-HNA monooxygenase) (EC 1.14.13.114) (Nicotinate degradation protein C) (Q88FY2)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Flavin-dependent monooxygenase (FMO) that catalyzes the decarboxylative hydroxylation of 6-hydroxynicotinic acid (6-HNA) to 2,5-dihydroxypyridine (2,5-DHP) with concomitant oxidation of NADH, a step in the aerobic nicotinate degradation pathway.
Interaction partners:
- 2,5-dihydroxypyridine 5,6-dioxygenase
- N-formylmaleamate deformylase
- Maleate isomerase
- Nicotinate dehydrogenase subunit A
- Nicotinate dehydrogenase subunit B
- HTH-type transcriptional repressor NicR
- Maleamate amidohydrolase
- Putative metabolite transport protein NicT
- Porin-like protein NicP
- Aminotransferase
Sequence:
MRGRQKIAIVGAGLGGAAAATLLQQAGFDVEVFEQAPAFTRLGAGIHIGPNVMKIFRRMGLEQKLELMGSHPDFWFSRDGNTGDYLSRIPLGEFARREYGAAYITIHRGDLHALQIEAIQPGTVHFGKRLEKIVDEGDQVRLDFADGTHTVADIVIGADGIHSKIREELLGAEAPIYSGWVAHRALIRGVNLAQHADVFEPCVKWWSEDRHMMVYYTTGKRDEYYFVTGVPHEAWDFQGAFVDSSQEEMRAAFEGYHPTVQKLIDATESITKWPLRNRNPLPLWSRGRLVLLGDACHPMKPHMAQGACMAIEDAAMLTRCLQETGLSDHRTAFALYEANRKERASQVQSVSNANTWLYSQEDPAWVYGYDLYGQQLESGEAA
Protein: D-aspartate oxidase 2 (DASOX 2) (DASPO 2) (DDO-2) (EC 1.4.3.1) (Q19564)
Organism: Caenorhabditis elegans
Function: Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. Highest catalytic efficiency for D-Glu followed by D-Asp and NMDA. May play a role in the egg-laying events and early development of the worm, in addition to quality control of the germ cells.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase
- Aspartate aminotransferase
- D-aspartate oxidase 3
- D-aspartate oxidase 1
- Probable citrate synthase, mitochondrial
- Isocitrate dehydrogenase subunit
- Pyruvate carboxylase 1
- Phosphoenolpyruvate carboxykinase
- Phosphoenolpyruvate carboxykinase
Sequence:
MANIIPKIAIIGEGVIGCTSALQISKAIPNAKITVLHDKPFKKSCSAGPAGLFRIDYEENTEYGRASFAWFSHLYRTTKGSETGVKLVSGHIQSDNLESLKQQQRAYGDIVYNFRFLDDRERLDIFPEPSKHCIHYTAYASEGNKYVPYLKNLLLEQKIEFKQQEVTSLDAVADAGYDVIVNCAGLYGGKLAGDDDTCYPIRGVILEVDAPWHKHFNYRDFTTFTIPKEHSVVVGSTKQDNRWDLEITDEDRNDILKRYIALHPGMREPKIIKEWSALRPGRKHVRIEAQKRTSVGNSKDYMVVHHYGHGSNGFTLGWGTAIEATKLVKTALGL
Protein: Eyes absent homolog (EC 3.1.3.48) (E9QGZ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MENTQDLNEQSVKKSTTDSHAPDPVDNRALEMQELTDVQHSVNSGSDGTSKLDKNILSNNITTNGTGGENMTILNTADWLLGCSSPPTAPIKSEPLNSSEAVSSAGDSGLDTYTGSVISSSGFSPRPAHQYSPPLYPSKPYPHILTTPVAPPMSAYTGQSQFSSMQQSTVYTPYSQTTPPYGLSTYATDLGVMLPGIKTEGGLTQTQSTLQSGLSYSPGFTTPQPGQTAYSPYQMPAGSGFTTSPGLYTSNNSNPGNFTTQQQEYPSYTTFGQNQYAQYYSTSSYGSYMTSNSSLDGTGSVSTYQLQDPIMTGQAADLNPGEFEAGQSPSTPIKEMEDRACRGGGAKARGRGRKNNPSPPPDSDLERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPLAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDASSDDNGQDLGTYSFATDGFHAAATSASLCLATGVRGGVDWMRKLAFRYRRVKELYCTYKNNVGGLLGPAKREAWLQLRAEVEALTDSWLTSALKSLSIISSRSNCVNVLVTTTQLIPALAKVLLYSLGSAFPIENIYSATKIGKESCFERVMQRFGRKVVYVVIGDGVEEEQAAAKHNMPFWRISSHSDLLALHQALEFEYL