wanglab/gogpt-training-data huggingface dataset:
Protein: Glycosidase (EC 3.2.-.-) (G8BGU6)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}. Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}.
Interaction partners:
Sequence:
MKAIYVLFLTLLSVTLAADVVSCNATQHCPEDSPCCSQFGECGTGAYCLGGCDIRYSYNLTACMPMPRMDDYSKTFDSKSAVKEIELANEYLGNATEADWVYTGWIDYYNSSLLLQMPNHTTGTVLSSTKYLWYGKVSAKMKTSHGGGVVTAFILFSDVQDEIDYEFVGYNLQAAESNFYAQGILNYTNSKNATVNDTFEYYHLYEMDWHEDHITWSIDNKAVRTLNRNETWNETTKRHDFPQTPSRIQFSLWPGGDSSNGVGTIEWAGGEIDWNAEDIKKYGYFYAHIKEIDVEVYDLPGNVSLSSNSSNSDDYHAFLYDSTDGDESNIYLTNKKTWLGNDDATGFDPDNDRDTQNENETTTIVKTSGSSTITSVQTSTKRVSANAPAQNTAAANKATATQDSTTTDYDPSAGVGGFVQNSKETSSGDSSSSGGAAGLTYEVGKESIFFAIALGFVSYFV
Protein: Histone H1.8 (Histone H1oo) (Oocyte-specific histone H1) (Oocyte-specific linker histone H1) (osH1) (Q8IZA3)
Organism: Homo sapiens (Human)
Function: May play a key role in the control of gene expression during oogenesis and early embryogenesis, presumably through the perturbation of chromatin structure. Essential for meiotic maturation of germinal vesicle-stage oocytes. The somatic type linker histone H1c is rapidly replaced by H1oo in a donor nucleus transplanted into an oocyte. The greater mobility of H1oo as compared to H1c may contribute to this rapid replacement and increased instability of the embryonic chromatin structure. The rapid replacement of H1c with H1oo may play an important role in nuclear remodeling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}.
Interaction partners:
- Histone H1t
- Histone H3.1t
- Testis-specific H1 histone
- Histone H1.10
- Histone H1.1
- Histone H1.5
- Histone H1.0
- Histone H1.2
- Histone H1.3
- Histone H1.4
Sequence:
MAPGSVTSDISPSSTSTAGSSRSPESEKPGPSHGGVPPGGPSHSSLPVGRRHPPVLRMVLEALQAGEQRRGTSVAAIKLYILHKYPTVDVLRFKYLLKQALATGMRRGLLARPLNSKARGATGSFKLVPKHKKKIQPRKMAPATAPRRAGEAKGKGPKKPSEAKEDPPNVGKVKKAAKRPAKVQKPPPKPGAATEKARKQGGAAKDTRAQSGEARKVPPKPDKAMRAPSSAGGLSRKAKAKGSRSSQGDAEAYRKTKAESKSSKPTASKVKNGAASPTKKKVVAKAKAPKAGQGPNTKAAAPAKGSGSKVVPAHLSRKTEAPKGPRKAGLPIKASSSKVSSQRAEA
Protein: AT5g48790/K24G6_12 (LOW PSII ACCUMULATION protein (DUF1995)) (Q94F50)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Trafficking protein particle complex subunit-like protein
- Ferredoxin C 2, chloroplastic
- NDR1/HIN1-like protein 1
- Cysteine-rich receptor-like protein kinase 7
- Protein RER1B
- Protein transport protein SEC24 B
- Calcium-dependent protein kinase 29
- 26S proteasome non-ATPase regulatory subunit 2 homolog B
- Trafficking protein particle complex subunit
Sequence:
MSPSFSIATTVSPASLAGTLASNSKNVLCSLHSKNNDITKTNRNLKFRACSVSGGYNNNTSVDNVPFPRDYVELINQAKEAVEMALKDEKQLMEIEFPTSGLASVPGDGEGATEMTESINMIREFCDRLLAPEKARSTRIFFPEANEVKFAQKTVFGGTYFKLDYLTKPSLFEDFGFFERVKMADRVKPEDELFLVAYPYFNVNEMLVVEELYKEAVVNTDRKLIIFNGELDRIRSGYYPKFFYPKLAALTKTLLPKMETVYYIHNFKGQKGGVLFRCYPGPWQVLRRTRNKYICVHQQESMPSLKEVALDILASA
Protein: Trafficking protein particle complex subunit 5 (41-2 protein antigen) (Q7KQM2)
Organism: Plasmodium falciparum (isolate 3D7)
Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:Q03337}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q03337}. Cell membrane {ECO:0000250|UniProtKB:P15847}; Peripheral membrane protein {ECO:0000305}. Host membrane {ECO:0000250|UniProtKB:P15847}; Peripheral membrane protein {ECO:0000305}. Note=Schizont membrane, internal surface of parasitized erythrocytes and on membranous structures in the erythrocyte cytoplasm. {ECO:0000250|UniProtKB:P15847}.
Interaction partners:
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 6A, putative
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 2, putative
- Trafficking protein particle complex subunit 8, putative
- Trafficking protein particle complex subunit 2-like protein, putative
- Ras-related protein Rab-1A
- Ras-related protein Rab-1B
- Trafficking protein particle complex subunit 13 N-terminal domain-containing protein
Sequence:
MDKSKSSIEKELNRIKQDVSLSAFSILFSEMVQYCLYKSKRGYRIEDCLHEMGLRVGYKLNEYLTYKNKVKRSINIINILTFISKHVWKYLFQHSSDLLKSQDSIYEYMICDKNILLNKFINVPKDYGNINCAAFAAGIVEGFLCSSEFQADVTAHTIHEGDDNYNTTIFIKFYPEVVEREKNH
Protein: Gamma-curcumene synthase (EC 4.2.3.94) (PatTpsA) (Q49SP7)
Organism: Pogostemon cablin (Patchouli) (Mentha cablin)
Function: Sesquiterpene synthase involved in gamma-curcumene biosynthesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
Sequence:
MAAFTANAVDMRPPVITIHPRSKDIFSQFSLDDKLQKQYAQGIEALKEEARSMLMAAKSAKVMILIDTLERLGLGYHFEKEIEEKLEAIYKKEDGDDYDLFTTALRFRLLRQHQRRVPCSVFDKFMNKEGKFEEEPLISDVEGLLSLYDAAYLQIHGEHILQEALIFTTHHLTRIEPQLDDHSPLKLKLNRALEFPFYREIPIIYAHFYISVYERDDSRDEVLLKMAKLSYNFLQNLYKKELSQLSRWWNKLELIPNLPYIRDSVAGAYLWAVALYFEPQYSDVRMAIAKLIQIAAAVDDTYDNYATIREAQLLTEALERLNVHEIDTLPDYMKIVYRFVMSWSEDFERDATIKEQMLATPYFKAEMKKLGRAYNQELKWVMERQLPSFEEYMKNSEITSGVYIMFTVISPYLNSATQKNIDWLLSQPRLASSTAIVMRCCNDLGSNQRESKGGEVMTSLDCYMKQHGASKQETISKFKLIIEDEWKNLNEEWAATTCLPKVMVEIFRNYARIAGFCYKNNGDAYTSPKIVQQCFDALFVNPLRI
Protein: Kinetochore protein ndc80 (NMS complex subunit ndc80) (Q10198)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores.
Interaction partners:
- Kinetochore protein spc24
- Kinetochore protein nuf2
- Kinetochore protein spc25
- DASH complex subunit spc19
- Spindle pole body component alp14
- DASH complex subunit dam1
- Kinetochore protein mis13
- Outer kinetochore KNL1 complex subunit spc7
- Spindle assembly checkpoint serine/threonine-protein kinase bub1
- Microtubule protein alp7
Sequence:
MQDSSSYARRYSQAPSSSNLRTTTFGFNGLGTSRTSLAPQRTLVNARQSIDPDGLSSRVLTPTMRPSLAPNTRRSSVRVSNASFISQTPNITSIKDPRPLSDRRYQQECATQVVNYLLESGFSQPLGLNNRFMPSTREFAAIFKHLYNKLDPNFRFGARYEEDVTTCLKALNYPFLDSISRSRLVAIGSPHVWPAILGMLHWVVSLIQCTEKAVAMVYTVEQNSLDDHLVDKVLFDYLVRTYHLYLDESPEESEPEKELKATFNQQNQDLYNQTEALKSTNEELINQIKSAEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQVNIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVSEREQLDRNLNMIGSKISELRKEVFDTDLLIQASIDSLEKKVQKFNSLAYRIGIVPIAAIRSANNDFELEINPEGPNYINLDLKNKVRPFINEVRRSITLEFHEEQNKSLKLQEHVDTVNDLIAELQDELRGIESRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLKLSSHNSMLQLDQRIQSINIEADQIAHACMEYKNNIYKEVAFVLGEIIHFKLHVQDSLEDLKMDYQKELDDLSRSEL
Protein: Galectin-1 (Gal-1) (Lectin galactoside-binding soluble 1) (Q49I35)
Organism: Sus scrofa (Pig)
Function: Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P09382}. Cytoplasm {ECO:0000250|UniProtKB:P09382}. Secreted {ECO:0000250|UniProtKB:P09382}. Note=Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000250|UniProtKB:P09382}.
Interaction partners:
Sequence:
MACGLVASNLNLKPGECLKVRGEVAPDAKSFVLNLGKDSNNLCLHFNPRFDMHGDINTIVCNSKDGGAWGAEQRESAFPFQPGSVVEVCISFGQTDLTIKLPDGYEFSFPNRLNLEAIEHLAADGDFKIKCVAFE
Protein: Signal-regulatory protein beta 1A (A0A0A6YYP6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLLLDAWTHIPHSVLLLILLLGFKGAAVRELKVIQPVKSFFVGAGGSATLNCTVTSLLPVGPIRWYRGVGQSRLLIYPFTGEHSPRITNVSDVTKRNNMDFSIRISNVTPADSGTYYCVKFQRGSSEPDIEIQSGGGTELLVLAKPSSPMVSGPAARAVPQQTVTFTCRSHGFFPRNLTLKWFKNGDEISHLETSVEPEETSVSYRVSSTVQVVLEPRDVRSQIICEVDHVTLDRAPLRGIAHISEFIQVPPTLEIRQQPTMVWNVINVTCQIQKFYPPSFQLTWLENGNISRREVPFTLIVNKDGTYNWISCLLVNISALEENMVVTCKVEHDEQAEVIETHTVLVTEHQRVKGTATKSELKTAGIAKIPVAVLLGSKILLLIAATVIYMHKKQNA
Protein: Virulence protein F (P15597)
Organism: Agrobacterium tumefaciens (strain 15955)
Function: In the host plant, component of SCF(virF) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins such as the host VIP1, after its implication in T-DNA translocation to the host nucleus (By similarity). Required for the formation of tumors of a wild-type size on certain plant species only.
Subcellular location: Host nucleus {ECO:0000269|PubMed:26571494}.
Interaction partners:
Sequence:
MRNSSLRDASGSNDAQVPHKTELLNLPDHVLTEVAKRLATNNPVESAENIANFSKSHRFTRDAVRTEPLEKFSSRLKILSRNAKLLSHAVRHAATLPDGEQLSEAQLSQMRSEVATRPVLGVAYTHQDGQPEERLSGNHLDHKINNIPNLVFNVAEPIMFNEISALEVMAEVRPIARSIKTAHDDARAELMSADRPRSTRGL
Protein: VIP peptides [Cleaved into: Intestinal peptide PHI-27-like; Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide)] (P45644)
Organism: Meleagris gallopavo (Wild turkey)
Function: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MEHRGTSPLLLALALLSALCWRARALPPRGAAFPAVPRLGNRLPFDAASESDRAHGSLKSESDILQNTLPENEKFYFDLSRIIDRNDRHADGIFTTVYSHLLAKLAVKRYLHSLIRKRVSSQDSPVKRHSDAVFTDNYSRFRKQMAVKKYLNSVLTGKRSQEELNPAKLADEAEILEPSFSENYDDVSVDELLSHLPLDL
Protein: precorrin-2 dehydrogenase (EC 1.3.1.76) (A0A1D8PGS2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- precorrin-2 dehydrogenase
- Porphobilinogen deaminase
- Uroporphyrinogen-III synthase
- Uroporphyrinogen decarboxylase
- Sulfite reductase subunit beta
- assimilatory sulfite reductase
- Adenylyl-sulfate kinase
- phosphoadenylyl-sulfate reductase
- Sulfate adenylyltransferase
- Delta-aminolevulinic acid dehydratase
Sequence:
MTNLLTSNITTGETHLLIGYSAVSNTRIVSIIESGANPILITDSQPQNFPPNIMQYVTDNKLPVLIDKDFPTKIPHYLTTLGRAEVDSIVDRVYVSLPSSQLALKQEIYQRCRKLRIPVNTTDSPDLCTFTMLSTYTSGDFQLGVTTNGKGCKLASRIKRELVNSLPSDIDAICKQVGELRRQIQMEDKAESEHGEHEDDAINNHKFNSFVPEFNKTQEDLKLQRARWLSQIVEYYPLNKLGSISLKDLSSAYKLHKQANVPGAKEEDSEAGQMTLVGSGPGSVSLLTLGALQAIQTADLVLADKLVPQQVLDVIPTTHHTRLFIARKFPGNAEKAQEELLTLGLEALRRGEKVVRLKQGDPYIFGRGGEEFNFFSQHGFKPTVVPGITSALAAPVLSNIPMTHRDVADQVLICTGTGRRGAVPNLPDFVSSRTTVFLMALHRVVELIPLLVNDKKWDENLPVAIVERASCPDQRVIRTTLSKVGDAVEACGSRPPGLLVTGYACEVICKNSGSESLPWVVEEGCNSGDDGELKRIVELVNGNCKESTAVVSPNLQKEIAA
Protein: 1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform E (EC 2.3.-.-, EC 2.3.1.51) (MIP21173p) (D5AEK7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase 4, isoform D
- BcDNA.GH07066
- Phospholipid/glycerol acyltransferase domain-containing protein
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- phosphatidate phosphatase
- Diacylglycerol kinase 1
- Phosphatidate cytidylyltransferase, photoreceptor-specific
- Phospholipase
- Membrane-bound acylglycerophosphatidylinositol O-acyltransferase frj
Sequence:
MVVHKNSFVIKMGSLEKLKQLRLIHLCIALTFFTSGLCINFIQLLMHVFIKPIDKRLFRKLMYYACYSLYSQLIFVSDWYAGSKMTVYMDKEDFEKHAGKEHVLLIMNHKYEIDWLNGWMICEKLGVLGNCKAYAKKAIRYVPIIGWGWWLAEFVFLNRNFDQDKTIITEQLKVVFSYPDPTWLLLNAEGTRFTPAKHEASVKFAQERGMTVLKHHLIPRTKGFTASLAPIRGLCPVIYDINLAYRPTDKTPATMLSLLHGKSVEPHLLMRRIPLEQVPEDEKEAAAWLQNLFVEKDKIIDSFLETGSFFKTSGIKEVPAYVNKRRLCSLVNFVCWAVFSLSCIFYYVITSLLAANWTAFITALSVLGLFYWLMGQAINKTQISKASNYGSSKSVAK
Protein: Caffeic acid O-methyltransferase (I1I1F5)
Organism: Brachypodium distachyon (Purple false brome) (Trachynia distachya)
Interaction partners:
Sequence:
MGSTAADMAATADEEACMFALQLASSSILPMTLKNAIELGLLDTLVQASGKSLTPAEVAAKLPSSSNPAAPDMVDRMLRLLASYGVVSCAVEEGENGKLSRRYAAAPVCKWLTPNEDGVSMAALALMNQDKVLMESWYYLKDAVLDGGIPFNKAYGMSAFEYHGTDPRFNRVFNEGMKNHSIIITKKLLDLYPGFEGLGTLVDVGGGVGATVGAIVARHPAIKGINFDLPHVISEGIPFPGVTHVGGDMFQKVPSGDAILMKWILHDWSDAHCATLLKNCYDALPAHGKVVIVECILPVNPEATPKAQGVFHVDMIMLAHNPGGKERYEREFEELARGAGFTGVKATYIYANAWAIEFTK
Protein: Transcription factor NRM1 (Negative regulator of MBF targets 1) (P53718)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Negative regulatory component of the MBF complex involved in cell-cycle-dependent transcription.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcription factor MBP1
- Regulatory protein SWI6
- Protein phosphatase PP2A regulatory subunit B
- Protein STB1
- G1-specific transcriptional repressor WHI5
- Regulatory protein SWI4
- Homeobox protein YOX1
- Cyclin-dependent kinase 1
- Serine/threonine-protein kinase RAD53
- G1/S-specific cyclin CLN1
Sequence:
MSIMKQRLPLGEFSSSKINKLAIANIADASEPRNHGENNVGTVCLPSIKSLMVSPEVYENTKSLPVPLMRSSGGGMACASKSSCQDGISTKTTSRDYSELSKKLQIRLQFAYYKYKTKQTDKNFTDLKSKHSITRPSKVATHSKSEPLTRRRKLVLSQGHYKTPARSKIKTPSSICSHDNTSSFTSFRGVSESSSTTADMNVADTTTPIRNNINTKHSNSHNRTLYQRQETPTSIKAAKSLIHLFTSNQ
Protein: Midkine and pleiotrophin 2, isoform D (M9PDI0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- peptidylprolyl isomerase
Sequence:
MNLILALTTALHLVLVVLAHNPLSTRGESLSDGIRLVMEKRSGDVVHIRPARGTLEAETVASTTNSDTHRTRNNRKPNKPQEHSQQVGAHKSGSRKLVVAENGGALSSQLPQPNHKQGHKNTDKQQRGGGSKQQRGHSQHHGGNRKGPKAATPENGSTCRYAKSAWSNCDHKTNMRSRVLSLRKGEQNCLPTRTIQKKCKKGARGCRYEKGEWSQCVGGQITREDKLEPEATGGSDQNCNPVRTVSKKCKANGNSSGGKQHGQSRRTKEQKQKDKGASHISS
Protein: Chromosome partition protein Smc (Q98PK8)
Organism: Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
Interaction partners:
- Segregation and condensation protein A
- Segregation and condensation protein B
Sequence:
MKLIKIQAHGFKSFAEPIQLSFDGGVAGIIGPNGSGKSNINDAIKWVLGEQSSKSLRGDNMEDVIFAGSKNVKEMNKASVTLTFDNSNNASSVPHKVFTITRELERGKGSNIYYINDEIVRYKDIKDIALESGISKSSLAIISQGTVSDIAEASPEDRRGIFEEAAGVSKYKSRKKEALRKLEKTNESLEKIQTVILELEKQLKPLKNQAEKARIYLQKSKELKDVEVGLIIHNLDFYSTKLKEFEIELEGVVETKENLEQQVRKCENIIEQNSGDRLKFEKELHFLVQDLDNLNEKLRNLELISANENQRRELIISGQIKVNPEEKMKVIKEQLQIIKSRINFYTKQTEELSQIVSDKKNEVQELEKTISTKRIEQNKISNKLNETKVKINILLEHKKNKTNMFKGTKTIVEHKNIFKGYHGLVSEVLKVDQEYIPAIDAVLNNALQHIVVEDAQIAVTAVNFLKKNDGGRATFIPLKSIKPKSIKDEHFLALNMKKGFIDVASNLVKYEPKFEVLSKFLLGNILVVSDIESAKDIAAILDNKYMIVTLEGDLIRTGGVITGGVQQASTNLIGLDEQIAKLEEIVPIISKEVENTSNQITNLEHKKYELTNVVSEFSVEAAKVYEKLSNDQKSFDSLTAEYQTISAKDLGESSSSALDQQINEIQAKKVILQAQIRAKKESILSLNTDFSKVTLEKNDLEKSLRILNDSFSKKITEKNKAEFYLDTNQKRLSEFYNMTYEMAKDNFSLSIDITEAEEFVGRIKEEIKDLGNINIDSIKSYEEISERYDGLKATESEIVDAKDKIESAIKEMDKIIITKLRDTLSAINEEFNNVFQSMFGGGEARVEFVDPSDILESGIDIKAQPPGKSIKNLKLFSGGEKSLIAISLLFAILKSKPLPLCILDEVEAALDDANVVRYAEYLQKLKTKTQFLVITHRHGTMSRVDHLFGATMQTRGVTSFFSVELARAKELIKDTKIES
Protein: Follitropin subunit beta (Follicle-stimulating hormone beta subunit) (FSH-B) (FSH-beta) (Follitropin beta chain) (P18427)
Organism: Rattus norvegicus (Rat)
Function: Together with the alpha chain CGA constitutes follitropin, the follicle-stimulating hormone, and provides its biological specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled receptor, on target cells to activate downstream signaling pathways. Follitropin is involved in follicle development and spermatogenesis in reproductive organs.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01225}. Note=Efficient secretion requires dimerization with CGA. {ECO:0000250|UniProtKB:P01225}.
Interaction partners:
- Glycoprotein hormones alpha chain
- Follicle-stimulating hormone receptor
- Lutropin-choriogonadotropic hormone receptor
- Gonadotropin-releasing hormone receptor
- Thyrotropin receptor
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Progonadoliberin-1
- Prolactin
- Pro-opiomelanocortin
- Sulfite oxidase, mitochondrial
Sequence:
MMKSIQLCILLWCLRAVCCHSCELTNITISVEKEECRFCISINTTWCEGYCYTRDLVYKDPARPNTQKVCTFKELVYETIRLPGCARHSDSLYTYPVATECHCGKCDSDSTDCTVRGLGPSYCSFGEMKE
Protein: cAMP-dependent protein kinase type 3 (PKA 3) (EC 2.7.11.11) (P05986)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- cAMP-dependent protein kinase type 2
- cAMP-dependent protein kinase type 1
- Ras-like protein 2
- Adenylate cyclase
- Ras-like protein 1
- Zinc finger protein MSN4
- Zinc finger protein MSN2
- 3',5'-cyclic-nucleotide phosphodiesterase 2
- Protein SOK2
Sequence:
MYVDPMNNNEIRKLSITAKTETTPDNVGQDIPVNAHSVHEECSSNTPVEINGRNSGKLKEEASAGICLVKKPMLQYRDTSGKYSLSDFQILRTLGTGSFGRVHLIRSNHNGRFYALKTLKKHTIVKLKQVEHTNDERRMLSIVSHPFIIRMWGTFQDSQQVFMVMDYIEGGELFSLLRKSQRFPNPVAKFYAAEVCLALEYLHSKDIIYRDLKPENILLDKNGHIKITDFGFAKYVPDVTYTLCGTPDYIAPEVVSTKPYNKSVDWWSFGVLIYEMLAGYTPFYNSNTMKTYENILNAELKFPPFFHPDAQDLLKKLITRDLSERLGNLQNGSEDVKNHPWFNEVIWEKLLARYIETPYEPPIQQGQGDTSQFDRYPEEEFNYGIQGEDPYMDLMKEF
Protein: Deoxyhypusine synthase (DHS) (EC 2.5.1.46) (Deoxyhypusine synthase from chromosome 34) (DHS34) (B5APK2)
Organism: Leishmania donovani
Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Interaction partners:
Sequence:
MANIAESAVLVSSASSAQAVAKLTQVRGPTSGFDKAQHIIGSYSTMGFQATNYGLARSIAQRMIRKQPPSKVYQIKDGKYVLVPPDVGEDGKTLQQEHVYPNLFMGVTANLMGTGCREAVRFLVQEGVVHRSLEASAPASADGTDDQLMFARLKREYVETYGGPPHPDEEIPRAHSFLCAIVVSGGGVEHDLRRACTAYTLHHYASEAQGHVSSTVSSEATAPPKGLQQRAEKPLGTRAAAGTAKPARFGNVEYPRQGSTGSELFDCLMRTFVQRLCARQARLRAAAMAKPIPDKYDDVCSWSVTPSEVWALCGLWLVDMLAEALGAVRSCTSRLTSGSAVGTAESVTANGKGPEADRDAHIATSASYRAEALARARTTVVYWAALQQVSLFSPSFVDGDITSYLLPTPAPAARPAHRKGGPVADENAGNSKELKRSRKASSSSSTSATAVKVKPPVVERLQVDLVRDVYSINKLAMLSKKTGMLICGGGVVKHHVCNANLMRNGADFTIILSNGQEFDGSDAGAKPEEALSWGKVRMEGAFVKVYGEVSTYLPLLLAEVFVPAVRQRRATDDAQPRRKRSSRGARPPQDVSGHSHLCRGE
Protein: ESCRT-related protein CHMP1A (Protein CHARGED MULTIVESICULAR BODY PROTEIN 1A) (Protein CHROMATIN MODIFYING PROTEIN 1A) (Vacuolar protein-sorting-associated protein 46.1) (Q8LE58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ESCRT-dependent multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. Mediates the MVB sorting of the auxin carriers PIN1, PIN2 and AUX1. Required for embryonic axis establishment and seedling growth. Required for autophagic degradation of plastid proteins. Promotes the efficient sequestration of cargo from plastids into autophagosomes. Mediates the efficient delivery of autophagic plastid bodies to the vacuole, but not into the cytoplasm.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9HD42}. Endosome membrane {ECO:0000250|UniProtKB:Q9HD42}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HD42}.
Interaction partners:
- Protein HOMOLOG OF MAMMALIAN LYST-INTERACTING PROTEIN 5
- Vacuolar protein sorting-associated protein 2 homolog 2
- Protein SUPPRESSOR OF K
- Vacuolar protein sorting-associated protein 32 homolog 2
- Vacuolar protein sorting-associated protein 32 homolog 1
- Vacuolar protein sorting-associated protein
- Vacuolar protein sorting-associated protein 2 homolog 1
- Vacuolar protein sorting-associated protein 24 homolog 1
- Vacuolar protein sorting-associated protein 60.1
- Vacuolar protein sorting-associated protein 60.2
Sequence:
MGNTDKLMNQIFELKFTSKSLQRQARKCEKEERSEKLKVKKAIEKGNMDGARIYAENAIRKRSEQMNYLRLSSRLDAVVARLDTQAKMATITKSMTNIVKSLESSLTTGNLQKMSETMDSFEKQFVNMEVQAEFMDNAMAGSTSLSTPEGEVNSLMQQVADDYGLEVSVGLPQPAGHAIPTKTEEKVEEDDLTRRLAELKARG
Protein: Small ribosomal subunit protein mS33 (Mitochondrial 37S ribosomal protein S27) (P53305)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11278769, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS19m
- Small ribosomal subunit protein uS12m
Sequence:
MNVPKARLLKVAELSAKIFDQNFNPSGIRTGSKILNERLKGPSVASYYGNPDILKFRHLKTLYPDIEFVDLEEQYRLSMVEAKKRRGKGAPKKMKKDAAATAKGKGKKKK
Protein: Calmodulin, putative (Q587D7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTHVGAAHSLPPQFDSLSPEEVDMLRDSFIYMDRDNDGHVSKAELLDMVFRCVGEERYGPLVSYLLPLFDVADKDGDGKLSLAEFVMSFVDGPGVVPAEVINSCVSSIRVRLTDEEIVTLQDSFRRIDTKADGYIDREELLAALKENLKDTFPDLRENNFNDIVAVIMASADVDNDGRLCLSEFIRSFQEDQGVLPAVFVDARSNGFVQHLSPAEVEVLREAFATLDKNHDGYVEFADIYESLWEAVSDENYDKNQIYELCDLIMVTTDRSKSGVLTLGDFVRGFIRNVTLVQLPVATAHEEILRCCERVQLLFESGELERLSGYTETGENTTKCVNPGGLVSVLSNVFRDGFPLLEEEILSSVIGALVAASENDLDKKFGIEEFISCFAGGPCSSSDGVGLLDHENAISESDVQTVSRLLRDLGKSADEGGNVQEPFVLEAVRNTFRDDPEKADRVVQYVQYNTTCPSNLGSGVGGLGSSSKLLSSKEDSASLPTKKFSGPVRGVDAAVQCEQVSETQGEPEEEEEELRVAEPLTEKGVGGTSLGLRDLLKTSSGANVGAKTGRLLTSRPVYRSMRISEWAANQRSGLNLSDATIEGKQKGFDSKLRKEFEKFAEGNDYIERSRFVKLYLSMEHFGLPPSEAQVNELVSRYCRGDKLKFNEFCIIMLRRVGM
Protein: Fasciclin-like arabinogalactan protein 11 (Q8LEJ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a cell surface adhesion protein.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Chitinase-like protein 2
- Fasciclin-like arabinogalactan protein 3
- Cellulose synthase A catalytic subunit 7
- Cellulose synthase A catalytic subunit 4
- COBRA-like protein 4
- Cellulose synthase A catalytic subunit 8
- Fasciclin-like arabinogalactan protein 16
- Fasciclin-like arabinogalactan protein 15
- Fasciclin-like arabinogalactan protein 17
- Fasciclin-like arabinogalactan protein 14
Sequence:
MATSRTFIFSNLFIFFLVIATTYGQAPAPGPSGPTNITAILEKAGQFTLFIRLLKSTQASDQINTQLNSSSSNGLTVFAPTDNAFNSLKSGTLNSLSDQQKVQLVQFHVLPTLITMPQFQTVSNPLRTQAGDGQNGKFPLNITSSGNQVNITTGVVSATVANSVYSDKQLAVYQVDQVLLPLAMFGSSVAPAPAPEKGGSVSKGSASGGDDGGDSTDSSDAERTGFGFGIRITTVAAIAASSSLWI