wanglab/gogpt-training-data huggingface dataset:
Protein: Geranylgeranyl pyrophosphate synthase 7, chloroplastic (GGPP synthase 7) (GGPS7) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase 7) (Dimethylallyltranstransferase 7) (EC 2.5.1.1) (Farnesyl diphosphate synthase 7) (Farnesyltranstransferase 7) (EC 2.5.1.29) (Geranyltranstransferase 7) (EC 2.5.1.10) (Q9ZU77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Geranylgeranyl diphosphate reductase, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Phytoene synthase 1, chloroplastic
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- Isopentenyl phosphate kinase
- Farnesyl pyrophosphate synthase 1, mitochondrial
- Ent-copalyl diphosphate synthase, chloroplastic
- Dehydrodolichyl diphosphate synthase 7
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
Sequence:
MTTLNLSIFPSVKISSSASIPGFIKIQPFLLRRKLSTVLSVTARDEGIIHNHFDFTSYMIGKANAVNEALDSAVSLREPIKIHEAIRYSLLARGKRVRPVLCIAACELVGGEESVALPAACAVEMIHTMSLIHDDLPCMDNDDLRRGKPTNHKVFGEDVAVLAGDALISFAFEHLATSTAVSPARVVRAIGELAKAIGSKGLVAGQVVDLTSGGMDQNDVGLEVLEFIHVHKTAVLLEAATVLGAIVGGGSDEEVEKLRRFARCIGLLFQVVDDILDVTKSSEELGKTAGKDLIADKLTYPKLMGLEKSKDFADKLLSDAHEQLHGFDSSRVKPLLALANYIAKRQN
Protein: Max-like protein 1 (G5EEH5)
Organism: Caenorhabditis elegans
Function: Transcriptional regulator which binds to the E box motif 5'-CACGTG-3', when in a heterodimeric complex with mdl-1. Involved in the control of lifespan in response to dietary restriction, the decline in protein homeostasis associated with normal aging and may overlap with the insulin-like signaling pathway. Involved in promoting infection by the microsporidian pathogen N.parisii.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Mad-like protein 1
- Protein mxl-3
- Mitogen-activated protein kinase pmk-3
- Mitogen-activated protein kinase pmk-1
- Mitogen-activated protein kinase pmk-2
- Max-like protein homolog 2
- Protein WBSCR14 homolog
- 5'-tyrosyl-DNA phosphodiesterase
- BCL7-like protein
Sequence:
MSDMSDLEDDQTGHCGSGEHSGPFDPKRHAREQHNALERRRRDNIKDMYTSLREVVPDANGERVQASRAVILKKAIESIEKGQSDSATLSVDVAEQESKNAKLREEIARLKAKKDPSSSQSIIQ
Protein: Nuclear pore complex protein Nup50 (50 kDa nucleoporin) (Nuclear pore-associated protein 60 kDa-like) (Nucleoporin Nup50) (O08587)
Organism: Rattus norvegicus (Rat)
Function: Component of the nuclear pore complex that has a direct role in nuclear protein import. Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling. Interacts with regulatory proteins of cell cycle progression including CDKN1B. This interaction is required for correct intracellular transport and degradation of CDKN1B.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10891499}. Nucleus membrane {ECO:0000269|PubMed:10891499}; Peripheral membrane protein {ECO:0000269|PubMed:10891499}; Nucleoplasmic side {ECO:0000269|PubMed:10891499}. Note=Dissociates from the NPC structure early during prophase of mitosis (By similarity). Associates with the newly formed nuclear membrane during telophase (By similarity). Localizes to the nucleoplasmic fibrils of the nuclear pore complex (PubMed:10891499). In the testis, the localization changes during germ cell differentiation from the nuclear surface in spermatocytes to the whole nucleus (interior) in spermatids and back to the nuclear surface in spermatozoa (PubMed:9073512). {ECO:0000250|UniProtKB:Q9UKX7, ECO:0000269|PubMed:10891499, ECO:0000269|PubMed:9073512}.
Interaction partners:
- Nuclear pore complex protein Nup153
- Nuclear pore complex protein Nup98-Nup96
- Nucleoporin 205
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup88
- Nuclear pore membrane glycoprotein 210
- Nuclear pore complex protein Nup155
- Nucleoporin NUP188
- Nucleoporin NUP35
Sequence:
MAKRVAEKELTDRNWDEEDEVEEMGTFSVASEEVMKNRAVKKAKRRNIGFESDSGGAFKGFKGLVVPSGGGGFSGFGGGSGGKPLEGLTNGNSTDSATPFSSAKTAAEPKAAFGSFAVNGPTTLVDKKISSPKCNSSNQPPSSGPASSTSCTGNTYHKQLAGLNCSVRDWIVKHVNTNPLCDLTPIFKDYERYLATIEKQLENGGSSSSERQTDRATAAMEPPSLFGSTKLQQDSPFSFHGNKAEDTSEKLEFTAEKKSDAAQGATSASFNFGKKIESSVLGSLSSGSLTGFSFSPGNSSLFGKDAAQSKAASSPFSAKASESQAGGSSSECRDGEEEESDEPPKVVVTEVKEEDAFYSKKCKLFYKKDNEFKEKGVGTLHLKPTATQKTQLLVRADTNLGNILLNVLIPPNMPCTRTGKNNVLIVCVPNPPLDEKQPTLPVTMLIRVKTSEDADELHKILLQKKDV
Protein: Poly(A) RNA polymerase cid11 (PAP) (EC 2.7.7.19) (Caffeine-induced death protein 11) (Polynucleotide adenylyltransferase cid11) (O74326)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MELLTFTCCPFEGQMQQKKRRFDANLVQLQESEHRNDQINETVDAELTNECWKLYMRLKPSNEEVSRRQQFVDKLRTILSTEIKDAKLDLFVFGSTENNLAIQQSDVDVCIITNGSKYLNSTCQLAQLLYSYGMKQIVCVSRARVPIVKIWDPQFDIHCDLNINNDVAKINTKMLRLFVSIDPRVRPLGLIIKYWAKQRALCDAAGSGTITSYTISCMLVNFLQTRNPPILPAMLDLMSNDDNKMFVDDIVGFKEKATLNKTSLGRLLIDFFYYYGFSFNYLDSVVSVRSGTVLNKQEKGWAMEVNNSLCVEEPFNTARNLANTADNPSVKGLQSEFQRAFRLMSENNACERLCKICEEYQFLDITNEANYGNTNTPFNTAYESFGCNHTVLPEAAAYPKPYYPPQITLSDGGNMNFLYYIPDESNHQSYENKANRDSDFQGQTSLTQGSAPPWHYIPCQSWLVWYPSEDASNPASGN
Protein: Mitochondrial import inner membrane translocase subunit Tim8 B (Deafness dystonia protein 2 homolog) (P62077)
Organism: Mus musculus (Mouse)
Function: Probable mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial import inner membrane translocase subunit Tim10
- Large ribosomal subunit protein mL53
- NADH dehydrogenase iron-sulfur protein 5
- Mitochondrial import receptor subunit TOM7 homolog
- Mitochondrial import inner membrane translocase subunit Tim9
- Small ribosomal subunit protein mS33
- NADH dehydrogenase 1 subunit C1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- Mitochondrial import inner membrane translocase subunit Tim10 B
Sequence:
MAELGEADEAELQRLVAAEQQKAQFTAQVHHFMELCWDKCVEKPGSRLDSRTENCLSSCVDRFIDTTLAITGRFAQIVQKGGQ
Protein: SWI5-dependent HO expression protein 3 (Q5ABV6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into the emerging bud (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Transcriptional regulatory protein ASH1
- Myosin 2
- 60S ribosomal subunit assembly/export protein LOC1
Sequence:
MTDTPNSPSKSTTKSASSSTKVIDSLHSKIDELTDELTALKQSHQELTKKHSITAKKNDSFVDQLANAKHENDMLSALLKRKERRILDLEDQFNELTSQNESLVLSNKNMKIRCENLQSNSNANIAEFERLKISYDALIASQMEYKNHYQQELNSLQTAFDNYKLENTRRFEELQTSIVSNDKDIDTLLDSLTNKRKAMDNIYVNKNNKVLQLLGNLAHLAKLHGQDTKSQVEQNVSVIEQLLAKHPDLQEKILEKEKIEVDLAEIIAHSNDVLANSSFDEDTTLINSPDLENNQNFNTTHSTSGSATPNSNSHSLQSKKRKNYKRNSLILKESPPIISENVPSSLPKKPQVNNNLINIPKARSKFNTPPTTPRQFTNHNNDFEVTHQWNGNNNINNHRRNNSVDSRSDNSQHRRNNSYDSRSDHGQHRRQPSQQNNNYNNNNYNNNNNNNNNNSNNGFVKRSGSVRNVNNYNNNNGNANNNGNNHGNKSKRRSTYNNNNNNNSKRNSQLFDNNFVLNV
Protein: Zinc finger HIT domain-containing protein 3 (Q7ZUF9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear FMR1-interacting protein 1.
- Mitochondrial rRNA methyltransferase 1 homolog
- Transcriptional adapter.
- Zinc finger HIT-type-containing 6.
- ATP-dependent RNA helicase
- Phosphatidylinositol-glycan biosynthesis class W protein
- Synergin, gamma.
- Tubulin-specific chaperone D
- Myosin XIX
- Gametogenetin-binding protein 2.
Sequence:
MQLCGVCSELVPKYRCPACRIRYCSVSCFKRHKEDDSCDPVKESDPASSKPAAVSNAEEPWTVEDLLDEDSQTDKVPLQRLQQLGDSEALKGLLRNPHLRQLMMSVDSAENKAKAMKDAMQEPLFVEFADQCLKIIEPSETDNNEDDDDEY
Protein: Ribosomal protein L19 (J3KTE4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLRLQKRLASSVLRCGKKKVWLDPNETNEIANANSRQQIRKLIKDGLIIRKPVTVHSRARCRKNTLARRKGRHMGIGKRKGTANARMPEKVTWMRRMRILRRLLRRYRESKKIDRHMYHSLYLKVKGNVFKNKRILMEHIHKLKADKARKKLLADQAEARRSKTKEARKRREERLQAKKEEIIKTLSKEEETKK
Protein: Myomesin 1 (A0A8I6GBP8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSLPFYQRSHQHYDLSYRNKDLHTTMSHYQQEKKRSAVYTHGSTAYSSRSSAAHRQESEALRQASAASYQQQASKAYSLGTSSSQHYQGSEVSRKTASSYDYGYSHGLTDSSLLLEDYSSRLSPQTKRAKRSLLSGEETGNLSGNYMVPIYSGRQVHISGIRDSEEERIKEAAAYIAQRTLLESEEAIMASKQSTASKQSTASKQSIASKQSTASKQSTASKQSTASKQATSTFQQEETFERKSRNISIREKAEELSLRKTLEETQAYHGKLNEDHLLHAPEFIIKPRSHTVWEKENVKLHCSVAGWPEPRLTWYKNQVPINVHANPEKYIIESRYGMHTLEISKCDFEDTAQYRASAMNVQGEVSAYASVVVKRYKGELDDSLLRGGVSMPLSFAVTPYGYASKFEIHFDDKFDVSFGREGETMSLGCRVVITPEIKHVQPEVQWYRNGAPVSPSKWVQPHWSGDRATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYVFVRDADAEIEGAPAAPLDVVSLDANKDYIIISWKQPAVDGGSPILGYFIDKCEVGTDTWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNKTGIGLPSRVSEPVAALDPAEKARLKSRPSAPWTGQIIVTEEEPTEGVIPGPPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCDVGTENWQRVNTELPVKSPRFALFDLVEGKSYRFRVRCSNSAGVGEPSESTEVTVVGDKLDIPKAPGKIIPSRNTDTSVVVSWEESKDAKELVGYYIESSVVGSGQWEPCNNNPVKGSRFTCHGLTTGQSYIFRVRAVNAAGLSEYSQDSEAIEVKAAIGGGVSPDVWPQLSDTPGGLTDSGGAMSGASPPTSQKDALPSSKPNKPSPPSSPSNRGQKEVSKVNGSVQEELSPPSMEVASKEQSKSGPPEKKKDPVAVPSPPYDITCLESFRDSMVLGWKQPDKTGGAEITGYYVNYREVVGGVPGKWREANIKAVSDAAYKISELKENTVYQFQVSAMNIAGLGAPSAVSECFKCEEWTIAVPGPPHSLKLSEVRKNSLVLQWKPPVYSGRTPVTGYFVDLKEASAKDDQWRGLNEAAIPNKYLRVQGLKEGISYVFRVRAINQAGVGKPSDLAGPVVAETRPGTKEVVVNVDDDGVISLNFECDQMTPKSEFVWSKDYVPSEDSPRLEVESKGNKTKMVFKDLGPDDLGTYSCDVTDTDGIASSYLIDEEEMKRLLALSQEHKFPTVPTKSELAVEILEKGQVRFWMQAEKLSGNAKVNYIFNEKEIFEGPKYKMHIDRNTGIIEMFMEKLQDEDEGTYTFQIQDGKATGHSTLVLIGDVYKKLQKEAEFQRQEWIRKQGPHFAEYLSWEVTGECNVLLKCKVANIKKETHIVWYKDEREISVDEKHDFKDGICTLLITEFSKKDAGFYEVILKDDRGKDKSRLKLVDEAFQDLMTEVCRKIALSATDLKIQSTAEGIRLYSFVCYYLDDLKVNWSHNGTGIKYTDRVKSGVTGEQIWLQINEPTQNDKGKYVMELFDGKTGHQKSVDLSGQAFDEAFAEFQRLKQAAIAEKNRARVLGGLPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKPLTSDDHCSLKFEAGKTAFFTISGVSTADSGKYGLVVKNKYGSETSDFTVSVFIPEEEARKGASEPPKGNQKSK
Protein: Serine/threonine-protein kinase PAK 5 (EC 2.7.11.1) (p21-activated kinase 5) (PAK-5) (p21-activated kinase 7) (PAK-7) (Q9P286)
Organism: Homo sapiens (Human)
Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.
Subcellular location: Mitochondrion. Cytoplasm. Nucleus. Note=Shuttles between the nucleus and the mitochondria, and mitochondrial localization is essential for the role in cell survival.
Interaction partners:
- Cell division control protein 42 homolog
- SH2/SH3 adapter protein NCK1
- Ras-related C3 botulinum toxin substrate 2
- Rho guanine nucleotide exchange factor 7
- Rho guanine nucleotide exchange factor 6
- Ras-related C3 botulinum toxin substrate 3
- Roundabout homolog 2
- Roundabout homolog 1
- LIM domain kinase 1
- Cytoplasmic protein NCK2
Sequence:
MFGKKKKKIEISGPSNFEHRVHTGFDPQEQKFTGLPQQWHSLLADTANRPKPMVDPSCITPIQLAPMKTIVRGNKPCKETSINGLLEDFDNISVTRSNSLRKESPPTPDQGASSHGPGHAEENGFITFSQYSSESDTTADYTTEKYREKSLYGDDLDPYYRGSHAAKQNGHVMKMKHGEAYYSEVKPLKSDFARFSADYHSHLDSLSKPSEYSDLKWEYQRASSSSPLDYSFQFTPSRTAGTSGCSKESLAYSESEWGPSLDDYDRRPKSSYLNQTSPQPTMRQRSRSGSGLQEPMMPFGASAFKTHPQGHSYNSYTYPRLSEPTMCIPKVDYDRAQMVLSPPLSGSDTYPRGPAKLPQSQSKSGYSSSSHQYPSGYHKATLYHHPSLQSSSQYISTASYLSSLSLSSSTYPPPSWGSSSDQQPSRVSHEQFRAALQLVVSPGDPREYLANFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHDNVVDMYSSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDSLPPRVKDLHKVSSVLRGFLDLMLVREPSQRATAQELLGHPFLKLAGPPSCIVPLMRQYRHH
Protein: Chitin-binding domain protein cbd-1 (O45599)
Organism: Caenorhabditis elegans
Function: In unfertilized oocytes, maintains egg-1 and egg-2 at the plasma membrane together with chitin synthase chs-1 and kinase mbk-2. Essential for the formation of a continuous and cohesive chitin layer following fertilization.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20971008}. Note=Localizes around oocytes in the proximal region of the germline. {ECO:0000269|PubMed:20971008}.
Interaction partners:
- Pumilio domain-containing protein 5
- Uncharacterized protein
- G2/mitotic-specific cyclin-B
- CCCH-type zinc finger protein oma-2
- Chondroitin proteoglycan 1
- Embryonic mRna
- LDL receptor repeat-containing protein egg-1
- Chondroitin proteoglycan 3
- Uncharacterized protein C05C10.5
- MEiotic SPindle
Sequence:
MGPQLATVSLLLLTFFSNSIQYPHSPAATECPAYFNGNIAGNACSREYSICVNGVRQAATCSDDSVFYEDECVPVDESPECRVDENTEEDDTPYAEFDCTSKQDGIYSIGCSNQFISCVAGGAYMAKCPDSLVFNERTQDCRESCDEVKQDTTTAPQVYEDGEEGYGEASGEIAGDYERQPSNEQPDSIDFDCNGLEDGNYADGCNDVFYSCSNNMVFQRYCPPGTVFNINQQSCDFQCTTDDPTTTVSYSTSTITTPQEDDSEYSSTTSADVISTTTTPSIDAIETTTTGFDAVTTTTTTQTPFVCQEGQVNSFGMCSSRFNRCQNNSVRSKQCPVNTLFESSLVMCVFDLPQCQPITVPAAPAYNSYGPPSDTIVSPFDENVRLKPKFDRRRKYHHGKPSYGPVNGNSYLENPFFIPRHRGGSHRDHRRYGYGPAIDSPFSTAFRGRAALSDQFKDYRRARMGKIQGDARKVDGNKRFLIDDEFEGPNAKFVESNIEQVFPKNRHSKKQLGPHEDPDGYDDEKTFDAKDLFGATRRKRSAYYGTEQSVYGQQSAQISARQAQVNKDCQQYTTPTFLTFGDCFDQFIFCSGNGINRMAACPIGETFDKTLRSCSETCGVSTTIVAVTIGTQTSDDLSAPSEYIENDGVTTQSTWNDQPSTTQAPNSYESYTTQYSSNDVPSTSAAPIGDRCSLDASGLFSLGCSQKYIQCSNGAAIVRRCGESLYFNEATQECTYRDEVPECGSQGSTSSPVITTPGQDQSSNYYGIPSDDVPSTTQTPVGDRCAYVASGLFDLGCSQKYIQCSDSAASVRECEGSLYFDERSQSCRFRDEVFKCQTADVSSSSTVPYLDFTTTPASPSEDEPTTYEPSVAPYIPSVTVNPVDTCTSLSDGTHGTGCSSFYFVCSHGRLISSGNCQLGEGYDPSVQGCRTFSEIPARACDEQEVTTDAGLVQLMPYKTLEEVLTTTEAATTVANDGPTDTYITGSTKYSTTDSGEYTIPYGDETTSTRSYDRADNDSEDEEEDDVEHDQKCTVGSRTPVGFCVRTYLECTDAGNVEKLCRIGKLFDSHSNRCVPRIGCGKEAIRDAIKDMIATTPAPAQPKQFEGRCAHVDGEAVFSIGVCSSKYLRCSYGASKLQQCSEDRVFSNDKLECIVRESVSACTVPKNPSIKKYYTSNDQSAFCDGKEDGLYRNERDCSAILQCFGGELFEHPSCQSSLAFNQLTGKCDYPQKVSGCENHGQTNGECSEHGSFIADANNCEVFYRCVWGRKVVMTCPSGTVFNPLLSVCDWPSAVPSCSGQASDSNSSYGSSTYNDDKSGY
Protein: RuBisCO chaperone RbcX (A0A0H3K9R3)
Organism: Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Function: An RbcL-specific chaperone. The central cleft of the RbcX homodimer (RbcX2) binds the C-terminus of an RbcL monomer, stabilizing the C-terminus and probably preventing its reassociation with chaperonin GroEL-ES. At the same time the peripheral region of RbcX2 binds a second RbcL monomer, bridging the RbcL homodimers in the correct orientation. The RbcX2(2)-bound RbcL dimers then assemble into the RbcL8 core (RbcL8-(RbcX2)8). RbcS binding triggers the release of RbcX2.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00855}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00855}. Note=Most protein is cytoplasmic, but some is in the carboxysome. This cyanobacterium makes beta-type carboxysomes (Probable). {ECO:0000255|HAMAP-Rule:MF_00855, ECO:0000305}.
Interaction partners:
Sequence:
MQFMGTASRMASTQRAKPMEMPRISRDTARMLVNYLTYQAVCVIRDQLAETNPAGAYRLQVFSAEFSFQDGEAYLAALLNHDRELGLRVMTVREHLAEHILDYLPEMTIAQIQEANINHRRALLERLTGLGAEPSLPETEVSDRPSDSATPDDASNASHAD
Protein: Myotilin (Myofibrillar titin-like Ig domains protein) (Titin immunoglobulin domain protein) (Q9JIF9)
Organism: Mus musculus (Mouse)
Function: Component of a complex of multiple actin cross-linking proteins. Involved in the control of myofibril assembly and stability at the Z lines in muscle cells (By similarity).
Subcellular location: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9UBF9}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UBF9}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q9UBF9}. Note=Sarcomeric, also localized to the sarcolemma. Colocalizes with MYOZ1 at the Z-lines in skeletal muscle. {ECO:0000250|UniProtKB:Q9UBF9}.
Interaction partners:
- Filamin-C
- Myozenin-1
- Alpha-actinin-2
- Telethonin
- LIM domain-binding protein 3
- Nebulin
- Alpha-actinin-3
- Troponin C, skeletal muscle
- Myozenin-2
- Actin, alpha skeletal muscle
Sequence:
MFNYERPKHFIQPQNPCGSRLQPPGPEVSGFPSQTKQSSIVIQPRQCTEQRFSASSTVSSHITVSSSAYPAPQQLAGPNPGQKVTATYNQSPASFLSSILPSQPDYCNSKIPSTVDSNYQQSSVNQPVNAMSSQAANARPTPKTPDHEIQGSKEALIQDLERKLKCKDTLLHNGNQRLTYEEKMARRLLGPQNAAAVFQAQNSDVQDSPQHNPEQARLHVPTSQVRSRSSSRAEANDQDAIQEKFYPPRFIQVPENMSIEEGRFCRMDFKVSGLPAPDVSWYLNGRPVQSDELHKMIVSEKGFHSLIFEVVRASDAGPYACVARNRAGEATFTVQLDVLAKEHKRAPMFIFKPQSKKVFEGETVKLECQISAIPPPKLFWKRNNEMVQFNTDRISLYHDNAGRVTLLIKDVNKKDAGWYTVSAVNEAGVTTCNTRLDVTARPIQTLPAPKQLRVRPTFSKYLALNGRGLDVKQAFNPEGEFQRLAAQSGLYESEEL
Protein: Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2) (Q99665)
Organism: Homo sapiens (Human)
Function: Receptor for interleukin-12. This subunit is the signaling component coupling to the JAK2/STAT4 pathway. Promotes the proliferation of T-cells as well as NK cells. Induces the promotion of T-cells towards the Th1 phenotype by strongly enhancing IFN-gamma production.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-12 receptor subunit beta-1
- Tyrosine-protein kinase JAK2
- Signal transducer and activator of transcription 4
- Interleukin-27 receptor subunit alpha
- Non-receptor tyrosine-protein kinase TYK2
- Interleukin-12 subunit alpha
- Interleukin-12 subunit beta
- Interferon gamma
- Interleukin-6
- Interleukin-10
Sequence:
MAHTFRGCSLAFMFIITWLLIKAKIDACKRGDVTVKPSHVILLGSTVNITCSLKPRQGCFHYSRRNKLILYKFDRRINFHHGHSLNSQVTGLPLGTTLFVCKLACINSDEIQICGAEIFVGVAPEQPQNLSCIQKGEQGTVACTWERGRDTHLYTEYTLQLSGPKNLTWQKQCKDIYCDYLDFGINLTPESPESNFTAKVTAVNSLGSSSSLPSTFTFLDIVRPLPPWDIRIKFQKASVSRCTLYWRDEGLVLLNRLRYRPSNSRLWNMVNVTKAKGRHDLLDLKPFTEYEFQISSKLHLYKGSWSDWSESLRAQTPEEEPTGMLDVWYMKRHIDYSRQQISLFWKNLSVSEARGKILHYQVTLQELTGGKAMTQNITGHTSWTTVIPRTGNWAVAVSAANSKGSSLPTRINIMNLCEAGLLAPRQVSANSEGMDNILVTWQPPRKDPSAVQEYVVEWRELHPGGDTQVPLNWLRSRPYNVSALISENIKSYICYEIRVYALSGDQGGCSSILGNSKHKAPLSGPHINAITEEKGSILISWNSIPVQEQMGCLLHYRIYWKERDSNSQPQLCEIPYRVSQNSHPINSLQPRVTYVLWMTALTAAGESSHGNEREFCLQGKANWMAFVAPSICIAIIMVGIFSTHYFQQKVFVLLAALRPQWCSREIPDPANSTCAKKYPIAEEKTQLPLDRLLIDWPTPEDPEPLVISEVLHQVTPVFRHPPCSNWPQREKGIQGHQASEKDMMHSASSPPPPRALQAESRQLVDLYKVLESRGSDPKPENPACPWTVLPAGDLPTHDGYLPSNIDDLPSHEAPLADSLEELEPQHISLSVFPSSSLHPLTFSCGDKLTLDQLKMRCDSLML
Protein: Desiccation-related protein At2g46140 (LEA type-2 family protein At2g46140) (O82355)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Late embryogenesis abundant
- Zinc finger
- F21J9.19
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Uncharacterized protein
- Late embryogenis abundant protein 2
- At2g17660 family protein)
- At2g23110
- Alpha/beta-Hydrolases superfamily protein
- Zinc finger A20 and AN1 domain-containing stress-associated protein 7
Sequence:
MASADEKVVEEKASVISSLLDKAKGFFAEKLANIPTPEATVDDVDFKGVTRDGVDYHAKVSVKNPYSQSIPICQISYILKSATRTIASGTIPDPGSLVGSGTTVLDVPVKVAYSIAVSLMKDMCTDWDIDYQLDIGLTFDIPVVGDITIPVSTQGEIKLPSLRDFF
Protein: Putative aldehyde dehydrogenase-like protein C21C3 (EC 1.2.1.-) (Q9P7K9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSSTLTCYCPGDGSLLGEVKLFNKSDIDQSIILAEEAQKEWKSTSFAERRNFLKALKENIIRNQDKYAEIACKDTGKTLVDAAFGEILVTLEKINWTLANGEQSLRPTKRPNSLLTSYKGGYVKYEPLGVIAALVSWNYPLHNALGPIISALFAGNAIVVKGSELTAWSTHQYCEMVRSLLQSMGHSPELVQCITCLPDVADHLTSHSGIKHITFIGSQPIAKLVAASAAKQLTPLCLELGGKDPCILTDDHRLEEILSIVMRGVFQSAGQNCIGIERIIALDGVYDTIITKLYNRISTMRLGMYTQNDVDMGAMVSNNRFDHLESLIQDAVSKGARLVYGGHRFQHPKYPKGNYFLPTLLVDATNEMKIAQEECFAPIALVFRAKSPEHALEIANGTEFGLGASVFGRDKQLCQYFTDNLETGMVAVNDFGAFYLLQMPFGGCKKSGYGRFAGYEGLRGICNSKAIAYDRFSAIHTGIPPAVDYPIPDSQKAWQFVRGLMGTVYGAWISLVPNVYQLWRNS
Protein: Multiple coagulation factor deficiency protein 2 (Neural stem cell-derived neuronal survival protein) (Q8NI22)
Organism: Homo sapiens (Human)
Function: The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:12717434}. Endoplasmic reticulum {ECO:0000269|PubMed:12717434}. Golgi apparatus {ECO:0000269|PubMed:12717434}.
Interaction partners:
- Protein ERGIC-53
- Coagulation factor VIII
- VIP36-like protein
- Vesicular integral-membrane protein VIP36
- Coagulation factor V
- Protein ERGIC-53-like
- Cathepsin Z
Sequence:
MTMRSLLRTPFLCGLLWAFCAPGARAEEPAASFSQPGSMGLDKNTVHDQEHIMEHLEGVINKPEAEMSPQELQLHYFKMHDYDGNNLLDGLELSTAITHVHKEEGSEQAPLMSEDELINIIDGVLRDDDKNNDGYIDYAEFAKSLQ
Protein: Transcriptional regulatory protein GlrR (P0AFU4)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system GlrR/GlrK that up-regulates transcription of the glmY sRNA when cells enter the stationary growth phase. Regulates glmY transcription by binding to three conserved sites in the purL-glmY intergenic region.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor histidine kinase GlrK
- Sensor protein QseC
- Uncharacterized protein YfhG
- RNA polymerase sigma-54 factor
- Transcriptional regulatory protein QseB
- Nitrogen regulatory protein P-II 1
Sequence:
MSHKPAHLLLVDDDPGLLKLLGLRLTSEGYSVVTAESGAEGLRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYQAIDDALEQSAPATDERWREAIVTRSPLMLRLLEQARLVAQSDVSVLINGQSGTGKEIFAQAIHNASPRNSKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFVEARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDANDFKE
Protein: RUN and SH3 domain containing 1 (Uncharacterized protein DKFZp761A1822) (Q68CX2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQAMLHFGGRLAQSLRGTSKEAASDPSDSPNLPTPGSWWEQLTQASRVYASGGTEGFPLSRWAPGRHGTAAEEGAQERPLPTDEMAPGRGLWLGRLFGVPGGPAENENGALKSRRPSSWLPPTVSVLALVKRGAPPEMPSPQELEASAPRMVQTHRAVRALCDHTAARPDQLSFRRGEVLRVITTVDEDWLRCGRDGMEGLVPVGYTSLVL
Protein: Transformer 2 alpha (A0A8J8Y9E0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSDVEENNFEGRESRSQSKSPTGTPARVKSESRSGSRSPSRVSKHSESHSRSRSKSRSRSRRHSHRRYTRSRSHSHRRRSRSRSYTPEYRRRRSRSHSPMSNRRRHTGSRANPDPNTCLGVFGLSLYTTERDLREVFSRYGPLSGVNVVYDQRTGRSRGFAFVYFERIDDSKEAMERANGMELDGRRIRVDYSITKRAHTPTPGIYMGRPTHGGGGGGGGGGGGGGGGGGRRRDSYYDRGYDRGYDRYEDYDYRYRRSPSPYYSRYRSRSRSRSYSPRRY