wanglab/gogpt-training-data huggingface dataset:
Protein: Mitochondrial import inner membrane translocase subunit TIM16 (Presequence translocated-associated motor subunit PAM16) (P42949)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14981506, ECO:0000269|PubMed:14981507}; Peripheral membrane protein {ECO:0000269|PubMed:14981506, ECO:0000269|PubMed:14981507}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM14
- Mitochondrial import inner membrane translocase subunit TIM44
- Mitochondrial import inner membrane translocase subunit TIM17
- Mitochondrial import inner membrane translocase subunit TIM50
- GrpE protein homolog
- Import motor subunit, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM21
- Presequence translocated-associated motor subunit PAM17
- Mitochondrial import inner membrane translocase subunit TIM23
- Mitochondrial DnaJ homolog 2
Sequence:
MAHRAFIQVIITGTQVFGKAFAEAYRQAASQSVKQGATNASRRGTGKGEYGGITLDESCKILNIEESKGDLNMDKINNRFNYLFEVNDKEKGGSFYLQSKVYRAAERLKWELAQREKNAKAKAGDASTAKPPPNSTNSSGADNSASSNQ
Protein: Serine/threonine-protein kinase RHS3 (EC 2.7.11.1) (AGC serine/threonine-protein kinase subfamily 1 member 6) (Protein ROOT HAIR SPECIFIC 3) (F4I4F2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in root hair growth and morphogenesis.
Interaction partners:
- Protein DETOXIFICATION 31
- Probable protein kinase At2g41970
- Probable LRR receptor-like serine/threonine-protein kinase At1g51880
- Probable LRR receptor-like serine/threonine-protein kinase At4g31250
- DNA-binding protein RHL1
- Protein ROH1A
- B3 domain-containing protein At1g16640
- U-box domain-containing protein 52
- Proline-rich receptor-like protein kinase PERK13
- COBRA-like protein 9
Sequence:
MLLKPGNKLVSPETSHHRDSASNSSNHKCQQQKPRKDKQKQVEQNTKKIEEHQIKSESTLLISNHNVNMSSQSNNSESTSTNNSSKPHTGGDIRWDAVNSLKSRGIKLGISDFRVLKRLGYGDIGSVYLVELKGANPTTYFAMKVMDKASLVSRNKLLRAQTEREILSQLDHPFLPTLYSHFETDKFYCLVMEFCSGGNLYSLRQKQPNKCFTEDAARFFASEVLLALEYLHMLGIVYRDLKPENVLVRDDGHIMLSDFDLSLRCSVNPTLVKSFNGGGTTGIIDDNAAVQGCYQPSAFFPRMLQSSKKNRKSKSDFDGSLPELMAEPTNVKSMSFVGTHEYLAPEIIKNEGHGSAVDWWTFGIFIYELLHGATPFKGQGNKATLYNVIGQPLRFPEYSQVSSTAKDLIKGLLVKEPQNRIAYKRGATEIKQHPFFEGVNWALIRGETPPHLPEPVDFSCYVKKEKESLPPAATEKKSKMFDEANKSGSDPDYIVFEYF
Protein: Syncrip, isoform H (A8JR54)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNKFEMAEGNGELLDDINQKADDRGDGERTEDYPKLLEYGLDKKVAGKLDEIYKTGKLAHAELDERALDALKEFPVDGALNVLGQFLESNLEHVSNKSAYLCGVMKTYRQKSRASQQGVAAPATVKGPDEDKIKKILERTGYTLDVTTGQRKYGGPPPHWEGNVPGNGCEVFCGKIPKDMYEDELIPLFENCGIIWDLRLMMDPMTGTNRGYAFVTFTNREAAVNAVRQLDNHEIKPGKCLKINISVPNLRLFVGNIPKSKGKDEILEEFGKLTAGLYEVIIYSSPDDKKKNRGFCFLEYESHKAASLAKRRLGTGRIKVWGCDIIVDWADPQEEPDEQTMSKVKVLYVRNLTQDVSEDKLKEQFEQYGKVERVKKIKDYAFIHFEDRDSAVEAMRGLNGKEIGASNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGNLSPTHPSIMSLTPMRPGARMPLRTPIPREYVVGKRKFDGGHQNPADVKRRYPSGLIGNGGSWGSLPLPQQPLGTNGEQWYMDTFSAWS
Protein: Parvalbumin beta (Parvalbumin II) (Parvalbumin pI 4.10) (Parvalbumin-2) (P02619)
Organism: Esox lucius (Northern pike)
Function: In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
Interaction partners:
Sequence:
SFAGLKDADVAAALAACSAADSFKHKEFFAKVGLASKSLDDVKKAFYVIDQDKSGFIEEDELKLFLQNFSPSARALTDAETKAFLADGDKDGDGMIGVDEFAAMIKA
Protein: Mucin family signaling protein Msb2, putative (AFU_orthologue AFUA_4G04070) (Q5AXD9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MVSQTALIAAALSLAGLELVAAQQPNAHHEHKQLKRQLFGSSDQSNNLGWLESFLSSNSDSGTTSSTTTSQNSGVTAASSKDSDPDVVIVPITLSVDENGKTHTITGTANTGVATGAASTTTKQSTVAEVTASATTESQPTATSTSSSTREDTDLSGILGSLLGGSSSSDSSASTTQTGISRAATDSTISETETTDSSTSPSSTSSSGGLLESLLGGSDSSASTSTSSTTSSSTSTSDGLLGLNLNLNGDSTSSTSTTTGSSPSATSTSSSNGLLENLLGDSTSTSTSTSTADSSSATSTSSSGGLLDGLLGGDSTSSSGTTTATSPSATSTSGGLLDGLFGTDSTSSSATTSVTTPTSTSGGLLGGLFGTDSSSSASTAVIPSSTSTSSGGFLDSLFGTDSSTPTPLPGASSTSGGLIGNILPTISVSVPESTPTGSSDAVASSTPTLLPPDLTSILIPSSSSGATSVPVIPQVPTSSVAATPTPSVGISVPSSSSVSVQPAPTTTSTASSEDSTTTVGTTTTTTVEAEPTDWVPTSIIIEPSPTETETSSEETTTVAPTQLPGSISPAGGVPDAPEGSTLIQLGFTRELRYSFVATHSLSSSQIFLYIPQGLMYALEEASSDIAMFAISPYDSEATTGYIATVAQAYIPTEKVDVLRKLLHNPISRLYDQPSESVKTLMSMIDPSIPLLVGEYDDSSFGGSSGSGDGSGSDGDGDDSNDTYDDSTAGASSSGSTKASSVGIGVGVVAGAAAYGAGMFWVARRYRKKRQLHRRTSSTADQMSDRGGSIFAGGGRLSRGSGSQRTQMISAPVMAENSLGWN
Protein: Protein F37C4.5 (O44400)
Organism: Caenorhabditis elegans
Interaction partners:
- Hypersensitive to pore-forming toxin protein 40
- Non-specific serine/threonine protein kinase
- Integrin Cytoplasmic domain-Associated Protein homolog
- Putative 6-phosphogluconolactonase
- Protein simr-1
Sequence:
MAHIVQTHKLTLHDVAIDQALVYSSDSNCAELKRTFQVELAHGYNEVKVQNLPFDLVQDSIRVSGAGEAVIHDVSVKNQEGAEFVIPERVLAIKAIFEEKERAKDKVADSRVAVQKRIEGLDNLITEVAKHGKDGAFHFDGRTIESLNALHGFHQDTTVDLRAQIRTLDQDLRKAEEEYARASQDYDNTGYRWRNSAQYASIIVESEAGGAAQLTITYQVNNVSWTPFYDIRVTAGVEAEMHVTYFGKVRQYSGEDWKTVPLVLSTARPAHGVKQLPKLGALEASIVVPEPECNRGGRGGYGGGYAQDSVVMACAAPMMEMGRSRKSMKMSYAAVKSSNIASEFSIGRPATIDDRTDEYKVNIGQFTLDTKLSNVTVPSRNATAFLVANSVNTSDYPLVAGQASIFLDGAFVNKTEFEDAVVSQKFEVSLGVDPNIRIEYKPVRNYQEQSGTVEKINSQVTEKTTAVTNLRPNSVLLTIREQLPRSTDSRIKVHLNTPEAVEVDEASVEPTVGAAITPEKILDYTVQLAPGQSSTFVVKYTTEHPQAEQIRYEEKF
Protein: Protein jagged-2 (Jagged2) (P97607)
Organism: Rattus norvegicus (Rat)
Function: Putative Notch ligand involved in the mediation of Notch signaling. May have a role in neurogenesis in the peripheral nervous system, limb development and in the adult brain.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Notch homolog 4, isoform CRA_b.
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 2
- Protein jagged-1
- Recombining binding protein suppressor of hairless
- Transcription factor HES-1
- Mastermind-like transcriptional coactivator 1
- Hairy/enhancer-of-split related with YRPW motif 1.
- Mastermind-like transcriptional coactivator 2
Sequence:
GACCDGDGRTTRAGGCGRDECDTYVRVCLKEYQAKVTPTGPCSYGYGATPVLGSNSFYLPPAGAAGDRARARSRTGGHQDPGLVVIPFQFAWPRSFTLIVEAWDWDNDTTPDEELLIERVSHAGMINPEDRWKSLHFSGHVAHLELQIRVRCDENYYSATCNKFCRPRNDFFGHYTCDQYGNKACMDGWMGKECKEAVCKQGCNLLHGGCTVPGECRCSYGWQGKFCDECVPYPGCVHGSCVEPWHCDCETNWGGLLCDKDLNYCGSHHPCVNGGTCINAEPDQYLCACPDGYLGKNCERAEHACASNPCANGGSCHEVLSGFECHCPSGWSGPTCALDIDECASNPCAAGGTCVDQVDGFECICPEQWVGATCQLDANECEGKPCLNAFSCKNLIGGYYCDCLPGWKGANCHININDCHGQCQHGGTCKDLVNGYQCVCPRGFGGRHCELEYYKCASSPCRRGGICEDLVDGFRCHCPRGLSGPLCEVDVDLWCEPNPCLNGARCYNLEDDYYCACPEDFGGKNCSVPRETCPGGACRVIDGCGFEAGSRAHGAAPSGVCGPHGHCVSLPGGNFSCICDSGFTGTYCHENIDDCMGQPCRNGGTCIDEVDSFACFCPSGWEGELCDINPNDCLPDPCHSRGRCYDLVNDFYCVCDDGWKDKTCHSREFQCDAYTCSNGGTCYDSGDTFRCACPPGWKGSTCTIAKNSSCVPNPCVNGGTCVGSGDSFSCICRDGWEGRTCTHNTNDCNPLPCYNGGICVDGVNWFRCECAPGFAGPDCRINIDECQSSPCAYGATCVDEINGYRCSCPPGRSGPRCQEVVIFTRPCWSRGVSFPHGSSWVEDCNSCRCLDGHRDCSKVWCGWKPCLLSPQPSALSAQCPPGQQCREKAMGQCLQPPCENWGECTAEDPLPPSTPCLPRTTHLDNNCARLTLHFNRDQVPQGTTVGAICSGIRALPATRAAARDRLLLLLCDRASSGASAVEVAVSFSPARDLPDSSLIQSTAHAIVAAITQRGNSSLLLAVTEVKVETVVMGGSSTGLLVPVLCSVFSVLWLACMVICVWWTRKRRKERERSRLPRDESANNQWAPLNPIRNPIERPGSSGLGTGGHKDVLYQCKNFTPPPRRAGEALPGPASHGAGGEDEEDEELSRGDGRLSRSREVPLTQIHQRPQLLPGKASLLAPGPKVDNRAVRSTKDVRCAGRE
Protein: Proteasome subunit beta (Q38AZ8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit beta
- Proteasome subunit beta
- Proteasome subunit beta
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit beta
- Proteasome subunit beta
Sequence:
MLADFESVLRSEFSLKDCPRIGPFTWHNIPGVNDAAEDGSALGLNNPLGVSADRTDDFSVMPYSGEELTRDPLCTSNCINSDRRIWKLMLPCPVPRSVPKLDMKKGTTTLGFHFDGGIIIAVDSRASSGQYISSQTVMKVLEINEYLLGTMAGGAADCQYWERVLGMECRLWELRNNCRISVAAASKILANITYQYRNHGLSMGTMVAGWDQFGPSLYYVDDKGTRVKHEIFSVGSGSIYAYGVLDQGYRKNLTVEEACDLARRSIFHATYRDGASGGIVTVYHVHPKGWTQISRDDQTKLYDRYSSQSA
Protein: Calsequestrin (F6P0J3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004564}.
Interaction partners:
- Ryanodine receptor 2b
- Si:ch211-199i15.5.
- Ryanodine receptor 1a
- Ryanodine receptor 3.
- Ryanodine receptor 1b
- Aspartyl/asparaginyl beta-hydroxylase isoform X3
- Triadin.
- Uncharacterized protein.
- Calsequestrin
- Calsequestrin
Sequence:
MKWRWVIWGVLLSLGYQCWSETGLDFPEYDGKDRVHQLTAKNYKSVMKKYDVMVIYLHKPVGEDRMARKQFEVEELALELLTSPAALTYQLAAQVLDGLDDEDIGFGLVDSKKDRAVAKKLGMLEVDSIYIFADDEIIEYDGALAADTLLEFLYDVIEDPVEIISNDRELKGFHNIEEDMKLMGFFKSNKSPYFIEYDDAAEEFHPFIKFFATFEPKIAKKLNLKMNEVDFYEPFMDKPVTIPGKPYMEDDIINFIEDHDRPTLRKLEPHSMYEIWEDDINGQHIVAFAEESDPDGYEFLEILKEVAQENTENPELSIIWIDPDDFPLMVPYWEKTFGIDLSSPQIGVVDVENADSVWMEMDDEEHMPTADQLDAWIEDVMTGNINPNDENQYHDDDDEDDDDHDDEDDDDHDDDDDDEDEDHDDDDDDEDLDDDDDEDLDEDDDDDEDHDDDD
Protein: Envelope glycoprotein M (gM) (F5HDD0)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04035}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04035}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}. Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04035, ECO:0000269|PubMed:12771417}. Note=During virion morphogenesis, this protein accumulates in the trans-Golgi network where secondary envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04035}.
Interaction partners:
Sequence:
MRASKSDRFLMSSWVKLLFVAVIMYICSAVVPMAATYEGLGFPCYFNNLVNYSALNLTVRNSAKHLTPTLFLEKPEMLVYIFWTFIVDGIAIVYYCLAAVAVYRAKHVHATTMMSMQSWIALLGSHSVLYVAILRMWSMQLFIHVLSYKHVLMAAFVYCIHFCISFAHIQSLITCNSAQWEIPLLEQHVPDNTMMESLLTRWKPVCVNLYLSTTALEMLLFSLSTMMAVGNSFYVLVSDAIFGAVNMFLALTVVWYINTEFFLVKFMRRQVGFYVGVFVGYLILLLPVIRYENAFVQANLHYIVAINISCIPILCILAIVIRVIRSDWGLCTPSAAYMPLATSAPTVDRTPTVHQKPPPLPAKTRARAKVKDISTPAPRTQYQSDHESDSEIDETQMIFI
Protein: Secretory carrier-associated membrane protein 5 (Secretory carrier membrane protein 5) (hSCAMP5) (Q8TAC9)
Organism: Homo sapiens (Human)
Function: Required for the calcium-dependent exocytosis of signal sequence-containing cytokines such as CCL5. Probably acts in cooperation with the SNARE machinery. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT) in case of endoplasmic reticulum stress by inhibiting the endocytosis pathway.
Subcellular location: Cell membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Mainly localizes in Golgi apparatus membrane. Upon calcium-triggered exocytosis, it translocates to the cell membrane. Highly enriched in synaptic vesicles (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MAEKVNNFPPLPKFIPLKPCFYQDFEADIPPQHVSMTKRLYYLWMLNSVTLAVNLVGCLAWLIGGGGATNFGLAFLWLILFTPCSYVCWFRPIYKAFKTDSSFSFMAFFFTFMAQLVISIIQAVGIPGWGVCGWIATISFFGTNIGSAVVMLIPTVMFTVMAVFSFIALSMVHKFYRGSGGSFSKAQEEWTTGAWKNPHVQQAAQNAAMGAAQGAMNQPQTQYSATPNYTYSNEM
Protein: tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) (P25745)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs.
Subcellular location: Cytoplasm.
Interaction partners:
- Sulfurtransferase TusE
- High frequency lysogenization protein HflD
- tRNA modification GTPase MnmE
- tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG
- Cysteine desulfurase IscS
- Sulfur carrier protein TusA
- Sulfurtransferase TusD
- tRNA sulfurtransferase
- Adenylosuccinate lyase
- tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC
Sequence:
MSETAKKVIVGMSGGVDSSVSAWLLQQQGYQVEGLFMKNWEEDDGEEYCTAAADLADAQAVCDKLGIELHTVNFAAEYWDNVFELFLAEYKAGRTPNPDILCNKEIKFKAFLEFAAEDLGADYIATGHYVRRADVDGKSRLLRGLDSNKDQSYFLYTLSHEQIAQSLFPVGELEKPQVRKIAEDLGLVTAKKKDSTGICFIGERKFREFLGRYLPAQPGKIITVDGDEIGEHQGLMYHTLGQRKGLGIGGTKEGTEEPWYVVDKDVENNILVVAQGHEHPRLMSVGLIAQQLHWVDREPFTGTMRCTVKTRYRQTDIPCTVKALDDDRIEVIFDEPVAAVTPGQSAVFYNGEVCLGGGIIEQRLPLPV
Protein: Bisphosphoglycerate mutase (BPGM) (EC 5.4.2.4) (2,3-bisphosphoglycerate mutase, erythrocyte) (2,3-bisphosphoglycerate synthase) (EC 5.4.2.11) (2,3-diphosphoglycerate mutase) (DPGM) (BPG-dependent PGAM) (P07738)
Organism: Homo sapiens (Human)
Function: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity.
Interaction partners:
- Phosphoglycerate kinase 1
- Phosphoglycerate kinase 2
- Beta-enolase
- Alpha-enolase
- Gamma-enolase
- Phosphoglycerate mutase 2
- Phosphoglycerate mutase 1
- Glyceraldehyde-3-phosphate dehydrogenase
- Enolase 4
- Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
Sequence:
MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVLNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYNVTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRGKTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEAIQAAIKKVEDQGKVKQAKK
Protein: Gamma-aminobutyric acid receptor-associated protein (GABA(A) receptor-associated protein) (MM46) (O95166)
Organism: Homo sapiens (Human)
Function: Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in autophagy: while LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. Also required for the local activation of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, regulating ubiquitination and degradation of TIAM1, a guanyl-nucleotide exchange factor (GEF) that activates RAC1 and downstream signal transduction. Thereby, regulates different biological processes including the organization of the cytoskeleton, cell migration and proliferation. Involved in apoptosis.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19056683}. Endomembrane system {ECO:0000250|UniProtKB:P60517}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60517}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P60517}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P60517}. Note=Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae. Colocalizes with microtubules (By similarity). Also localizes to discrete punctae along the ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:P60517, ECO:0000250|UniProtKB:Q9DCD6}.
Interaction partners:
- Optineurin
- Ubiquitin-like-conjugating enzyme ATG3
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
- Cysteine protease ATG4B
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
- FUN14 domain-containing protein 1
- Sequestosome-1
- Ubiquitin-like modifier-activating enzyme ATG7
- Next to BRCA1 gene 1 protein
- Reticulophagy regulator 1
Sequence:
MKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYGL
Protein: Transcription factor (A0A8I5ZNQ2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR009404, ECO:0000256|RuleBase:RU003796}.
Interaction partners:
Sequence:
ITPQRITNSGSVLIGSPYTPAPAMVTQTHIAEAAGWVPSDRKRAREFIDSDFSESKRSKKGDKNGKGLRHFSMKVCEKVQRKGTTSYNEVADELVSEFTNASNHLAADSAYDQKNIRRRVYDALNVLMAMNIISKEKKEIKWIGLPTNSAQECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNQGPPAVNSTIQLPFIVINTSRKTVIDCSISSDKFEYLFNFDNTFEIHDDIEVLKRMGMSFGLESGKCSLEDLKIAKSLVPKALEGYITDVSTGPSWLNQGLLLNSTQSVSNLDPTTGATVPQSSVNQGLCLDAEVALATGQFLAPNSHQSSTAASQFSESRGETPCSFNDEEEEDEEEDPSSPE
Protein: Sulfopyruvate decarboxylase subunit beta (EC 4.1.1.79) (Q6LWM0)
Organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
Function: Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde.
Interaction partners:
- Sulfopyruvate decarboxylase subunit alpha
- L-sulfolactate dehydrogenase/
- 2-phosphosulfolactate phosphatase
- Similar to phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
- Methyl-coenzyme M reductase operon protein C
- Conserved archaeal protein
Sequence:
MELTRYEIIKILMEYVTDEIVVCNIGIPSKELFKINDREKNFYMLGSMGLSSSIGHGLALSVNEKVIAIDGDGSVLMNMGSLATIGKTTPKDFLLLIVDNCAYGSTGNQETHSTCTDLYQVSKACGIDSIGVFNEEQLRDAVKLALSESGTKVIVAKARPHNENVPNINLVPTEIKHRFMNAIKK
Protein: Chaperone protein FimC (P31697)
Organism: Escherichia coli (strain K12)
Function: Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH.
Subcellular location: Periplasm.
Interaction partners:
- Type-1 fimbrial protein, A chain
- Protein FimF
- Protein FimG
- Type 1 fimbrin D-mannose specific adhesin
- Outer membrane usher protein FimD
- Fimbrin-like protein FimI
- Uncharacterized fimbrial-like protein SfmH
- Uncharacterized fimbrial-like protein SfmF
- Uncharacterized fimbrial-like protein SfmA
- Probable autotransporter YfaL
Sequence:
MSNKNVNVRKSQEITFCLLAGILMFMAMMVAGRAEAGVALGATRVIYPAGQKQEQLAVTNNDENSTYLIQSWVENADGVKDGRFIVTPPLFAMKGKKENTLRILDATNNQLPQDRESLFWMNVKAIPSMDKSKLTENTLQLAIISRIKLYYRPAKLALPPDQAAEKLRFRRSANSLTLINPTPYYLTVTELNAGTRVLENALVPPMGESTVKLPSDAGSNITYRTINDYGALTPKMTGVME
Protein: Neurexophilin (G3X9N5)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Neurexin-1
- Neurexin-2
- Neurexin-3
Sequence:
MRLLPEWLLLLFGPWLLRKAVCGQIVESGRPQYLDLRPAMAGGGARGQQLPAPASSEGLGMARSWSWAWPANHTGALAKPGTAGGPSVPRTKRKPSIKAARAKKIFGWGDFYFRVHTLKFSLLVTGKIVDHVNGTFSVYFRHNSSSLGNLSVSIVPPSKRVEFGGVWLPGPASHPLQSTLALEGVLPGLGPPLGMAGQGLGSNLGGALAGPLGSALGVPGAKESRAFNCHVEYEKTNRARKHRPCLYDPSQVCFTEHTQSQAAWLCAKPFKVICIFVSFLSFDYKLVQKVCPDYNFQSEHPYFG
Protein: Piwi-like 4 (Drosophila), isoform CRA_a (Testis tissue sperm-binding protein Li 85P) (A0A140VKG8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGRARVKARGIARSPSATEVGRIQASPLPRSVDLSNNEASSSNGFLGTSRISTNDKYGISSGDAGSTFMERGVKNKQDFMDLSICTREKLAHVRNCKTGSSGIPVKLVTNLFNLDFPQDWQLYQYHVTYIPDLASRRLRIALLYSHSELSNKAKAFDGAILFLSQKLEEKVTELSSETQRGETIKMTITLKRELPSSSPVCIQVFNIIFRKILKKLSMYQIGRNFYNPSEPMEIPQHKLSLWPGFAISVSYFERKLLFSADVSYKVLRNETVLEFMTALCQRTGLSCFTQTCEKQLIGLIVLTRYNNRTYSIDDIDWSVKPTHTFQKRDGTEITYVDYYKQQYDITVSDLNQPMLVSLLKKKRNDNSEAQLAHLIPELCFLTGLTDQATSDFQLMKAVAEKTRLSPSGRQQRLARLVDNIQRNTNARFELETWGLHFGSQISLTGRIVPSEKILMQDHICQPVSAADWSKDIRTCKILNAQSLNTWLILCSDRTEYVAESFLNCLRRVAGSMGFNVDYPKIIKVQENPAAFVRAIQQYVDPDVQLVMCILPSNQKTYYDSIKKYLSSDCPVPSQCVLARTLNKQGMMMSIATKIAMQMTCKLGGELWAVEIPLKSLMVVGIDVCKDALSKDVMVVGCVASVNPRITRWFSRCILQRTMTDVADCLKVFMTGALNKWYKYNHDLPARIIVYRAGVGDGQLKTLIEYEVPQLLSSVAESSSNTSSRLSVIVVRKKCMPRFFTEMNRTVQNPPLGTVVDSEATRNEWYDFYLISQVACRGTVSPTYYNVIYDDNGLKPDHMQRLTFKLCHLYYNWPGIVSVPAPCQYAHKLTFLVAQSIHKEPSLELANHLFYL
Protein: Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB) (Q66T47)
Organism: Sus scrofa (Pig)
Function: Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Growth/differentiation factor 8
- Growth/differentiation factor 11
- Inhibin beta A chain
- Bone morphogenetic protein 4
- Serine/threonine-protein kinase receptor
- Inhibin beta B chain
- Bone morphogenetic protein 2
- receptor protein serine/threonine kinase
- Mothers against decapentaplegic homolog
- Growth/differentiation factor 7
Sequence:
MTAPWAALALLWGSLCVGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEAGGPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRNAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEELQEVVVHKKMRPAIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSLIRRSVNGTTSDCLVSLVTSVTNVDLPPKESSI