wanglab/gogpt-training-data huggingface dataset:
Protein: Activin receptor type-1B (EC 2.7.11.30) (Activin receptor type IB) (ACTR-IB) (Activin receptor-like kinase 4) (ALK-4) (Serine/threonine-protein kinase receptor R2) (SKR2) (Q61271)
Organism: Mus musculus (Mouse)
Function: Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a 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, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas 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 such as ACVR1B. 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. ACVR1B also phosphorylates TDP2.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Activin receptor type-2B
- Growth/differentiation factor 8
- Activin receptor type-2A
- Inhibin beta A chain
- Growth/differentiation factor 11
- Mothers against decapentaplegic homolog 2
- Activin receptor type-1C
- Mothers against decapentaplegic homolog 3
- Nodal
- Activin receptor type-1
Sequence:
MAESAGASSFFPLVVLLLAGSGGSGPRGIQALLCACTSCLQTNYTCETDGACMVSIFNLDGVEHHVRTCIPKVELVPAGKPFYCLSSEDLRNTHCCYIDFCNKIDLRVPSGHLKEPAHPSMWGPVELVGIIAGPVFLLFLIIIIVFLVINYHQRVYHNRQRLDMEDPSCEMCLSKDKTLQDLVYDLSTSGSGSGLPLFVQRTVARTIVLQEIIGKGRFGEVWRGRWRGGDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTIEGMIKLALSAASGLAHLHMEIVGTQGKPGIAHRDLKSKNILVKKNGMCAIADLGLAVRHDAVTDTIDIAPNQRVGTKRYMAPEVLDETINMKHFDSFKCADIYALGLVYWEIARRCNSGGVHEDYQLPYYDLVPSDPSIEEMRKVVCDQKLRPNVPNWWQSYEALRVMGKMMRECWYANGAARLTALRIKKTLSQLSVQEDVKI
Protein: Adenylosuccinate synthetase (AMPSase) (AdSS) (EC 6.3.4.4) (IMP--aspartate ligase) (P65887)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00011}.
Interaction partners:
Sequence:
MTSVVVVGTQWGDEGKGKITDFLSANAEVIARYQGGDNAGHTIVIDGKKFKLHLIPSGIFFPEKISVIGNGMVVNPKSLVKELSYLHEEGVTTDNLRISDRAHVILPYHIELDRLQEEAKGDNKIGTTIKGIGPAYMDKAARVGIRIADLLDKDIFRERLERNLAEKNRLFEKLYDSKAIVFDDIFEEYYEYGQQIKKYVIDTSVILNDALDNGKRVLFEGAQGVMLDIDQGTYPFVTSSNPVAGGVTIGSGVGPSKIDKVVGVCKAYTSRVGDGPFPTELFDEVGERIREVGHEYGTTTGRPRRVGWFDSVVMRHSRRVSGITNLSLNSIDVLSGLDTVKICVAYDLDGQRIDYYPASLEQLKRCKPIYEELPGWSEDITGVRNLEDLPENARNYVRRVSELVGVRISTFSVGPGREQTNILESVWS
Protein: Cell division control protein 25 (P04821)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Promotes the exchange of Ras-bound GDP by GTP. This protein positively controls the level of cellular cAMP at start, the stage at which the yeast cell division cycle is triggered.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ras-like protein 2
- Ras-like protein 1
- Adenylate cyclase
- M-phase inducer phosphatase
- Inhibitory regulator protein IRA1
- cAMP-dependent protein kinase type 1
- Inhibitory regulator protein IRA2
- G protein-coupled receptor GPR1
- Negative regulator of sporulation MDS3
- Protein DSS4
Sequence:
MSDTNTSIPNTSSAREAGNASQTPSISSSSNTSTTTNTESSSASLSSSPSTSELTSIRPIGIVVAAYDFNYPIKKDSSSQLLSVQQGETIYILNKNSSGWWDGLVIDDSNGKVNRGWFPQNFGRPLRDSHLRKHSHPMKKYSSSKSSRRSSLNSLGNSAYLHVPRNPSKSRRGSSTLSASLSNAHNAETSSGHNNTVSMNNSPFSAPNDASHITPQSSNFNSNASLSQDMTKSADGSSEMNTNAIMNNNETNLQTSGEKAGPPLVAEETIKILPLEEIEMIINGIRSNIASTWSPIPLITKTSDYKLVYYNKDLDIYCSELPLISNSIMESDDICDSEPKFPPNDHLVNLYTRDLRKNANIEDSSTRSKQSESEQNRSSLLMEKQDSKETDGNNNSINDDDNNNENNKNEFNEAGPSSLNSLSAPDLTQNIQSRVVAPSRSSILAKSDIFYHYSRDIKLWTELQDLTVYYTKTAHKMFLKENRLNFTKYFDLISDSIVFTQLGCRLMQHEIKAKSCSKEIKKIFKGLISSLSRISINSHLYFDSAFHRKKMDTMNDKDNDNQENNCSRTEGDDGKIEVDSVHDLVSVPLSGKRNVSTSTTDTLTPMRSSFSTVNENDMENFSVLGPRNSVNSVVTPRTSIQNSTLEDFSPSNKNFKSAKSIYEMVDVEFSKFLRHVQLLYFVLQSSVFSDDNTLPQLLPRFFKGSFSGGSWTNPFSTFITDEFGNATKNKAVTSNEVTASSSKNSSISRIPPKMADAIASASGYSANSETNSQIDLKASSAASGSVFTPFNRPSHNRTFSRARVSKRKKKYPLTVDTLNTMKKKSSQIFEKLNNATGEHLKIISKPKSRIRNLEINSSTYEQINQNVLLLEILENLDLSIFINLKNLIKTPSILLDLESEEFLVHAMSSVSSVLTEFFDIKQAFHDIVIRLIMTTQQTTLDDPYLFSSMRSNFPVGHHEPFKNISNTPLVKGPFHKKNEQLALSLFHVLVSQDVEFNNLEFLNNSDDFKDACEKYVEISNLACIIVDQLIEERENLLNYAARMMKNNLTAELLKGEQEKWFDIYSEDYSDDDSENDEAIIDDELGSEDYIERKAANIEKNLPWFLTSDYETSLVYDSRGKIRGGTKEALIEHLTSHELVDAAFNVTMLITFRSILTTREFFYALIYRYNLYPPEGLSYDDYNIWIEKKSNPIKCRVVNIMRTFLTQYWTRNYYEPGIPLILNFAKMVVSEKIPGAEDLLQKINEKLINENEKEPVDPKQQDSVSAVVQTTKRDNKSPIHMSSSSLPSSASSAFFRLKKLKLLDIDPYTYATQLTVLEHDLYLRITMFECLDRAWGTKYCNMGGSPNITKFIANANTLTNFVSHTIVKQADVKTRSKLTQYFVTVAQHCKELNNFSSMTAIVSALYSSPIYRLKKTWDLVSTESKDLLKNLNNLMDSKRNFVKYRELLRSVTDVACVPFFGVYLSDLTFTFVGNPDFLHNSTNIINFSKRTKIANIVEEIISFKRFHYKLKRLDDIQTVIEASLENVPHIEKQYQLSLQVEPRSGNTKGSTHASSASGTKTAKFLSEFTDDKNGNFLKLGKKKPPSRLFR
Protein: Chimeric ERCC6-PGBD3 protein (Chimeric CSB-PGBD3 protein) (P0DP91)
Organism: Homo sapiens (Human)
Function: Involved in repair of DNA damage following UV irradiation, acting either in the absence of ERCC6 or synergistically with ERCC6. Involved in the regulation of gene expression. In the absence of ERCC6, induces the expression of genes characteristic of interferon-like antiviral responses. This response is almost completely suppressed in the presence of ERCC6. In the presence of ERCC6, regulates the expression of genes involved in metabolism regulation, including IGFBP5 and IGFBP7. In vitro binds to PGBD3-related transposable elements, called MER85s; these non-autonomous 140 bp elements are characterized by the presence of PGBD3 terminal inverted repeats and the absence of internal transposase ORF.
Subcellular location: Nucleus {ECO:0000269|PubMed:26218421}.
Interaction partners:
Sequence:
MPNEGIPHSSQTQEQDCLQSQPVSNNEEMAIKQESGGDGEVEEYLSFRSVGDGLSTSAVGCASAAPRRGPALLHIDRHQIQAVEPSAQALELQGLGVDVYDQDVLEQGVLQQVDNAIHEASRASQLVDVEKEYRSVLDDLTSCTTSLRQINKIIEQLSPQAATSRDINRKLDSVKRQKYNKEQQLKKITAKQKHLQAILGGAEVKIELDHASLEEDAEPGPSSLGSMLMPVQETAWEELIRTGQMTPFGTQIPQKQEKKPRKIMLNEASGFEKYLADQAKLSFERKKQGCNKRAARKAPAPVTPPAPVQNKNKPNKKARVLSKKEERLKKHIKKLQKRALQFQGKVGLPKARRPWESDMRPEAEGDSEGEESEYFPTEEEEEEEDDEVEGAEADLSGDGTDYELKPLPKGGKRQKKVPVQEIDDDFFPSSGEEAEAASVGEGGGGGRKVGRYRDDGDEDYYKQRLSPKMPRTLSLHEITDLLETDDSIEASAIVIQPPENATAPVSDEESGDEEGGTINNLPGSLLHTAAYLIQDGSDAESDSDDPSYAPKDDSPDEVPSTFTVQQPPPSRRRKMTKILCKWKKADLTVQPVAGRVTAPPNDFFTVMRTPTEILELFLDDEVIELIVKYSNLYACSKGVHLGLTSSEFKCFLGIIFLSGYVSVPRRRMFWEQRTDVHNVLVSAAMRRDRFETIFSNLHVADNANLDPVDKFSKLRPLISKLNERCMKFVPNETYFSFDEFMVPYFGRHGCKQFIRGKPIRFGYKFWCGATCLGYICWFQPYQGKNPNTKHEEYGVGASLVLQFSEALTEAHPGQYHFVFNNFFTSIALLDKLSSMGHQATGTVRKDHIDRVPLESDVALKKKERGTFDYRIDGKGNIVCRWNDNSVVTVASSGAGIHPLCLVSRYSQKLKKKIQVQQPNMIKVYNQFMGGVDRADENIDKYRASIRGKKWYSSPLLFCFELVLQNAWQLHKTYDEKPVDFLEFRRRVVCHYLETHGHPPEPGQKGRPQKRNIDSRYDGINHVIVKQGKQTRCAECHKNTTFRCEKCDVALHVKCSVEYHTE
Protein: Uncharacterized derlin-like protein C365.08c (Q9Y7Y0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ERAD-associated E3 ubiquitin-protein ligase hrd1
- Cell division cycle protein 48
- Protein OS-9 homolog
- Ubiquitin fusion degradation protein 1
- Putative ERAD-associated E3 ubiquitin-protein ligase component
- Nuclear protein localization protein 4
- Endoplasmic reticulum chaperone BiP
- UBX domain-containing protein 3
- Uncharacterized derlin-like protein C1687.17c
- Uncharacterized Sel1-like repeat-containing protein C1B3.10c
Sequence:
MASEFSGQIQELLSRIPPVTRYILLGTAATTILTLCQLLSPSMLVLHYPLVVRQKQWYRLFTNYLYAGTGFDFIMNIYFFYQYSTYLENFVFARNAKKYIIYLVKVALLIDAFSLISGLGSALNQSLAAAIAYNWSLFNSFSKIQFLFGFHVQGKYLPYVLLGFSFLTGGLPSLVVLGFGIISAMIVNFFDSIHTPVVHRSNSPKLNSQKVSGTFIGKGKKLGT
Protein: Protein CSN12 homolog (O13873)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- 26S proteasome complex subunit rpn15
- THP3 homolog C2A9.11c
- SAGA complex subunit Sus1
- SAC3 family protein 1
- SAC3 family protein 2
- Probable 26S proteasome regulatory subunit rpn3
- Pdp3-interacting factor 1
- Cell division control protein 31
- PCI domain-containing protein C1105.07c
Sequence:
MSERPLPLNVYFSTINSAVARSNSVLLAKNLSIPWGKTLTSVLNFDIPGTYSSDDVLKLTVERSISKNWTDIVLLHLQVLLYLVRDHDPAAAFKQQTELAQHLYREFSSGRCTGVHLPVLFIVCKDLRFLAINAHNAMLRRKQQLKVISVDESEENEQLEATARLINRAFTICINDRAPLSTSRKWGAYYIMGLLFKLYLRLDCVHLTNNVLRAMKVVELPDISLFPKSHVVIFHYYLGIVAFLNQNYKNASAELEIAFSLCHKGYNRNLELILSYWIPTRILVNHQLPTKNLLSKFPNLASVYIPLTRALKSGNLGEFGKCLQKNETLLAKTKIYLTLEGTRDLCIRNLFRKTWIICGKSTRLPVSVFQIALQVAGTDLPKLHVEAILANMISKGYMRGYISRNFETVVLSAKDPFPKNVST
Protein: Class 2 porin (PorB protein) (Q9Z3B6)
Organism: Neisseria meningitidis
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|RuleBase:RU000469}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|RuleBase:RU000469}.
Interaction partners:
Sequence:
EVSRVKNQGVKTKTATQIADFGSKIGFKGQEDLGNGMKAIWQLEQKASIAGTNSGWGNRQSFIGLKGGFGTVRVGNLNTVLKDSGDNVNAWESGSNTGDVLGLGTIGRVESREISVRYDSPVFAGFSGSVQYVPRDNANDKDKYTHKQSSRESYHAGLKYENAGFFGQYAGSFAKYADLKDNAERVAVGTTGAHPVKDYQVHRVVAGYDANDLYVSVAGQYEAAKNNDTNPATNGKKLEQTQVAATAAYRFGNVTPRVSYAHGFKAKVNGKKAARYQYDQVIVGADYDFSKRTSALVSVGWLKEGKGVNKTEKTASM
Protein: D-ribitol-5-phosphate cytidylyltransferase (EC 2.7.7.40) (2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein) (Isoprenoid synthase domain-containing protein) (hISPD) (A4D126)
Organism: Homo sapiens (Human)
Function: Cytidylyltransferase required for protein O-linked mannosylation. Catalyzes the formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate. CDP-ribitol is a substrate of FKTN during the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Shows activity toward other pentose phosphate sugars and mediates formation of CDP-ribulose or CDP-ribose using CTP and ribulose-5-phosphate or ribose-5-phosphate, respectively. Not Involved in dolichol production.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:26687144}.
Interaction partners:
- Ribitol-5-phosphate transferase FKTN
- Ribitol-5-phosphate xylosyltransferase 1
- Ribitol 5-phosphate transferase FKRP
- Protein O-mannosyl-transferase 1
- Protein O-mannosyl-transferase 2
- Beta-1,4-glucuronyltransferase 1
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Transcription and mRNA export factor ENY2
- Protein O-mannose kinase
- Dystroglycan 1
Sequence:
MEAGPPGSARPAEPGPCLSGQRGADHTASASLQSVAGTEPGRHPQAVAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHKRISLVEAGVTRHRSIFNGLKALAEDQINSKLSKPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERARHRASEMPQAFLFDVIYEAYQQCSDYDLEFGTECLQLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKERISQEICVVMDTEEDNKHVGHLLEEVLKSELNHVKVTSEALGHAGRHLQQIILDQCYNFVCVNVTTSDFQETQKLLSMLEESSLCILYPVVVVSVHFLDFKLVPPSQKMENLMQIREFAKEVKERNILLYGLLISYPQDDQKLQESLRQGAIIIASLIKERNSGLIGQLLIA
Protein: Band 3 anion transport protein (Anion exchange protein 1) (AE 1) (Anion exchanger 1) (MEB3) (Solute carrier family 4 member 1) (CD antigen CD233) (P04919)
Organism: Mus musculus (Mouse)
Function: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:2713407}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}. Basolateral cell membrane {ECO:0000250|UniProtKB:P02730}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}. Note=Detected in the erythrocyte cell membrane and on the basolateral membrane of alpha-intercalated cells in the collecting duct in the kidney. {ECO:0000250|UniProtKB:P02730}.
Interaction partners:
- Glycophorin-A
- Ankyrin-1
- Protein 4.2
- Ankyrin-3
- Ankyrin-2
- Protein 4.1
- Ammonium transporter Rh type A
- Glyceraldehyde-3-phosphate dehydrogenase
- Alpha-adducin
- Beta-adducin
Sequence:
MGDMRDHEEVLEIPDRDSEEELENIIGQIAYRDLTIPVTEMQDPEALPTEQTATDYVPSSTSTPHPSSGQVYVELQELMMDQRNQELQWVEAAHWIGLEENLREDGVWGRPHLSYLTFWSLLELQKVFSKGTFLLGLAETSLAGVANHLLDCFIYEDQIRPQDREELLRALLLKRSHAEDLGNLEGVKPAVLTRSGGASEPLLPHQPSLETQLYCGQAEGGSEGPSTSGTLKIPPDSETTLVLVGRANFLEKPVLGFVRLKEAVPLEDLVLPEPVGFLLVLLGPEAPHVDYTQLGRAAATLMTERVFRITASMAHNREELLRSLESFLDCSLVLPPTDAPSEKALLNLVPVQKELLRRRYLPSPAKPDPNLYNTLDLNGGKGGPGDEDDPLRRTGRIFGGLIRDIRRRYPYYLSDITDALSPQVLAAVIFIYFAALSPAVTFGGLLGEKTRNLMGVSELLISTAVQGILFALLGAQPLLVLGFSGPLLVFEEAFFSFCESNNLEYIVGRAWIGFWLILLVMLVVAFEGSFLVQYISRYTQEIFSFLISLIFIYETFSKLIKIFQDYPLQQTYAPVVMKPKPQGPVPNTALFSLVLMAGTFLLAMTLRKFKNSTYFPGKLRRVIGDFGVPISILIMVLVDSFIKGTYTQKLSVPDGLKVSNSSARGWVIHPLGLYRLFPTWMMFASVLPALLVFILIFLESQITTLIVSKPERKMIKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASGPGAAAQIQEVKEQRISGLLVSVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPFVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRLILPLIFRELELQCLDGDDAKVTFDEENGLDEYDEVPMPV
Protein: Cofilin 2 (Muscle), isoform CRA_a (Cofilin 2 (Muscle), isoform CRA_c) (Cofilin isoform) (cDNA, FLJ94864, Homo sapiens cofilin 2 (muscle) (CFL2), mRNA) (Q549N0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDIGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGNVVVSLEGKPL
Protein: Alsin Rho guanine nucleotide exchange factor ALS2 (Amyotrophic lateral sclerosis 2 isoform 1) (A0A0S2Z5Q7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSKKRSSTEAEGSKERGLVHIWQAGSFPITPERLPGWGGKTVLQAALGVKHGVLLTEDGEVYSFGTLPWRSGPVEICPSSPILENALVGQYVITVATGSFHSGAVTDNGVAYMWGENSAGQCAVANQQYVPEPNPVSIADSEASPLLAVRILQLACGEEHTLALSISREIWAWGTGCQLGLITTAFPVTKPQKVEHLAGRVVLQVACGAFHSLALVQCLPSQDLKPVPERCNQCSQLLITMTDKEDHVIISDSHCCPLGVTLTESQAENHASTALSPSTETLDRQEEVFENTLVANDQSVATELNAVSAQITSSDAMSSQQNVMGTTEISSARNIPSYPDTQAVNEYLRKLSDHSVREDSEHGEKPVPSQPLLEEAIPNLHSPPTTSTSALNSLVVSCASAVGVRVAATYEAGALSLKKVMNFYSTTPCETGAQAGSSAIGPEGLKDSREEQVKQESMQGKKSSSLVDIREEETEGGSRRLSLPGLLSQVSPRLLRKAARVKTRTVVLTPTYSGEADALLPSLRTEVWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGKEVIHLEAGGYHSLALTAKSQVYSWGSNTFGQLGHSDFPTTVPRLAKISSENGVWSIAAGRDYSLFLVDTEDFQPGLYYSGRQDPTEGDNLPENHSGSKTPVLLSCSKLGYISRVTAGKDSYLALVDKNIMGYIASLHELATTERRFYSKLSDIKSQILRPLLSLENLGTTTTVQLLQEVASRFSKLCYLIGQHGASLSSFLHGVKEARSLVILKHSSLFLDSYTEQVSSPVSCSISAGLFCQGEQLLNQKRLD
Protein: Peroxisome assembly protein 12 (Peroxin-12) (Peroxisome assembly factor 3) (PAF-3) (O00623)
Organism: Homo sapiens (Human)
Function: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10. When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:9922452}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein PEX13
- Peroxisome biogenesis factor 2
- Peroxisomal targeting signal 1 receptor
- Peroxisomal membrane protein PEX14
- Peroxisomal biogenesis factor 19
- Peroxisomal biogenesis factor 3
- Peroxisomal ATPase PEX6
- Peroxisomal targeting signal 2 receptor
- Peroxisomal membrane protein PEX16
Sequence:
MAEHGAHFTAASVADDQPSIFEVVAQDSLMTAVRPALQHVVKVLAESNPTHYGFLWRWFDEIFTLLDLLLQQHYLSRTSASFSENFYGLKRIVMGDTHKSQRLASAGLPKQQLWKSIMFLVLLPYLKVKLEKLVSSLREEDEYSIHPPSSRWKRFYRAFLAAYPFVNMAWEGWFLVQQLRYILGKAQHHSPLLRLAGVQLGRLTVQDIQALEHKPAKASMMQQPARSVSEKINSALKKAVGGVALSLSTGLSVGVFFLQFLDWWYSSENQETIKSLTALPTPPPPVHLDYNSDSPLLPKMKTVCPLCRKTRVNDTVLATSGYVFCYRCVFHYVRSHQACPITGYPTEVQHLIKLYSPEN
Protein: Cytochrome bc1 complex cytochrome b subunit (EC 7.1.1.8) (Cytochrome bc1 reductase complex subunit QcrB) (Ubiquinol--cytochrome c reductase cytochrome b subunit) (P9WP37)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Cytochrome b subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of ubiquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. The cytochrome b subunit contains two ubiquinol reactive sites: the oxidation (QP) site and the reduction (QN) site.
Subcellular location: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable cytochrome c oxidase subunit 3
- Cytochrome bc1 complex cytochrome c subunit
- Uncharacterized protein Rv2876
- Probable cytochrome c oxidase polypeptide 4
- Cytochrome bc1 complex Rieske iron-sulfur subunit
- Probable cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 2
- Superoxide dismutase
- Uncharacterized zinc protease Rv2782c
- NADH-quinone oxidoreductase subunit M
Sequence:
MSPKLSPPNIGEVLARQAEDIDTRYHPSAALRRQLNKVFPTHWSFLLGEIALYSFVVLLITGVYLTLFFDPSMVDVTYNGVYQPLRGVEMSRAYQSALDISFEVRGGLFVRQIHHWAALMFAAAIMVHLARIFFTGAFRRPRETNWVIGSLLLILAMFEGYFGYSLPDDLLSGLGLRAALSSITLGMPVIGTWLHWALFGGDFPGTILIPRLYALHILLLPGIILALIGLHLALVWFQKHTQFPGPGRTEHNVVGVRVMPVFAFKSGAFFAAIVGVLGLMGGLLQINPIWNLGPYKPSQVSAGSQPDFYMMWTEGLARIWPPWEFYFWHHTIPAPVWVAVIMGLVFVLLPAYPFLEKRFTGDYAHHNLLQRPRDVPVRTAIGAMAIAFYMVLTLAAMNDIIALKFHISLNATTWIGRIGMVILPPFVYFITYRWCIGLQRSDRSVLEHGVETGIIKRLPHGAYIELHQPLGPVDEHGHPIPLQYQGAPLPKRMNKLGSAGSPGSGSFLFADSAAEDAALREAGHAAEQRALAALREHQDSIMGSPDGEH
Protein: Gelsolin (Actin-depolymerizing factor) (ADF) (Brevin) (P20305)
Organism: Sus scrofa (Pig)
Function: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (By similarity). Plays a role in ciliogenesis (By similarity).
Subcellular location: [Isoform 2]: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
Interaction partners:
- Caspase-3
- Cofilin-1
- Vinculin
- Hematopoietic lineage cell-specific protein
- Src substrate cortactin
Sequence:
LGALVVALCALSPPARAATASRGAPQARAPQGRVSPMRPSTMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPPNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVAVQRLFQVKGRRVVRATEVPVSWESFNRGDCFILDLGNDIYQWCGSNSNRYERLKATQVSKGIRDNERSGRAHVHVSEEDAEPAGMLQVLGPKPTLPEGTEDTVKEDAANRKLAKLYKVSNGAGTMTVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALKTASDFISKMNYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQVDGPGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYRGGTSREGGQTAPASTRLFQVRASSSGATRAVEVIPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDSFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVVEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPINVVKQGFEPPSFVGWFLGWDDNYWSVDPLDRAIAELAA
Protein: Sorting nexin-18 (SH3 and PX domain-containing protein 3B) (Q96RF0)
Organism: Homo sapiens (Human)
Function: Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Stimulates the GTPase activity of DNM2. Promotes DNM2 location at the plasma membrane. Together with DNM2, involved in autophagosome assembly by regulating trafficking from recycling endosomes of phospholipid scramblase ATG9A.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:22718350}; Peripheral membrane protein {ECO:0000269|PubMed:18411244}; Cytoplasmic side {ECO:0000269|PubMed:18411244}. Endosome membrane {ECO:0000269|PubMed:29437695}; Peripheral membrane protein {ECO:0000269|PubMed:18411244}; Cytoplasmic side {ECO:0000269|PubMed:18411244}. Recycling endosome membrane {ECO:0000269|PubMed:29437695}; Peripheral membrane protein {ECO:0000269|PubMed:18411244}; Cytoplasmic side {ECO:0000269|PubMed:18411244}. Cell membrane {ECO:0000269|PubMed:20427313}; Peripheral membrane protein {ECO:0000269|PubMed:18411244}; Cytoplasmic side {ECO:0000269|PubMed:18411244}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18411244}; Peripheral membrane protein {ECO:0000269|PubMed:18411244}; Cytoplasmic side {ECO:0000269|PubMed:18411244}. Note=Localized at sites of endocytosis at the cell membrane (PubMed:18411244). Detected on newly formed macropinosomes (PubMed:21048941). Partially colocalized with clathrin and dynamin at the cell membrane (PubMed:20427313). Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation (PubMed:18411244). {ECO:0000269|PubMed:18411244, ECO:0000269|PubMed:20427313, ECO:0000269|PubMed:21048941}.
Interaction partners:
- Sorting nexin-9
- Sorting nexin-33
- Dynamin-2
- Autophagy-related protein 16-1
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
Sequence:
MALRARALYDFRSENPGEISLREHEVLSLCSEQDIEGWLEGVNSRGDRGLFPASYVQVIRAPEPGPAGDGGPGAPARYANVPPGGFEPLPVAPPASFKPPPDAFQALLQPQQAPPPSTFQPPGAGFPYGGGALQPSPQQLYGGYQASQGSDDDWDDEWDDSSTVADEPGALGSGAYPDLDGSSSAGVGAAGRYRLSTRSDLSLGSRGGSVPPQHHPSGPKSSATVSRNLNRFSTFVKSGGEAFVLGEASGFVKDGDKLCVVLGPYGPEWQENPYPFQCTIDDPTKQTKFKGMKSYISYKLVPTHTQVPVHRRYKHFDWLYARLAEKFPVISVPHLPEKQATGRFEEDFISKRRKGLIWWMNHMASHPVLAQCDVFQHFLTCPSSTDEKAWKQGKRKAEKDEMVGANFFLTLSTPPAAALDLQEVESKIDGFKCFTKKMDDSALQLNHTANEFARKQVTGFKKEYQKVGQSFRGLSQAFELDQQAFSVGLNQAIAFTGDAYDAIGELFAEQPRQDLDPVMDLLALYQGHLANFPDIIHVQKGKAWPLEQVIWSVLCRLKGATLTAVPLWVSESYSTGEEASRDVDAWVFSLECKLDCSTGSFLLEYLALGNEYSFSKVQRVPLMTVLSF