wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxisome assembly protein 12 (Peroxin-12) (Q01961)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Function: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 and/or PEX20 receptors from peroxisomes to the cytosol, thereby promoting PEX5 and PEX20 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 and/or PEX20 through the peroxisomal membrane (By similarity). PEX12 also regulates PEX5 and/or PEX20 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (By similarity). When PEX5 or PEX20 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5 and/or PEX20, leading to its subsequent degradation (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:Q04370}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDFYSNLDSRSLDSETPTLFEIISAQELEKLLTPSIRYILVHYTQRYPRYLLKVANHFDELNLAIRGFIEFRQLSHWNSTFIDKFYGLKKVRNHQTISTERLQSQVPTLLEQRRRLSKTQIAVSLFEIVGVPYLRDKLDHLYDKLYPKLMMNNLDPKESLKTFVQYYFLKLYPILLSVLTTIQVLLQVLYLSGTFKSPSIIMWLFKMKYARLNSYDYTLDEQRVNKFLNKTSPGKLGTGNNRIRPITLTESLYLLYSDLTRPLKKGLLITGGTLFPASIFLLKFLEWWNSSDFATKMNKPRNPFSDSELPPPINLSKDLLADRKIKKLLKKSQSNDGTCPLCHKQITNPAVIETGYVFCYTCIFKHLTSSELDEETGGRCPITGRRLLGCRINKTTGEWTVDGIRRLMM
Protein: Replication factor C subunit 3 (Replication factor C3) (O14003)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. Subunit 3 binds ATP. Also involved in replication and DNA damage checkpoint controls, probably functioning as a checkpoint sensor.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Replication factor C subunit 4
- Replication factor C subunit 1
- Replication factor C subunit 2
- Checkpoint protein rad17
- Replication factor C subunit 5
- Telomere length regulation protein elg1
- Chromosome transmission fidelity protein 18
- Proliferating cell nuclear antigen
- Sister chromatid cohesion protein dcc1
- Checkpoint protein hus1
Sequence:
MSIEKGKGRAMDIDLPLGSESTLPWVEKYRPANLEDVVSHKDIISTLEKFISSNRVPHMLFYGPPGTGKTSTILACARKIYGPNYRNQLMELNASDDRGIDAVREQIKNFASTRQIFASTFKMIILDEADAMTLAAQNALRRVIEKYTKNVRFCIICNYINKISPAIQSRCTRFRFQPLPPKEIEKTVDHVIQSEHCNIDPDAKMAVLRLSKGDMRKALNILQACHAAYDHIDVSAIYNCVGHPHPSDIDYFLKSIMNDEFVIAFNTISSIKQQKGLALQDILTCIFEALDELEIKPNAKIFILDQLATIEHRMSFGCSEKIQLSAMIASIKTGVDLAAKVN
Protein: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA) (F1LM47)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03220}.
Interaction partners:
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Citrate synthase, mitochondrial
Sequence:
MAASMFFGRQLAAAALRSHRSQTTVRATAQALGSSGLFNKHGFQMQQQQQQQRSLSLHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFTSGLKGGVKIVFSPEEAKAVSSQMIGQKLITKQTGAKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPEAIVKEPVDIIEGVKKEQAVTLAKKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDADGKVLCMDAKINFDSNSAYRQKKIFALQDWSQEDERDKDAADADINYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKRVQAILVNIFGGIMRCDIIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSEIVTLAKEAHVDVKFQLPI
Protein: PRAME family member 6 (Q5VXH4)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex, which mediates ubiquitination of target proteins, leading to their degradation. The CRL2(PRAMEF6) complex mediates ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding.
Interaction partners:
- Ubiquitin-like protein FUBI
- Kelch domain-containing protein 3
- Kelch domain-containing protein 2
- Protein fem-1 homolog C
- demerged
- Amyloid protein-binding protein 2
- Cullin-2
- Melanoma antigen preferentially expressed in tumors
- E3 ubiquitin-protein ligase RBX1
- Kelch domain-containing protein 10
Sequence:
MSIRTPPRLLELAGRSLLRDQALAMSTLEELPTELFPPLFMEAFSRRRCEALKLMVQAWPFRRLPLRPLIKMPCLEAFQAVLDGLDALLTQGVHPRRWKLQVLDLQDVCENFWMVWSEAMARGCFLNAKRNKTPVQDCPRMRGQQPLTVFVELWLKNRTLDEYLTCLLLWVKQRKDLLHLCCKKLKILGMPFRNIRSILKMVNLDCIQEVEVNCKWVLPILTQFTPYLGHMRNLQKLVLSHMDVSRYVSPEQKKEIVTQFTTQFLKLCCLQKLSMNSVSFLEGHLDQLLSCLKTSLKVLTITNCVLLESDLKHLSQCPSISQLKTLDLSGIRLTNYSLVPLQILLEKVAATLEYLDLDDCGIIDSQVNAILPALSRCFELNTFSFCGNPISMATLENLLSHTIILKNLCVELYPAPRESYDADGTLCWSRFAQIRAELMKRVRDLRHPKRILFCTDCCPDCGNRSFYDLEADQCCC
Protein: Signal transducer and activator of transcription (A0A669KB53)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
Sequence:
MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMVSTTAGLCVALNKCVCSEAGSAPWQIPGLSAGGSPGGAKESAVLR
Protein: Protein NDRG2 (N-myc downstream-regulated gene 2 protein) (Protein Ndr2) (Q9QYG0)
Organism: Mus musculus (Mouse)
Function: Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14985363, ECO:0000269|PubMed:16520977}. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MAELQEVQITEEKPLLPGQTPETAKEAELAARILLDQGQTHSVETPYGSVTFTVYGTPKPKRPAIFTYHDVGLNYKSCFQPLFRFGDMQEIIQNFVRVHVDAPGMEEGAPVFPLGYQYPSLDQLADMIPCILQYLNFSTIIGVGVGAGAYILSRYALNHPDTVEGLVLINIDPNAKGWMDWAAHKLTGLTSSIPDMILGHLFSQEELSGNSELIQKYRGIIQHAPNLENIELYWNSYNNRRDLNFERGGETTLKCPVMLVVGDQAPHEDAVVECNSKLDPTQTSFLKMADSGGQPQLTQPGKLTEAFKYFLQGMGYMASSCMTRLSRSRTASLTSAASIDGSRSRSRTLSQSSESGTLPSGPPGHTMEVSC
Protein: NDR1/HIN1-like protein 10 (AtNHL10) (Protein YELLOW-LEAF-SPECIFIC GENE 9) (Q9SJ52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in plant immunity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FNH6}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Senescence-induced receptor-like serine/threonine-protein kinase
- Cytochrome P450 81F2
- RBR-type E3 ubiquitin transferase
- Protein EXORDIUM-like 1
- Mitogen-activated protein kinase 3
- Protein YLS7
- Elicitor peptide 2
- Uncharacterized protein At5g41620
- Elicitor peptide 3
- Protein VACUOLELESS GAMETOPHYTES
Sequence:
MAAEQPLNGAFYGPSVPPPAPKGYYRRGHGRGCGCCLLSLFVKVIISLIVILGVAALIFWLIVRPRAIKFHVTDASLTRFDHTSPDNILRYNLALTVPVRNPNKRIGLYYDRIEAHAYYEGKRFSTITLTPFYQGHKNTTVLTPTFQGQNLVIFNAGQSRTLNAERISGVYNIEIKFRLRVRFKLGDLKFRRIKPKVDCDDLRLPLSTSNGTTTTSTVFPIKCDFDF
Protein: Polybia-CP (Pol-CP-NH2) (Polybia chemotactic peptide) (P0C1R0)
Organism: Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp)
Function: Potent antimicrobial peptide that is active against both Gram-positive and Gram-negative bacteria (B.subtilis (MIC=15 ug/ml or 4-16 uM), S.epidermidis (MIC=8-16 uM), S.aureus (MIC=15 ug/ml or 4 uM), E.coli (MIC=8-64 uM) and P.aeruginosa (MIC=64-128 uM)). Also shows cytotoxicity towards HEK293 cells (32 uM). Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane. Acts by disrupting bacterial membrane. Also acts in inflammation since it is chemotactic for polymorphonucleated leukocytes (PMNL). Shows potent antitumor activity against prostate (PC-3) and bladder (Biu-87) cancer cell lines. Causes a reduced hemolysis to mammalian erythrocytes (HC(50)=50 uM) and has no mast cell degranulation activity at physiological concentrations. In addition, when tested in vitro on the parasite Trypanosoma cruzi (responsible of the Chagas disease), is able to reduce the number of the three forms (epimastigote, trypomastigote and amastigote), probably acting through the apoptotic cell death pathway.
Subcellular location: Secreted {ECO:0000269|PubMed:16129513}. Target cell membrane {ECO:0000269|PubMed:21745529, ECO:0000269|PubMed:22450985}.
Interaction partners:
Sequence:
ILGTILGLLKSL
Protein: MgtC/SapB family protein (O53255)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MLTVVAVIGILECGLVLHMPDNDLWYCGPWTLWVMAGRGVASGAGVWRGDRVATPLAVAITAAGLVSGARIGPGAAAKRDPQLAQWNEIRSHYQEIAEWIDHDTATAHPAVAATQISAAGSFGRANMVDYLGLLDSRADETVRRDEFSRWLSAKPDYLVTTEQSVDAATIALPEFRHAYDRAATIGTLNVYRRNSPDGDEPLPADGN
Protein: p44-12 outer membrane protein (Q2GIM8)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MMSMAIVMAGNDVRAHDDVSALETGGAGYFYVGLDYSPAFSKIRDFSIRESNGETKAVYPYLKDGKSVKLESHKFDWNTPDPRIGFKDNMLVAMEGSVGYGIGGARVELEIGYERFKTKGIRDSGSKEDEADTVYLLAKELAYDVVTGQTDNLAAALAKTSGKDIVQFAKAVGVSHPGIDKKVCDGGHARGKKSGDNGSLADYTDGGASQTNKTAQCSGMGTGKAGKRGLGLTEFVNKTKVGEGKNWPTGYVNDGDNVNVLGDTNGNAEAVAKDLVQELTPEEKTIVAGLLAKTIEGGEVVEIRAVSSTSVMVNACYDLLSEGLGVVPYACVGLGGNFVGVVDGHITPKLAYRLKAGLSYQLSPVISAFAGGFYHRVVGDGVYDDLPAQLP
Protein: Paladin (Q803E0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- Zinc finger protein 646.
- Sulfotransferase
Sequence:
MGTTASAAPQATLHERLHSDSMTDSRRSIQTLGIHNNKAKSIITNKVAPVVITYNCRQEFQIHDDVLRTNYKVGRISDNMPEHHLVQGSFFMVQDVFSKADVLNTTASYGAPNFRQSGGGFPLYGMGQTSLGGFKRVLESLQTRGHQEVIFFCLREEPVVFLHLQEDFLPYTPRRKENLHENLQHLQRGASSEDLELTIRKELHDFAKLNDNMFYVYNDIEHLKGEPQKICICSEEDIHITEEVYRRPRFTMPAYRYYRLPLPMEGAPMEEQFDAFVKVLRENPSLSLNRDASRLLPALLFSCQVGVGRTNLGLILGTLVMMHLTRTTAEKTTPAEEEVKDEHKIQFRVIESLIGKLPKGQEVMEEVNRAIDLCSEMHDIRESIYENKQKLEGIGEDYQTQGSSTKDYFLHGALQSLERYFYLIVFNAYLHEQYPLAFACSFSQWLCSNAWIYRLLSCMNQSELRAPADLVTKGARVLVADEYLAPDVLSTIKEMKVANFRRVPKMSIYGMAQPTSEAASVVLAYLCDEKRKHSSVLWVNLQDELLLEANNQIFSPREPTRVEQCIRVCSAQPEDIQSLEASLKAQLLASQQWLEVTLEQEKQMKMIKSCSTVQEIFNQLKSSHHALQYRRIPFPECSAPSEEGFDQLLDVMKATLAEDSLSAFVFNCSNGKARTTTAMVIATLTLWHFNGFPEFCEDEIVSVPDAKYTKGEFEVVMKLVRLLPDGQRMKREVDAALDSVSETMTPLHYHLREIIICTYRQIRSCKSDAELLALQALLYLERYIYLILYNSYLHLEKRDSWRRPFSVWMQQVAAPAGVYELLNQLGFSEFEDLRDSTLCRLRRRWLQQNRHGLPFRGELI
Protein: (thale cress) hypothetical protein (A0A178UNB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEMKLLFTSAFTQMFGYSNHMDQASNCQSTRNKIIKMMKKEEFPSGFQVPLHYPKYSKSDYEVMDDLRLDLLLKQYGFSFEGSLEDKRVFAIESFLWPDQL
Protein: C-mannosyltransferase dpy-19 (EC 2.4.1.-) (Protein dumpy-19) (P34413)
Organism: Caenorhabditis elegans
Function: C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins such as unc-5 and mig-21. Mediates the attachment of alpha-mannose in C-C linkage to the C2 of the indole ring of tryptophan. C-mannosylation takes place in the endoplasmic reticulum and frequently found in thrombospondin (TSP) type-1 repeats and in the WSXWS motif of type I cytokine receptors. Required to orient neuroblasts QL and QR correctly on the anterior/posterior (A/P) axis: QL and QR are born in the same A/P position, but polarize and migrate left/right asymmetrically, QL migrates toward the posterior and QR migrates toward the anterior. Required with unc-40 to express mab-5 correctly in the Q cell descendants.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Abnormal cell migration protein 21
- Protein glp-1
- V-type proton ATPase 116 kDa subunit a 1
- Endoprotease bli-4
- Cuticle collagen dpy-10
Sequence:
MAKKPKNSPEKSKYSSDTSSSLYSQTWLASVVIIGLLVGYINYQHVYTLFENDKHFSHLADFEREMAYRTEMGLYYSYYKTIINAPSFLEGVQEITHDTVTEHGHEINTLNRFNLYPEVILAFLYRPFRAFAKSANWQIELCWQVNRGELRPVESCEGIGNPHYFYITGVFIVAGTVASSIFYLGVLVSDSIFGGFLSVLCFAFNHGEATRVQWTPPLRESFAFPFIIGHIAILTFVIKYKKSGHSMILLLTSMAVPALLFWQFTQFAFFTQICSIFLAFSLDLIPFSTAKTVIHSHIISFLIGFLLLFGNEMMITALYFPSILALGMIIYISPLLSNLKFRPAYVLFLAIIFASITLGLKIGLSKGLGIEDDAHIFDILRSKFTSFANFHTRLYTCSAEFDFIQYSTIEKLCGTLLIPLALISLVTFVFNFVKNTNLLWRNSEEIGENGEILYNVVQLCCSTVMAFLIMRLKLFMTPHLCIVAALFANSKLLGGDRISKTIRVSALVGVIAILFYRGIPNIRQQLNVKGEYSNPDQEMLFDWIQHNTKQDAVFAGTMPVMANVKLTTLRPIVNHPHYEHVGIRERTLKVYSMFSKKPIAEVHKIMKEMGVNYFVFQLMNCSNDERRPECVYRGMWDEEDPKNSGRTALCDLWILAANSKDNSRIAPFKIVYNANRNYIVLKI
Protein: Homer protein homolog 1b isoform 1 (Homer scaffold protein 1b) (B8JIC5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
- Metabotropic glutamate receptor 5
- Metabotropic glutamate receptor 1
- Homer scaffold protein 3b.
- SH3 and multiple ankyrin repeat domains 3b.
- Glutamate receptor, metabotropic 5b.
- Chloride intracellular channel protein
- BR serine/threonine kinase 2b.
Sequence:
MEDEEMVIRLPGRSSAPGGVGETTVLRHKEVHHFFFLPFREQPIYSTRAHVFQIDPSTKKNWMPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMSFTKTSQKFGQWADSRANTVYGLGFSSEHHLAKFADKFAEYKEAARIAKEKSLEKMELASSPSQESPADIHSPLTPPVTADLCRINGTGDDVTLSDVSPNSMLQSDLSPTTPTLAHSPTTNKHWEAELAALKSNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVSELESQSSQTNVIKSQKTELNQTIEELECTLRAKEEEMMRLKEEVENAKQLQAQKDELTKKLEDTDMRNKELEEQLSDLEQRLESSQVDQENLRKNLKTLLEILDGKIFELTELRDNLAKLIEDS
Protein: Vancomycin aglycone glucosyltransferase (EC 2.4.1.310) (Glycosyltransferase GtfB) (P96559)
Organism: Amycolatopsis orientalis (Nocardia orientalis)
Function: Glucosyltransferase that transfers glucose to the 4-OH-Phegly(4) residue of vancomycin aglycone (AGV) to produce devancoaminyl-vancomycin (DVV) in the biosynthesis of glycopeptide antibiotic chloroeremomycin, a member of the vancomycin group of antibiotics.
Interaction partners:
Sequence:
MRVLLATCGSRGDTEPLVALAVRVRDLGADVRMCAPPDCAERLAEVGVPHVPVGPSARAPIQRAKPLTAEDVRRFTTEAIATQFDEIPAAAEGCAAVVTTGLLAAAIGVRSVAEKLGIPYFYAFHCPSYVPSPYYPPPPLGEPSTQDTIDIPAQWERNNQSAYQRYGGLLNSHRDAIGLPPVEDIFTFGYTDHPWVAADPVLAPLQPTDLDAVQTGAWILPDERPLSPELAAFLDAGPPPVYLGFGSLGAPADAVRVAIDAIRAHGRRVILSRGWADLVLPDDGADCFAIGEVNHQVLFGRVAAVIHHGGAGTTHVAARAGAPQILLPQMADQPYYAGRVAELGVGVAHDGPIPTFDSLSAALATALTPETHARATAVAGTIRTDGAAVAARLLLDAVSREKPTVSA
Protein: L-cysteine S-thiosulfotransferase subunit SoxA (EC 2.8.5.2) (Cytochrome c551 subunit monoheme) (Protein SoxA) (SoxAX cytochrome complex subunit A) (Sulfur oxidizing protein A) (Thiosulfate-oxidizing multienzyme system protein SoxA) (TOMES protein SoxA) (Q8RLX0)
Organism: Chlorobaculum thiosulfatiphilum (Chlorobium limicola f.sp. thiosulfatophilum)
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c and which then may be used for reductive CO(2) fixation.
Subcellular location: Periplasm {ECO:0000269|PubMed:11863431}.
Interaction partners:
Sequence:
MKKTIQRGLFTGALVLLTAMTSKPAHAAVNYQALVDADVKKFQGYFLKEFPGVKLEDFGDGVYALDEDSRKQWKEMEEFPPYELDVEAGKALFNKPFANGKSLGSCFSNGGAVRGMYPYFDEKRKEVITLEMAINECRVANGEKPYAPKKGDIARVSAYIASISRGQKIDVKVKSKAAYDAYMKGKEMFYAKRGQLNMSCSGCHMEYSGRHLRAEIISPALGHTTHFPVFRSKWGEIGTLHRRYAGCNENIGAKPFPAQSKEYRDLEFFQTVMSNGLKFNGPASRK
Protein: Antithrombin-III (ATIII) (Serpin C1) (P01008)
Organism: Homo sapiens (Human)
Function: Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Prothrombin
- Coagulation factor IX
- Coagulation factor X
- Plasminogen
- Fibrinogen alpha chain
- Coagulation factor XII
- Coagulation factor XI
- Tissue factor
- Fibrinogen beta chain
- Vitronectin
Sequence:
MYSNVIGTVTSGKRKVYLLSLLLIGFWDCVTCHGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANPCVK
Protein: U-box domain-containing protein 73 (EC 2.3.2.27) (Plant U-box protein 73) (OsPUB73) (RING-type E3 ubiquitin transferase PUB73) (Q6K762)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Possesses E3 ubiquitin-protein ligase in vitro.
Interaction partners:
Sequence:
MDPEAEEAQLRLEMELAKKAKADMSGLQRSSSLGLDHAGLYPLPLPPGWRSAPTSPLRTPSSPPPLQFPPAWAADVAGTSGSAAPEDDGPARNAGADEATAGSAPKNEDPARAAGADDGPTRSDYAAMMRMALAKFQDDDAAADDEEAASAVMEQAMTGLMDLTYRKAKPPELPYEFATRWPIPIAHDGTLQAEVMRDPVILPSGYSVDQTYQNNQKRQNPWTNTSTFTDHSLPYSLSVPNHLLRDMISAWCLDHSDLSPSTTSDTPSTPLEPSEEEQIQRILKLFSGNSASQREALKLIQLLTKTTKGVQPCLAKYADIIPVLINLRRKYKSSWTQDLEEERLTIILNLTMHRQNREILAGQNELAGAIKKIVKKAGNRGKRTSSLAKVASIVAVLSEFDMFRKRMLDAGGMKMLRGMLKIKDTEVITEAATAILALYADGEGEQPARFHEVPQMLLECHMFTDGILLLLDRLPKSPRVFRKICDQALQLVNIVMAEDASGPVTRKGILSAISLIYEIVERDVGKMNAVKNMEDFIERLRQLSSDRLPMQKMLQVERIIRTLSDAFPAPTVRGRCQEPSGSRLLA
Protein: Peritrophin-48 (P91745)
Organism: Lucilia cuprina (Green bottle fly) (Australian sheep blowfly)
Function: May bind chitin or related oligosaccharide structures.
Interaction partners:
Sequence:
MIIKTLLASVAIMLIATVNAEYNVAKYCELVKIGTLMPSMISCQDYYICRLNNQPIPVKCGANTVFDKDTQGCVPEAQANCILSLDNPCENKDRTFAPSSKACNEWHYCLNGNIVANGSCQPGQIFDASKNSCIYGACNSDDDDSNSDFTPVLNICDIMQNGQFFGDFENCQNWQKCNNGRLQKGICLGNLVYDTKNGMCLQNDGTMCERTNGMVSEDGGAPDETLCTSSNDGPLPDKLTCSVYYICEQDTTSTPTTYKWIKTSCPNGQYFDVFGDGCLDRAKRRVYTGCNRCEYTTGSTTYWVNAVSNDCTKFSTCRNGRKITNEDGSCNSGYYFNEADQYCNMGDFTNYAETNGACQNYSCNGYDCTTKPSAT
Protein: E3 ubiquitin-protein transferase MAEA (EC 2.3.2.27) (Cell proliferation-inducing gene 5 protein) (Erythroblast macrophage protein) (Human lung cancer oncogene 10 protein) (HLC-10) (Macrophage erythroblast attacher) (P44EMLP) (Q7L5Y9)
Organism: Homo sapiens (Human)
Function: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase complex. MAEA is required for normal cell proliferation. The CTLH E3 ubiquitin-protein ligase complex is not required for the degradation of enzymes involved in gluconeogenesis, such as FBP1. Plays a role in erythroblast enucleation during erythrocyte maturation and in the development of mature macrophages (By similarity). Mediates the attachment of erythroid cell to mature macrophages; this MAEA-mediated contact inhibits erythroid cell apoptosis. Participates in erythroblastic island formation, which is the functional unit of definitive erythropoiesis. Associates with F-actin to regulate actin distribution in erythroblasts and macrophages (By similarity). May contribute to nuclear architecture and cells division events (Probable).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q4VC33}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17467196, ECO:0000269|PubMed:24143168, ECO:0000269|PubMed:29911972}. Nucleus matrix {ECO:0000269|PubMed:16510120}. Cell membrane {ECO:0000269|PubMed:9763581}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16510120}. Note=Detected in a nuclear, speckled-like pattern (PubMed:16510120). Localized with condensed chromatin at prophase; Detected in nuclear spindle poles at metaphase and in the contractile ring during telophase and cytokinesis (PubMed:16510120). Present in cytoplasm, nuclear matrix and at the cell surface in macrophages; predominantly nuclear in immature macrophages and predominantly detected at the cell surface in mature macrophages. Colocalizes with F-actin in macrophages (By similarity). {ECO:0000250|UniProtKB:Q4VC33, ECO:0000269|PubMed:16510120}.
Interaction partners:
- Armadillo repeat-containing protein 8
- E3 ubiquitin-protein transferase RMND5A
- WD repeat-containing protein 26
- Glucose-induced degradation protein 8 homolog
- Ran-binding protein 9
- Ran-binding protein 10
- Glucose-induced degradation protein 4 homolog
- Muskelin
- Protein yippee-like 5
- E3 ubiquitin-protein transferase RMND5B
Sequence:
MAVQESAAQLSMTLKVQEYPTLKVPYETLNKRFRAAQKNIDRETSHVTMVVAELEKTLSGCPAVDSVVSLLDGVVEKLSVLKRKAVESIQAEDESAKLCKRRIEHLKEHSSDQPAAASVWKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLDEVRQAMGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNNSVFTLTLQAGLSAIKTPQCYKEDGSSKSPDCPVCSRSLNKLAQPLPMAHCANSRLVCKISGDVMNENNPPMMLPNGYVYGYNSLLSIRQDDKVVCPRTKEVFHFSQAEKVYIM
Protein: Beta-defensin 129 (Beta-defensin 29) (DEFB-29) (Defensin, beta 129) (Q9H1M3)
Organism: Homo sapiens (Human)
Function: Has antibacterial activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Beta-defensin 125
- Defensin beta 118
- Beta-defensin 127
- Beta-defensin 128
- Beta-defensin 126
- Beta-defensin 121
- Beta-defensin 116
- Beta-defensin 110
- Beta-defensin 113
- Beta-defensin 124
Sequence:
MKLLFPIFASLMLQYQVNTEFIGLRRCLMGLGRCRDHCNVDEKEIQKCKMKKCCVGPKVVKLIKNYLQYGTPNVLNEDVQEMLKPAKNSSAVIQRKHILSVLPQIKSTSFFANTNFVIIPNATPMNSATISTMTPGQITYTATSTKSNTKESRDSATASPPPAPPPPNILPTPSLELEEAEEQ
Protein: Jim, isoform E (M9NFP1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAINFSASFAACIAAGLKVPRQIMYCITQDTGQPYVLYKDSQDAERNPGAIGATPAQWGSEMYPNIQQQAQQHLTAQQQQQQQQQNAAQAAAQAAAVAAAAGQPQSPPGGGQEARDNGSGDGRQQQVSPSSSPYPSVQQQQRANGAGDEDPMNHQLANQQNPAPNQNQSSNDPQHSGSNAGESGNPHVQQNGGPQNDPGNSFRTPDYYDPRHAAPQGGMLAPPGFPPLHYLNKGVLPMEQSGGGGGAGGGEAYALPEMLPAQQNGQQNAGPANTNANEGGAGANGSGGVGGATGASVGVGSVGVTSGGRTGNGPGRPHKNKPHSDLRLFKCLTCGKDFKQKSTLLQHDRIHTDARPFPCSECGKRFRQQSHLTQHLRIHANEKPFTCPYCSRSFRQRAILNQHIRIHSGEKPFACPECGKHFRQKAILNQHVRTHQDVSPHLIFKNGPHPTLWPSDVPFPGEDNDTKGDIAGTGGGYHDEDSQGTPDGSGGMHYPSYFKDGKDPRTGQKILPEVLQHIGVRPANMPLYVRCPICDKEFKQKTTLLQHGCIHIESRPYPCPECGKRFRQQSHLTQHLRIHTNEKPFGCMYCPRFFRQRTILNQHLRIHTGEKPYKCGQCGKDFRQKAILDQHTRTHQVGDRPFCCPMPNCRRRFATENEVTKHIDNHMNPNTTKVRRQQQQQHQQQQQQQQQQQQQQQQQNNNAVAQVANHLMNDAKSLAAQQFLNNNNPSAVDNKANILPVRSIASNAAAAAVVQQSVVKNELYFPQCYGPPFQHPFQAQQQQAQQPSVAHANGGPTPPVTVTVANSVASGVVVQQNASASVVAQ