wanglab/gogpt-training-data huggingface dataset:
Protein: Ras-related protein Rab-23 (EC 3.6.5.2) (Protein open brain) (Rab-15) (P35288)
Organism: Mus musculus (Mouse)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes (By similarity). Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14617350}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:14617350}. Cytoplasm {ECO:0000269|PubMed:14617350}. Endosome membrane {ECO:0000269|PubMed:14617350}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9ULC3}. Cytoplasmic vesicle, phagosome {ECO:0000305}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:Q9ULC3}.
Interaction partners:
- Protein smoothened
- Zinc finger protein GLI2
- Suppressor of fused homolog
- Transcriptional activator GLI3
- Ciliogenesis and planar polarity effector 2
- ADP-ribosylation factor-like protein 3
Sequence:
MLEEDMEVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQACVLVFSTTDRESFEAISSWREKVVAEVGDIPTALVQNKIDLLDDSCIKNEEAEGLAKRLKLRFYRTSVKEDLNVSEVFKYLAEKHLQKLKQQITEDPEQTHSSSNKIGVFNASVGSHLGQNSSSLNGGDVINLRPNKQRTKRTRNPFSSCSVP
Protein: DNA topoisomerase I, mitochondrial (TOP1mt) (EC 5.6.2.1) (Q8R4U6)
Organism: Mus musculus (Mouse)
Function: Releases the supercoiling and torsional tension of DNA introduced during duplication of mitochondrial DNA by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- DNA topoisomerase 2-alpha
- DNA topoisomerase 2-beta
- Tyrosyl-DNA phosphodiesterase 1
- Ribonuclease H2 subunit A
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- Exonuclease 1
- DNA topoisomerase 3-alpha
- ATP-dependent DNA helicase Q4
- DNA topoisomerase 3-beta-1
- DNA-directed RNA polymerase, mitochondrial
Sequence:
MLLLWLRALCRRFQHVPCRVPSCQVSRVAKANRAGWEETSKSSVKWRQLEHKGPYFTPAYEPLPDGVHFLYDGKPLKLSLAAEEVATFYGKMLHLECTSKEVFRRNFFSDWRKEMTPEERRLITHLDKCDFTEIHKHFLERAEARRTLPREQKQKLKEEAEKLQQEFGYCVLDGHREKIGNFKTEPPGLFRGRGDHPKMGMLKRRVMPEDVVINCSRDSKIPEPPAGHQWKEVRSDNTVMWLAAWVEHIQNSFKYVILNPSSKPKGEMDWQKYEVARRLKGVVDKIRAQYQADWKSPEMKKRQLAVALYFIDKLALRTGNEKEEGETADTVGCCSLRVEHIRLHAPAGGQEHVVELDFLGKDSIRYKNHVTVEKLVFQNLQHFMEDKDPRDDLFDALTTSSLNKHLQDLMEGLTAKVFRTYNASVTLQEQLRVLTRAEDSVTCKVLAYNRANRAVAVLCNHQRAVPKTFEKSMQTLQKKIETKKAQVAEAQVELQKAETDLRMRGDSKPKSFLQKQRRLLKLEEQLARLCAKATDKEENKQVALGTAKLNYLDPRISIAWCKRFGVPVEKIYNKTQRERFAWAFNQAGEDFEF
Protein: Inner membrane protein YidH (P0ADM0)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Inner membrane protein YidG
- Uncharacterized protein YidF
- Inner membrane protein YnbA
Sequence:
MKISRLGEAPDYRFSLANERTFLAWIRTALGFLAAGVGLDQLAPDFATPVIRELLALLLCLFSGGLAMYGYLRWLRNEKAMRLKEDLPYTNSLLIISLILMVVAVIVMGLVLYAG
Protein: Salivary acidic proline-rich phosphoprotein 1/2 (Db-s) (PRP-1/PRP-2) (Parotid acidic protein) (Pa) (Parotid double-band protein) (Parotid isoelectric focusing variant protein) (PIF-S) (Parotid proline-rich protein 1/2) (Pr1/Pr2) (Protein C) [Cleaved into: Salivary acidic proline-rich phosphoprotein 1/2; Salivary acidic proline-rich phosphoprotein 3/4 (Db-F) (PIF-F) (PRP-3/PRP-4) (Protein A); Peptide P-C] (P02810)
Organism: Homo sapiens (Human)
Function: PRP's act as highly potent inhibitors of crystal growth of calcium phosphates. They provide a protective and reparative environment for dental enamel which is important for the integrity of the teeth.
Subcellular location: Secreted.
Interaction partners:
- Cryptochrome-1
- Basic salivary proline-rich protein 4
- Uncharacterized protein
- Basic salivary proline-rich protein 1
- Cryptochrome-2
- ATP-dependent DNA helicase PIF1
- Basic salivary proline-rich protein 2
- DET1 homolog
- C4b-binding protein alpha chain
- Zinc finger protein 346
Sequence:
MLLILLSVALLAFSSAQDLDEDVSQEDVPLVISDGGDSEQFIDEERQGPPLGGQQSQPSAGDGNQNDGPQQGPPQQGGQQQQGPPPPQGKPQGPPQQGGHPPPPQGRPQGPPQQGGHPRPPRGRPQGPPQQGGHQQGPPPPPPGKPQGPPPQGGRPQGPPQGQSPQ
Protein: Ascorbate-specific PTS system EIIA component (Ascorbate-specific phosphotransferase enzyme IIA component) (P69820)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ascorbate-specific PTS system EIIB component
- Ascorbate-specific PTS system EIIC component
- Probable L-ascorbate-6-phosphate lactonase UlaG
- 3-keto-L-gulonate-6-phosphate decarboxylase UlaD
- L-ribulose-5-phosphate 3-epimerase UlaE
- L-ribulose-5-phosphate 4-epimerase UlaF
- Phosphocarrier protein HPr
- Putative L-ribulose-5-phosphate 3-epimerase SgbU
- 3-keto-L-gulonate-6-phosphate decarboxylase SgbH
- HTH-type transcriptional regulator UlaR
Sequence:
MKLRDSLAENKSIRLQAEAETWQEAVKIGVDLLVAADVVEPRYYQAILDGVEQFGPYFVIAPGLAMPHGRPEEGVKKTGFSLVTLKKPLEFNHDDNDPVDILITMAAVDANTHQEVGIMQIVNLFEDEENFDRLRACRTEQEVLDLIDRTNAAA
Protein: Small heat shock protein HSP16.5 (Q57733)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Chaperone that confers thermal protection to other proteins.
Subcellular location: Cytoplasm.
Interaction partners:
- Thermosome subunit
- Archaeal Lon protease
- Large ribosomal subunit protein uL16
- Thioredoxin
Sequence:
MFGRDPFDSLFERMFKEFFATPMTGTTMIQSSTGIQISGKGFMPISIIEGDQHIKVIAWLPGVNKEDIILNAVGDTLEIRAKRSPLMITESERIIYSEIPEEEEIYRTIKLPATVKEENASAKFENGVLSVILPKAESSIKKGINIE
Protein: PR domain zinc finger protein 5 (EC 2.1.1.-) (PR domain-containing 5) (F1Q8J8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Zinc finger protein 488
Sequence:
MRMLGMYVPDRFVLKSSQVQDGMGLYTTRTVKKGEKFGPFAGEKRMLGDLDESMDPRLMWEVRGNKGDVLYILDASNPRHANWLRFVHQAPSQEQKNLAAIQDGENIFYLAVDDIETDTELLIGYLDSDMEEEEEDLEEEQDIKDEDENSKDSKQLSADTELMIKKEDYPCLLCESSFPSEDVLAEHLQSLHNRGSAEDKEFKCRSCGKEFPVRQALQRHLLHCTESSSSSGDPSKAYQCVLCHGSFSSQSSFLQHKEACKGDERFICKAESCGKRFKSKDALKKHKGNIHIGGARRKLVCTICNKKCSSSLNLQEHRKVHEVFDCDACDKKFISTNQLKRHMITHSEKRPYTCEICSRSFKRLDQATAHKIIHSEDKPYKCKLCWKEFAHRNVYKNHKKTHSEERPFQCEECKALFRTPFSLQRHLLIHNNERTFKCDHCDATFKRKDTLNVHIQVVHDGHKKYKCDLCEKAFVTPSVLKSHKKTHTGEKEKICPYCGQKFASNGTLRVHIRSHTGERPYQCPYCDKAFSKNDGLKMHIRTHTREKPYKCSECNKAFSQKRGLDEHMRTHTGEKPFQCDVCDLSFSLKKMLIRHKLTHNPNRPMAECSLCHKKFTRNDYLKVHMENVHGETEG
Protein: Heat shock protein 90-5, chloroplastic (AtHSP90.5) (AtHsp90-5) (Heat shock protein 88-1) (Hsp88-1) (Hsp90C) (Protein EMBRYO DEFECTIVE 1956) (Protein chlorate-resistance 88) (Q9SIF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular chaperone required for chloroplast biogenesis. Essential for chloroplast biogenesis and maintenance, and thus for embryogenesis. May be involved in the disassembly of VIPP1 for thylakoid membrane formation and/or maintenance. Cooperates with TIC components and other molecular chaperones to drive transport of preproteins into chloroplasts and functions in the chloroplast stroma to facilitate membrane translocation during protein import into the organelle.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:12943545, ECO:0000269|PubMed:23382192}.
Interaction partners:
- Protein SGT1 homolog B
- Protein SGT1 homolog A
- Cysteine and histidine-rich domain-containing protein RAR1
- Peptidyl-prolyl cis-trans isomerase CYP40
- Heat shock 70 kDa protein 5
- Heat shock 70 kDa protein 4
- Heat shock protein 90-6, mitochondrial
- Endoplasmin homolog
- Protein TIC 40, chloroplastic
- Chaperonin 60 subunit alpha 1, chloroplastic
Sequence:
MAPALSRSLYTSPLTSVPITPVSSRLSHLRSSFLPHGGALRTGVSCSWNLEKRCNRFAVKCDAAVAEKETTEEGSGEKFEYQAEVSRLLDLIVHSLYSHKEVFLRELVSNASDALDKLRFLSVTEPSLLGDGGDLEIRIKPDPDNGTITITDTGIGMTKEELIDCLGTIAQSGTSKFLKALKENKDLGADNGLIGQFGVGFYSAFLVAEKVVVSTKSPKSDKQYVWESVADSSSYLIREETDPDNILRRGTQITLYLREDDKYEFAESTRIKNLVKNYSQFVGFPIYTWQEKSRTIEVEEDEPVKEGEEGEPKKKKTTKTEKYWDWELANETKPLWMRNSKEVEKGEYNEFYKKAFNEFLDPLAHTHFTTEGEVEFRSILYIPGMGPLNNEDVTNPKTKNIRLYVKRVFISDDFDGELFPRYLSFVKGVVDSDDLPLNVSREILQESRIVRIMRKRLIRKTFDMIQEISESENKEDYKKFWENFGRFLKLGCIEDTGNHKRITPLLRFFSSKNEEELTSLDDYIENMGENQKAIYYLATDSLKSAKSAPFLEKLIQKDIEVLYLVEPIDEVAIQNLQTYKEKKFVDISKEDLELGDEDEVKDREAKQEFNLLCDWIKQQLGDKVAKVQVSNRLSSSPCVLVSGKFGWSANMERLMKAQALGDTSSLEFMRGRRILEINPDHPIIKDLNAACKNAPESTEATRVVDLLYDTAIISSGFTPDSPAELGNKIYEMMAMAVGGRWGRVEEEEESSTVNEGDDKSGETEVVEPSEVRAESDPWQD
Protein: Ecto-NOX disulfide-thiol exchanger 2 (APK1 antigen) (Cytosolic ovarian carcinoma antigen 1) (Tumor-associated hydroquinone oxidase) (tNOX) [Includes: Hydroquinone [NADH] oxidase (EC 1.-.-.-); Protein disulfide-thiol oxidoreductase (EC 1.-.-.-)] (Q16206)
Organism: Homo sapiens (Human)
Function: May be involved in cell growth. Probably acts as a terminal oxidase of plasma electron transport from cytosolic NAD(P)H via hydroquinones to acceptors at the cell surface. Hydroquinone oxidase activity alternates with a protein disulfide-thiol interchange/oxidoreductase activity which may control physical membrane displacements associated with vesicle budding or cell enlargement. The activities oscillate with a period length of 22 minutes and play a role in control of the ultradian cellular biological clock.
Subcellular location: Cell membrane. Secreted, extracellular space. Note=Extracellular and plasma membrane-associated.
Interaction partners:
Sequence:
MQRDFRWLWVYEIGYAADNSRTLNVDSTAMTLPMSDPTAWATAMNNLGMAPLGIAGQPILPDFDPALGMMTGIPPITPMMPGLGIVPPPIPPDMPVVKEIIHCKSCTLFPPNPNLPPPATRERPPGCKTVFVGGLPENGTEQIIVEVFEQCGEIIAIRKSKKNFCHIRFAEEYMVDKALYLSGYRIRLGSSTDKKDTGRLHVDFAQARDDLYEWECKQRMLAREERHRRRMEEERLRPPSPPPVVHYSDHECSIVAEKLKDDSKFSEAVQTLLTWIERGEVNRRSANNFYSMIQSANSHVRRLVNEKAAHEKDMEEAKEKFKQALSGILIQFEQIVAVYHSASKQKAWDHFTKAQRKNISVWCKQAEEIRNIHNDELMGIRREEEMEMSDDEIEEMTETKETEESALVSQAEALKEENDSLRWQLDAYRNEVELLKQEQGKVHREDDPNKEQQLKLLQQALQGMQQHLLKVQEEYKKKEAELEKLKDDKLQVEKMLENLKEKESCASRLCASNQDSEYPLEKTMNSSPIKSEREALLVGIISTFLHVHPFGASIEYICSYLHRLDNKICTSDVECLMGRLQHTFKQEMTGVGASLEKRWKFCGFEGLKLT
Protein: SEC14 and spectrin domain containing 1 (C9JHW6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEASVILPILKKKLAFLSGGKDRRSGLILTIPLCLEQTNMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQWNVVKTVVVMLQNVVPAEVSLVCVVKPDEFWDKKVTHFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTEDFG
Protein: Coenzyme Q8B (M0R3F7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWLKVGGLLRGTGGQLGQTVGWPCGALGPGPHRWGPCGGSWAQKFYQDGPGRGLGEEDIRRAREARPRKTPRPQLSDRSRERKVPASRISRLANFGGLAVGLGLGVLAEMAKKSMPGGRLQSEGGSGLDSSPFLSEANAERIVQTLCTVRGAALKVG
Protein: Chitooligosaccharide deacetylase ChbG (COD) (EC 3.5.1.105) (Chitin disaccharide deacetylase) (Chitobiose deacetylase) (Chitobiose-6P deacetylase) (Chitotriose deacetylase) (Chitotriose-6P deacetylase) (P37794)
Organism: Escherichia coli (strain K12)
Function: ChbG is essential for growth on the acetylated chitooligosaccharides chitobiose and chitotriose but is dispensable for growth on cellobiose and chitosan dimer, the deacetylated form of chitobiose. Deacetylation of chitobiose-6-P and chitotriose-6-P is necessary for both the activation of the chb promoter by the regulatory protein ChbR and the hydrolysis of phosphorylated beta-glucosides by the phospho-beta-glucosidase ChbF. Catalyzes the removal of only one acetyl group from chitobiose-6-P to yield monoacetylchitobiose-6-P, the inducer of ChbR and the substrate of ChbF. It can also use chitobiose and chitotriose as substrates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22797760}.
Interaction partners:
- 6-phospho-beta-glucosidase
- HTH-type transcriptional regulator ChbR
- PTS system N,N'-diacetylchitobiose-specific EIIC component
- PTS system N,N'-diacetylchitobiose-specific EIIA component
- PTS system N,N'-diacetylchitobiose-specific EIIB component
- PTS system arbutin-, cellobiose-, and salicin-specific EIIBC component
Sequence:
MERLLIVNADDFGLSKGQNYGIIEACRNGIVTSTTALVNGQAIDHAVQLSRDEPSLAIGMHFVLTMGKPLTAMPGLTRDGVLGKWIWQLAEEDALPLEEITQELVSQYLRFIELFGRKPTHLDSHHHVHMFPQIFPIVARFAAEQGIALRADRQMAFDLPVNLRTTQGFSSAFYGEEISESLFLQVLDDAGHRGDRSLEVMCHPAFIDNTIRQSAYCFPRLTELDVLTSASLKGAIAQRGYRLGSYRDV
Protein: Homeobox protein Dlx4b (DLX-7) (Distal-less homeobox protein 4b) (Q98878)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: During larvae development, may be important for neurocranium morphogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q92988}.
Interaction partners:
Sequence:
MMSMSFMSDTLNSSDPSKSAFLEFGHGLASNQQHLSGFAHNIYPVHGLHSGGHLQHDAPYPSSAPHYSRPLGYAYPGPVSAAAPGAYMPYQPNNHSGALAHTRAENTNHEKPAVIENGEIRLNGKGKKIRKPRTIYSSVQLQALHQRFQQTQYLALPERADLAAKLGLTQTQVKIWFQNKRSKYKKIMKHGSSGPEGELLHTSSSSPCSPGLSQLWEVSMANKVPPMHPSSYMNNYGHWYPPHHQDPVPRPQMM
Protein: Chaperonin GroEL (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin-60) (Cpn60) (P0C923)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
Interaction partners:
- Co-chaperonin GroES
- Protein GrpE
- Chaperone protein DnaK
- Chaperone protein HtpG
- Heat shock protein 70
- ATP-dependent protease ATPase subunit HslU
- Glyceraldehyde-3-phosphate dehydrogenase
- Flagellar filament 41 kDa core protein
- ATP-dependent protease subunit HslV
- Thioredoxin
Sequence:
MAKDIYFNEDARKSLLSGVEKLSNAVKVTLGPKGRNVLIDKKFGSPTVTKDGVSVAREIELENPFENMGAQLLKEVAIKTNDVAGDGTTTATVLAYAIAREGLKNVSSGINPIGIKKGIDHAVNLAAEKIRQSAKKITTKEEIAQVASISANNDSYIGEKIAEAMDKVGKDGVITVEESKTFDTTISYVEGMQFDRGYLSPYFSTNKENMSVNFDDAFILIYEKKISSIKELLPVLEKVLGTNKPLLIIAEDIEGDALAALVLNSVRGALKVCAIKSPGFGDRRKAMLEDIAVLTGGVLISEELGLTLETVEIEQLGQAKTIKVDKDNTTIINTGNKEQIKERSELIKKQIEDSTSEYDKEKLQERLAKLVGGVAVINVGAVTEVELKEKKHRVEDALSATRAAVEEGVVPGGGSTLIEVAMYLDTIDTSKLSYEEKQGFEIVKRSLEEPMRQIISNAGFEGSIYIHQIKTEKKGLGFDASSFKWVNMIESGIIDPAKVTRSALQNAASIAGLLLTTECAITDIKEEKNTSGGGGYPMDPGMGMM
Protein: Large ribosomal subunit protein uL14 (50S ribosomal protein L14) (P0ADY3)
Organism: Escherichia coli (strain K12)
Function: This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.
Interaction partners:
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein bL20
- Elongation factor G
- Large ribosomal subunit protein uL30
- GTP pyrophosphokinase
- DNA-directed RNA polymerase subunit alpha
- Alternative ribosome-rescue factor A
Sequence:
MIQEQTMLNVADNSGARRVMCIKVLGGSHRRYAGVGDIIKITIKEAIPRGKVKKGDVLKAVVVRTKKGVRRPDGSVIRFDGNACVLLNNNSEQPIGTRIFGPVTRELRSEKFMKIISLAPEVL
Protein: Phosphate-binding protein PstS 1 (PBP 1) (PhoS1) (PstS-1) (38-kDa glycolipoprotein) (38-kDa lipoprotein) (P38) (Antigen Ag78) (Protein antigen B) (Pab) (P9WGU1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Functions in inorganic phosphate uptake, although probably not the main uptake protein under phosphate starvation. Binds phosphate; probably able to bind both H(2)PO(4)(-) and HPO(4)(2-). Part of the ABC transporter complex PstSACB involved in phosphate import (Probable).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305|PubMed:1906192}. Cell surface {ECO:0000269|PubMed:1612766, ECO:0000269|PubMed:25359607}. Secreted, cell wall {ECO:0000269|PubMed:10426995}. Secreted {ECO:0000305|PubMed:16622205, ECO:0000305|PubMed:1906192}. Note=A soluble cell wall-associated protein (PubMed:10426995). Also found in culture filtrate in increasing quantities during growth (PubMed:16622205, PubMed:1906192). {ECO:0000269|PubMed:10426995, ECO:0000269|PubMed:16622205, ECO:0000269|PubMed:1906192}.
Interaction partners:
- Phosphate transport system permease protein PstC 1
- Phosphate import ATP-binding protein PstB 2
- Phosphate transport system permease protein PstA 2
- Phosphate transport system permease protein PstC 2
- Phosphate transport system permease protein PstA 1
- Phosphate-binding protein PstS 2
- Phosphate import ATP-binding protein PstB 1
- Phosphate-binding protein PstS 3
- Lipoprotein LprA
- Lipoprotein LpqH
Sequence:
MKIRLHTLLAVLTAAPLLLAAAGCGSKPPSGSPETGAGAGTVATTPASSPVTLAETGSTLLYPLFNLWGPAFHERYPNVTITAQGTGSGAGIAQAAAGTVNIGASDAYLSEGDMAAHKGLMNIALAISAQQVNYNLPGVSEHLKLNGKVLAAMYQGTIKTWDDPQIAALNPGVNLPGTAVVPLHRSDGSGDTFLFTQYLSKQDPEGWGKSPGFGTTVDFPAVPGALGENGNGGMVTGCAETPGCVAYIGISFLDQASQRGLGEAQLGNSSGNFLLPDAQSIQAAAAGFASKTPANQAISMIDGPAPDGYPIINYEYAIVNNRQKDAATAQTLQAFLHWAITDGNKASFLDQVHFQPLPPAVVKLSDALIATISS
Protein: Malonyl-CoA-acyl carrier protein transacylase, mitochondrial (MCT) (EC 2.3.1.39) (Mitochondrial malonyl CoA:ACP acyltransferase) (Mitochondrial malonyltransferase) ([Acyl-carrier-protein] malonyltransferase) (Q8IVS2)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12882974}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Acyl carrier protein, mitochondrial
- Fatty acid synthase
- Acetyl-CoA carboxylase 1
- Acetyl-CoA carboxylase 2
- Small ribosomal subunit protein bS16m
- Partner and localizer of BRCA2
- GTPase Era, mitochondrial
- Small ribosomal subunit protein bS6m
- Malonate--CoA ligase ACSF3, mitochondrial
Sequence:
MSVRVARVAWVRGLGASYRRGASSFPVPPPGAQGVAELLRDATGAEEEAPWAATERRMPGQCSVLLFPGQGSQVVGMGRGLLNYPRVRELYAAARRVLGYDLLELSLHGPQETLDRTVHCQPAIFVASLAAVEKLHHLQPSVIENCVAAAGFSVGEFAALVFAGAMEFAEGLYAVKIRAEAMQEASEAVPSGMLSVLGQPQSKFNFACLEAREHCKSLGIENPVCEVSNYLFPDCRVISGHQEALRFLQKNSSKFHFRRTRMLPVSGAFHTRLMEPAVEPLTQALKAVDIKKPLVSVYSNVHAHRYRHPGHIHKLLAQQLVSPVKWEQTMHAIYERKKGRGFPQTFEVGPGRQLGAILKSCNMQAWKSYSAVDVLQTLEHVDLDPQEPPR
Protein: Vertebrate ancient long opsin b (Vertebrate ancient opsin-2) (A8YXX6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
Sequence:
MESFGFSVTESTDVTTPDDPFKGPLKSVAPWNYTFLACLMFIVTSLSITENFTVMLVTYRFKQLRKPLNYIIVNLSVADFLVSMTGGTISFLTNARGFFFLGVWACVLEGFAVTFFGIVALWSLAILAFERFFVICRPLKNVRLGGKHAAMGLIFVWTFSFIWTIPPVLGWNSYTVSKIGTTCEPNWYSTNYYDHTYIITFFVTCFILPLGVIIISYGKLMQKLRKVSNTHGRLGNARKPDREVARMVVVMIVAFMVGWTPYAAFSITVTACPTIYIDPRLGSIPAFFSKTAAVYNPIIYVFMNKQFRKCLIQMFKGNGTALESTNLNQTSDKGPITATADTHLGEMSTIAARVPMSMCNMEKSEEEEEEPEQSGNGGPKQLPLSDSRVCPL
Protein: ATPase GET3C (AtGET3C) (EC 3.6.-.-) (Guided entry of tail-anchored proteins 3 homolog C) (Q5XF80)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:28096354}.
Interaction partners:
- Protein GET4
- acid phosphatase
- Tetratricopeptide repeat
- At1g77230
- Probable ubiquitin receptor RAD23a
- Ubiquitin receptor RAD23
- Ubiquitin receptor RAD23d
- Ubiquitin receptor RAD23c
- Ubiquitin receptor RAD23b
- F9K20.24 protein
Sequence:
MAALLLLNRVSRSTSSISLHRVAGTLGFNSFNAQIHGDRISGTLFRVRSLATLAEGASHFNEMVSVNQRKYYLLGGKGGVGKTSCAASLAVKFASHGHPTIVVSTDPAHSLSDSFSQDLSGGVLKPVQGVDSPLLALEITPEIMKDEIKRQTGDKSVKNMMDSMGLGMFAGELGDLNLEDMLNAASPGIDEIAAISKVLQFMEAPEYSRFTRIVFDTAPTGHTLRLLSLPDFYDSSISKITKLKKKITAAASAFKLVFGKKEIQQKELPNELDQLKERMEKVRNVFRDVDTTEFVIVTIPTVMAINESSRLHASLRKENVPVHRLIVNQLLPQSESDCKFCSIRRKEQTRVLGLIQNDTELSGLKLIQSPLLDAEIRGVPALKFMGDLIWK
Protein: SUMO-specific isopeptidase USPL1 (EC 3.4.22.-) (Ubiquitin-specific peptidase-like protein 1) (Q3ULM6)
Organism: Mus musculus (Mouse)
Function: SUMO-specific isopeptidase involved in protein desumoylation. Specifically binds SUMO proteins with a higher affinity for SUMO2 and SUMO3 which it cleaves more efficiently. Also able to process full-length SUMO proteins to their mature forms (By similarity). Plays a key role in RNA polymerase-II-mediated snRNA transcription in the Cajal bodies (By similarity). Is a component of complexes that can bind to U snRNA genes (By similarity).
Subcellular location: Nucleus, Cajal body {ECO:0000250}.
Interaction partners:
- Desumoylating isopeptidase 1
- Small ubiquitin-related modifier 2
- Sentrin-specific protease 5
- Sentrin-specific protease 1
Sequence:
MTDDSLKIGNGLPLVGPGTDVGISSLPMLGYLGKNYASAKVTTDGHCPACRAKGKLSALKPYRISFQESVFLCEDLQCIYPLGSESLTNLISPDSEDCPTPSKPQKRKRLETNCRNSPLPVHSKKTRSHIVTDSEPIVNGKYNGEVCDDFSASFPDTSAHQDPASTAASVEQSEALEADDVVVAATEDPATVSVTSELEMPAKSRCLPLCQTLCVQWKNTQALCWLDCILSALVHLEVLRKTVLEACSREECVFGRLFEMYHQADELLHTHHLHGVTGEDCKKLTSEIFTEIDTCLNKVRDEIFAKLQPKLRCTLGDMESPVFALPVLLKLEPHVESLFTYSFSWNFECSHCGHQYQNRCVKSLVTFTNIVPEWHPLNAAHFGPCNSCNSKSQIRKMVLERASPILMLHFVEGLPRRDLQHYAFHFEGSLYQVTSVIQYQANNHFITWFLDADGSWLECDDLKGPCAKRHVTCEVPASETHIVIWERKSQVPIEEAACLPCMKPNVQPVSGEEQPTCPALCSLAGTATSEPSVAHPTSMAGAPQTLPEIQAVAHGDSVLSGAKGMVDSILPSALEETIQETASVSQVDSKDCLLEDKPVAGSAALVRVLAFQPQDSPGSSGSSLVSSLCEGKLVAPCVDSSFPSQAVSTDLQAVLSQAGDTVVPNPVTDAPVPVLVQELKSLATEKDSQTQLLPLKTEKLDPEQPGKSQASNLRKRETTASSKTVAARSAQNQPRKEDQKRAFVGSWVKGLLSRGGAFMPTCVLSQSRAVSDLQPSVKGASNFDGFKTKSISRRSKRMSRKAKHMEELSPRNSSPPLSWTAALTQAAENATSALLREQEGSRPAPLRHRSPGNESAISPASRGDAAEDQVHKLRLKLLKKLKAKKKKLAALISSPHREPSLSDHSEPASHCGTPASDQSEPVSHCGSPNDCESIEDLLKELQHQIDLADSKSGCTSAPDATSNNSQSHEEILAELLSPTAMSEPSESGELELRYLEMGDSTPAQAPSEFSVVSLNTCLKQDHDYCSPEKGQREVDLHSVMDSACIRTLNLGSPMKTDIFDDFFSTSALNSLTNDTLDIPHFDDSLFENC