wanglab/gogpt-training-data huggingface dataset:
Protein: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 (6PF-2-K/Fru-2,6-P2ase 2) (PFK/FBPase 2) (6PF-2-K/Fru-2,6-P2ase heart-type isozyme) (RH2K) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] (Q9JJH5)
Organism: Rattus norvegicus (Rat)
Function: Synthesis and degradation of fructose 2,6-bisphosphate.
Interaction partners:
- Fructose-1,6-bisphosphatase isozyme 2
- Hexokinase-2
- Fructose-1,6-bisphosphatase 1
- Hexokinase-3
- RCG30218, isoform CRA_b
- ATP-dependent 6-phosphofructokinase, liver type
- ATP-dependent 6-phosphofructokinase, platelet type
- ATP-dependent 6-phosphofructokinase, muscle type
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
- RAC-alpha serine/threonine-protein kinase
Sequence:
MSENSTFSTEDSSSSSYKPHASNLRRAGKKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQCALVALEDVKAYFTEESGQIAVFDATNTTRERRDMILNFAKQNAFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNRENVMEDFLKRIECYKVTYQPLDPDNYDKDLSFIKVMNVGQRFLVNRVQDYIQSKIVYYLMNIHVHPRTIYLCRHGESEFNLLGKIGGDSGLSLRGKQFAQALKKFLEEQEIQDLKVWTSQLKRTIQTAESLGVTYEQWKILNEIDAGVCEEMTYSEIEQRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHIIFKLTPVAYGCKVETITLNVEAVDTHRDKPTHNFPKSQTPVRMRRNSFTPLSSSNTIRRPRNYSVGSRPLKPLSPLRALDMQEGADQPKTQVQQGSAQATEHLQKALEFANGHREVENVLAKHRRPSMASLTLLS
Protein: SH3 and cysteine-rich domain-containing protein (Src homology 3 and cysteine-rich domain-containing protein) (P97306)
Organism: Mus musculus (Mouse)
Function: Promotes expression of the ion channel CACNA1H at the cell membrane, and thereby contributes to the regulation of channel activity. Plays a minor and redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity. Slows the rate of calcium-mediated inactivation of CACNA1C calcium channel activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29467163}. Cell membrane {ECO:0000269|PubMed:29467163}; Peripheral membrane protein {ECO:0000269|PubMed:29467163}; Cytoplasmic side {ECO:0000269|PubMed:29467163}. Cell membrane, sarcolemma {ECO:0000269|PubMed:29363593}; Peripheral membrane protein {ECO:0000269|PubMed:29363593}; Cytoplasmic side {ECO:0000269|PubMed:29363593}.
Interaction partners:
Sequence:
MIPPSGAREDSGDGLTGEATGTEQPPSPASTSSLESKLQKLKRSLSFKTKSLRSKSADNFFPRTNSDVKPQADLLAKASPGPSPIAIPGSPASMPTKAGLHPGSNSKLHAFQEHVFKKPTFCDVCNHMIVGTHAKHGLRCGACKMSIHHKCADGLAPQRCMGKLPKGFRRYYSSPLLIHEQFGCIKEVMPIACGNKVDPVYEALRFGTSLAQRTKKGGSGSGSDSPPRTSTSELVDVPEEADGPGDGSDMRTRSNSVFTYPENGMDDFRDQMKTTNHQGPLSKDPLQMNTYVALYRFIPQENEDLEMRPGDMITLLEDSNEDWWKGKIQDRVGFFPANFVQRVEEHEKIYRCVRTFIGCKDQGQITLKENQICVTSEEEQDGFIRVLSGKKRGLVPLDVLVDV
Protein: LIM domain-containing protein WLIM2a (Widely-expressed LIM protein 2) (AtWLIM2) (O04193)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to actin filaments and promotes cross-linking into thick bundles. Has an actin-stabilizing activity. The actin regulatory activities are not regulated by pH and [Ca(2+)].
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20817848}.
Interaction partners:
- Uncharacterized GPI-anchored protein At5g19230
- LIM domain protein
- Uncharacterized GPI-anchored protein At5g19240
- Zinc finger CCCH domain-containing protein 52
- Protein DA1-related 1
- Protein DA1-related 7
- Propionyl-CoA carboxylase
- Uncharacterized GPI-anchored protein At5g19250
- Uncharacterized GPI-anchored protein At3g06035
- Expansin-A13
Sequence:
MSFTGTQQKCRACEKTVYPVELLSADGISYHKACFKCSHCKSRLQLSNYSSMEGVVYCRPHFEQLFKESGSFSKNFQSPAKPLTDKPTPELNRTPSRLAGMFSGTQDKCATCTKTVYPIEKVTVESQCYHKSCFKCSHGGCPISPSNYAALEGILYCKHHFAQLFKEKGSYNHLIKSASIKRATAAATAAAAAVAAVPES
Protein: Uncharacterized protein F08B12.4 (Q19191)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPVEQDGLTGGRGVPHPNSAAGQALSGKTGGSSVPHPNSAAGQALSGGMTGGSAVPHPNSAAGQELTNKNLEEKSVLEGGTQVKPWLKNQPDLANIREQNHQ
Protein: Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Methylglyoxal synthase) (EC 4.2.3.3) (Triose-phosphate isomerase) (P48500)
Organism: Rattus norvegicus (Rat)
Function: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Glucose-6-phosphate isomerase
- glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Fructose-bisphosphate aldolase A
- Phosphoglycerate kinase 1
- Fructose-bisphosphate aldolase
- Transaldolase
- Phosphoglycerate kinase
- Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
Sequence:
MAPSRKFFVGGNWKMNGRKKCLGELICTLNAAKLPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWCKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ
Protein: KNL (Kinetochore null) Binding Protein (Q95QB8)
Organism: Caenorhabditis elegans
Interaction partners:
- Kinetochore NuLl
- Outer kinetochore KNL1 complex subunit knl-1
Sequence:
MTTPSPQEISTVTLNSLSKEERKKAILALQTKKNEIKLVIDEHQKKLAEFRQSIPDGCCEMFENEKKIRLKHSSTAELLPHLQKVGSSSVDKEKMINNIRQRVEVQVADQETFKSIEERNELLRRENENLKKEVNTVAAELLQEFESYE
Protein: Fez family zinc finger protein 1 (Zinc finger protein 312B) (A0PJY2)
Organism: Homo sapiens (Human)
Function: Transcription repressor. Involved in the axonal projection and proper termination of olfactory sensory neurons (OSN). Plays a role in rostro-caudal patterning of the diencephalon and in prethalamic formation. Expression is required in OSN to cell-autonomously regulate OSN axon projections. Regulates non-cell-autonomously the layer formation of the olfactory bulb development and the interneurons. May be required for correct rostral migration of the interneuron progenitors (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19318583}.
Interaction partners:
Sequence:
MDSSCHNATTKMLATAPARGNMMSTSKPLAFSIERIMARTPEPKALPVPHFLQGALPKGEPKHSLHLNSSIPCMIPFVPVAYDTSPKAGVTGSEPRKASLEAPAAPAAVPSAPAFSCSDLLNCALSLKGDLARDALPLQQYKLVRPRVVNHSSFHAMGALCYLNRGDGPCHPAAGVNIHPVASYFLSSPLHPQPKTYLAERNKLVVPAVEKYPSGVAFKDLSQAQLQHYMKESAQLLSEKIAFKTSDFSRGSPNAKPKVFTCEVCGKVFNAHYNLTRHMPVHTGARPFVCKVCGKGFRQASTLCRHKIIHTQEKPHKCNQCGKAFNRSSTLNTHTRIHAGYKPFVCEFCGKGFHQKGNYKNHKLTHSGEKQFKCNICNKAFHQVYNLTFHMHTHNDKKPFTCPTCGKGFCRNFDLKKHVRKLHDSSLGLARTPAGEPGTEPPPPLPQQPPMTLPPLQPPLPTPGPLQPGLHQGHQ
Protein: Rac-like GTP-binding protein RAC13 (Q41253)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Function: Could participate in a signal transduction pathway that controls cytoskeletal organization.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with the membrane when activated.
Interaction partners:
- Protein LOL2-like
- Protein LOL2-like
- Kinesin-like calmodulin-binding protein
- Kinesin-like calmodulin-binding protein
- Protein TIME FOR COFFEE-like
- Guanine nucleotide exchange factor SPIKE 1-like
- Guanine nucleotide exchange factor SPIKE 1-like
- Protein NAP1-like isoform X1
- RING-type E3 ubiquitin transferase
- RING-type E3 ubiquitin transferase
Sequence:
MSTARFIKCVTVGDGAVGKTCMLISYTSNTFPTDYVPTVFDNFSANVVVDGSTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLISKASYENIYKKWIPELRHYAHNVPVVLVGTKLDLRDDKQFLIDHPGATPISTSQGEELKKMIGAVTYIECSSKTQQNVKAVFDAAIKVALRPPKPKRKPCKRRTCAFL
Protein: dihydropyrimidinase (EC 3.5.2.2) (Q2XST3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTSPKPVKKVPIHLQSAQNRVYIKNGEIVNHDKSFKADVYIEDGIIKFVGPSSEITIPGGVRTIDASGLMIIPGGIDPHTHMQLPFGGAVAVDDFYHGTKAAVAGGTTMIIDFVLPNKHESMIEAYDKWRSWADPKVCCDYGLHVGITWWSKSVSEEIGILCKELGVNSFKTFMAYKGLYQLNDSDLLDVFERIRHLNGVAMVHAENGDIIAKNTQRLLAEGINGPEGHELSRPEEVEAEAVHRACVLAHQMKTPLFVSGLTSKSSAELVGRARRSGYCVFGETLASSLGRSMSAVPKGDRIYAITSPPIRESAETPRQLMKSLAYDDLQLTGSDNCTFNKEHKALGKGDFTKIPNGVNGVEDRMSLVWEKGVHAGLLDPCRFVAVTSTNAAKIFNIYPQKGRIAVGSDAVIVIWNPNATRTISKDTHHHACDFNIFEGMTVHGVCEFVLVRGRICAERGNVRVAEGFGRFIPTPVRPPFVYDIIEGKVQSQPEEQHEEKQNGSMAKRFAELDIQIPVQEPISAMLAGNLAMPAEGSLCSTPSVRGRVDGKRDLQESSFSISEELDRSGVRACIKVKNPPGGKSSGFW
Protein: Probable tetraacyldisaccharide 4'-kinase, mitochondrial (EC 2.7.1.130) (Protein LIPID X 4'-kinase) (AtLpxK) (Q8LEA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21709257}.
Interaction partners:
- Probable UDP-3-O-acylglucosamine N-acyltransferase 1, mitochondrial
- Probable lipid-A-disaccharide synthase, mitochondrial
- Probable UDP-3-O-acylglucosamine N-acyltransferase 2, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 5, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 2, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 3, mitochondrial
- Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial
- Probable 3-deoxy-D-manno-octulosonic acid transferase, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 1, mitochondrial
- Is a member of the PF|00364 Biotin-requiring enzymes family
Sequence:
MEKLRKVVNEIAYTRVHTNSPALHRSLVPFLTIASSLYGVALQIRRSLYRYSLLQKHRLPVPVISVGNLSWGGNGKTPMVEYISQFLVDSGLTPLILTRGYAGGDEVKMLERHLRGGPVKIGVGANRAATAALFLDKYGCVDSSSLRSFFDLHERAQVWTISEKIGCIILDDGMQHWSLSRDLEIVMLNGLNPWGNGHLMPHGPLREPLLALERADVAVVHHVDLITKQSLRDIENMIQGFKKSIPIFYSKMVPKYLFDVKNARSHVALEALRCASVLCVSAIGSADAFVKSIEMTGAHYVDRLDFSDHHLFEAEDVETMSRRAKGLEHKSNCKPIIVVTEKDYDRDPEILKCLDSYTVLVLCSELQITPILETDVDSFNYTLMKALAAKFYVSS
Protein: Hexaprenyl-diphosphate synthase large subunit ((2E,6E)-farnesyl-diphosphate specific) (HexPS) (EC 2.5.1.83) (Hexaprenyl diphosphate synthase) (Hexaprenyl pyrophosphate synthetase) (O66129)
Organism: Micrococcus luteus (Micrococcus lysodeikticus)
Function: Catalyzes the condensation of three molecules of isopentenyl diphosphate with farnesyl diphosphate (FPP) to yield (all-E)-hexaprenyl diphosphate (HexPP; C30), the precursor of the prenyl side chain of menaquinone-6. Large subunit Hexs-B catalyzes the condensation reaction and the final product chain length is cooperatively regulated by both the Hexs-A and Hexs-B subunits using the whole size of the hydrophobic cleft as a ruler.
Interaction partners:
Sequence:
MIALSYKAFLNPYIIEVEKRLYECIQSDSETINKAAHHILSSGGKRVRPMFVLLSGFLNDTQKDDLIRTAVSLELVHMASLVHDDYIDNSDMRRGNTSVHIAFDKDTAIRTGHFLLARALQNIATINNSKFHQIFSKTILEVCFGEFDQMADRFNYPVSFTAYLRRINRKTAILIEASCHLGALSSQLDEQSTYHIKQFGHCIGMSYQIIDDILDYTSDEATLGKPVGSDIRNGHITYPLMAAIANLKEQDDDKLEAVVKHLTSTSDDEVYQYIVSQVKQYGIEPAELLSRKYGDKAKYHLSQLQDSNIKDYLEEIHEKMLKRVY
Protein: RING-type domain-containing protein (O16684)
Organism: Caenorhabditis elegans
Interaction partners:
- RING-type domain-containing protein
Sequence:
MSKVIECEICNLEFSSVNEDQVPRILKCGHSVCQCCATKLLKNSAISCPFCRETTSVSAVKDLQKNFALLQIIEHTKTERVEEEDEADVPPKCATHKYNMAEFVCLDPNCSSDEKLMCRTCEEFGVHAGHSKGLLQTEALKLRTLLKDKLLKSEDQIVQIDKNIEEVDSAQQTNQVDGKVFQDKKDLISVYYTSIRETLDAQEALANQKLREIAESNSASNKLLLEELSESLETQKLKNEKLKSFLGMSNADLLALNSEIQLWDDSENTEVEPIQFDVALNFPEVNRLAVDVANASMSSSLEPDNITLWL
Protein: Stearoyl-[acyl-carrier-protein] 9-desaturase 5, chloroplastic (Stearoyl-ACP desaturase 5) (EC 1.14.19.2) (Acyl-[acyl-carrier-protein] desaturase 5) (Q9M879)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481}.
Interaction partners:
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Acyl carrier protein 5
- 3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic
- AT4g26130/F20B18_240
- 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic
Sequence:
MAMAMDRIVFSPSSYVYRPCQARGSRSSRVSMASTIRSATTEVTNGRKLYIPPREVHVQVKHSMPPQKLEIFKSLEGWADETLLTYLKPVEKSWQPTDFLPEPESEGFYDQVKELRERCKELPDDYFVVLVGDMITEEALPTYQTMLNTLDGVRDETGASPTPWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPKTENNPYLGFIYTSFQERATFISHGNTARLAKDRGDLKLAQICGTIAADERRHETAYTKIVEKLFEIDPDGTILGLADMMKKKISMPAHLMYDGQDDNLFEHFSTVAQRLGVYTAKDYADILEFLVERWNVETLTDLSSEGHRAQDFVCGLPARIRKIEERAQGRAKEAAKNIPFSWIFGRNIRA
Protein: AT5g61910/k22g18_30 (DCD (Development and Cell Death) domain protein) (Q8VZG6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
METEMDFSDGEQTNGNSHVTASQYFAPPGYNRSLVAAYGNGNTTIGLEKGIERRLDHHEQLPGYIFMCNGRTKTDCYRYRVFGIPRGGKDVVESIKPGMKLFLYDFEKRLLYGVYEATVGGRLDIEPEAFEGKYPAQVGFRIVMNCLPLTENTFKSAIYENYKGSKFKQELSPHQVMSLLSLFRSFTSPELDLLPHRLASRASAPRTLSFEERFIAATHLRNASSVLDPLSARHVEPRLGSVMAHQPVPRTSLLQHSYFRQDDYTTPPRESLSNLNQPYYPTEARQLRLLGDPSRSDSPRSEPPRSSIQDPQLKYLTILSNIRRYGSASDRLASENEYHPATPSEKDQFAVPYSDNKNYPSTLSGSEHPSASAANGSVYRSEFYNSASQKEGEASQQHEIPAGTYHHPEASTVSNTTKSMQPDMQAVSVAQSHTETAGYPTPAHGEASQPPAGAIGYTHQPQSVAGNYSTHSQPGNVEESTQSYAGTDSYSQQQYYAAMGPTTQLHAGGYIQKPHEIGYSQQPHDAATGYSQQPHDAATGYSQQPHDAATGYSQQPHAASTGYSQQTYAAATGYTQQPHAAAAGYTQQPHAAATGYSQQPHAAATAHAQQPYAAATAHAQQLHAVATGYALQLHAAATGYAQQPHAAATGYALQPHAQAVEYTMQPHAQAVGYMPQYHAHAVVYSQQGVTQGSVPRAPGTTDCNAANQAYSATGDWNAVHQSYYPQTADATTTYYQTS
Protein: Placenta-specific protein 9 (Q5JTB6)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- EMILIN-1
Sequence:
MRPLLCALTGLALLRAAGSLAAAEPFSPPRGDSAQSTACDRHMAVQRRLDVMEEMVEKTVDHLGTEVKGLLGLLEELAWNLPPGPFSPAPDLLGDGF
Protein: Interleukin-12 subunit beta (IL-12B) (Cytotoxic lymphocyte maturation factor 40 kDa subunit) (IL-12 subunit p40) (Q62712)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU281113}.
Interaction partners:
Sequence:
MCHQKLTFSWFAMVLLVSPLMAMWELEKDVYVVEVDWRPDAPGETVTLTCDSPEEDDITWTSDQRRGVIGSGKTLTITVREFLDAGQYTCHRGGETLSHSHLLLHKKENGIWSTEILKNFKNKTFLKREAPNYSGRFTCSWLVHRNTDLKFNIKSSSSSPESRAVTCGAASLSAEKVTLNQRDYEKYSVACQEDVTCPTAEETLPIELVVEAQQQNKYENYSTSFFIRDIIKPDPPKNLQVKPLKNSQVEVSWEYPDSWSTPHSYFSL
Protein: Endoplasmin homolog (92 kDa phosphoprotein) (Glucose-regulated protein 94 homolog) (GRP-94 homolog) (Q9NKX1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May play a role in late differentiation as well as in starvation response. When overexpressed, suppresses the ability to form normal fruiting bodies and impairs prespore differentiation as well as maturation into spores.
Subcellular location: Endoplasmic reticulum. Golgi apparatus. Note=In prespore cells, preferentially localizes in Golgi vesicles and cisternae. Colocalizes with trap1 in the prespore-specific vacuole.
Interaction partners:
- Protein SGT1 homolog
- Calreticulin
- Luminal-binding protein 1
- Luminal-binding protein 2
- Calnexin
- Activator of 90 kDa heat shock protein ATPase homolog
- Heat shock 70 kDa protein, mitochondrial
- J domain-containing protein
- Heat shock factor-type DNA-binding domain-containing protein
- CS domain-containing protein
Sequence:
MKSITKIFLILGLFAFLLVAFAPSSSVATVNLESDGYTEAEAKLIEEKGEKFTFQTEVNKLMNIIINSLYSKKEIFLRELISNASDALDKIRFLALTNADLLGEGEQSNLDIHIKIDKANNVLHITDRGVGMTKDELVRNLGTIAQSGTKEFIKKVSDSAESSNLIGQFGVGFYSLFLVADSVVVTSKSNDDDQYVWTSDSQSSYTIAKDPKGNTLGRGTRISLHIKDDSKEFLDQEVIKQLVKKYSQFINFPIYLYVSEEVEIPKEEQEDSKPITDDQVEETTTTTEEGEEETTTEEEGQTEEKKTKTVYKWEELNDSKPLWMKAAKDVTKEEYTEFFRSLSKTQDTPITYSHFKTEGDTEFRSILYIPENPPSNMFDLEAAGSGLKLFVRRVFITDNLKELVPNWLRFLVGVIDSDDLPLNVSREMLQQNKILDAIKKKVILVKFISMIKELSEDEDKTKYNEFFKKFGSSMKLGAIEDQANKKRLTKYLLFPSSKEELTTFAGYVERMKEGQDQIYFITGKSKDSVEASPLIEQAIKKGYEVLFLVDPIDEYLVPQLDKFDDKYKFTNLARSGVKFNEDKEEEDQRKQTAEEFKPLLSYLKKTLSDKLEKVVISKVLADSPSILVSNSWGVTANQERIMKAQAHQANAQPQFNSKKIMEINPSHPLIKKLLNRLNEFGEEDETTKVSAHVLYETSALTAGYSIDNPTNFADFIYKLMMINGDSLAQTNFETTKNENSGPSVSFGDDDENQQQDFQQPPQSTHDEL
Protein: Dynein regulatory complex protein 8 (EF-hand calcium-binding domain-containing protein 2) (Q5VUJ9)
Organism: Homo sapiens (Human)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8J3A0}.
Interaction partners:
Sequence:
MLGPGQVRLRPRVWRDKAGGRVADGASGLPPARGSWRETGTGRALGASSPPRPAQGSSSPGIQSGPSSRPGSPRGAEQAGTPRPRLSLGISQATGSAARWRTRRTGKGLGYNSDEIRPRTLLIEHLMEGGRRDHHTMTVLWGTQEIIVAEFHKKIKEAFEVFDHESNNTVDVREIGTIIRSLGCCPTEGELHDLIAEVEEEEPTGYIRFEKFLPVMTEILLERKYRPIPEDVLLRAFEVLDSAKRGFLTKDELIKYMTEEDGVSLRRPG
Protein: Type II secretion system core protein G (T2SS core protein G) (General secretion pathway protein G) (PilD-dependent protein PddA) (Q00514)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Core component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Pseudopilin (pilin-like) protein that polymerizes to form the pseudopilus. Further polymerization triggers pseudopilus growth. Type II pseudopilus confers increased bacterial adhesive capabilities.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:17172336, ECO:0000269|PubMed:8331069}; Single-pass membrane protein {ECO:0000255}. Note=Translocation to the cell inner membrane is independent of the presence of other Xcp components but depends on a functional Sec apparatus. {ECO:0000269|PubMed:17172336}.
Interaction partners:
- Type II secretion system protein J
- Type II secretion system protein K
- Type II secretion system protein I
- Type II secretion system protein E
- Type II secretion system protein H
- Type II secretion system protein F
- Secretin XcpQ
- Type II secretion system protein L
- Type II secretion system protein M
- Type II secretion system protein N
Sequence:
MQRRQQSGFTLIEIMVVVVILGILAALVVPQVMSRPDQAKVTVAKGDIKAIAAALDMYKLDNFAYPSTQQGLEALVKKPTGNPQPKNWNKDGYLKKLPVDPWGNPYQYLAPGTKGPFDLYSLGADGKEGGSDNDADIGNWDN
Protein: Sodium/hydrogen exchanger 9B2 (Na(+)/H(+) exchanger NHA2) (Na(+)/H(+) exchanger-like domain-containing protein 2) (NHE domain-containing protein 2) (Sodium/hydrogen exchanger-like domain-containing protein 2) (Solute carrier family 9 subfamily B member 2) (Q86UD5)
Organism: Homo sapiens (Human)
Function: Na(+)/H(+) antiporter that extrudes Na(+) or Li(+) in exchange for external protons across the membrane. Contributes to the regulation of intracellular pH, sodium homeostasis, and cell volume. Plays an important role for insulin secretion and clathrin-mediated endocytosis in beta-cells (By similarity). Involved in sperm motility and fertility (By similarity). It is controversial whether SLC9B2 plays a role in osteoclast differentiation or not (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18000046, ECO:0000269|PubMed:36177733}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Apical cell membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Note=Strong colocalization with LAMP1 and TCIRG1 in osteoclasts. In beta-cells colocalizes with RAB4A and SYP. Localizes to the basolateral membrane of polarized osteoclasts. {ECO:0000250|UniProtKB:Q5BKR2}.
Interaction partners:
- Sodium/hydrogen exchanger 5
- Sodium/hydrogen exchanger 6
- Sodium/hydrogen exchanger 2
- Sodium/hydrogen exchanger 1
- Sodium/hydrogen exchanger 7
- Sodium/hydrogen exchanger 8
- Sodium/hydrogen exchanger 9
Sequence:
MGDEDKRITYEDSEPSTGMNYTPSMHQEAQEETVMKLKGIDANEPTEGSILLKSSEKKLQETPTEANHVQRLRQMLACPPHGLLDRVITNVTIIVLLWAVVWSITGSECLPGGNLFGIIILFYCAIIGGKLLGLIKLPTLPPLPSLLGMLLAGFLIRNIPVINDNVQIKHKWSSSLRSIALSIILVRAGLGLDSKALKKLKGVCVRLSMGPCIVEACTSALLAHYLLGLPWQWGFILGFVLGAVSPAVVVPSMLLLQGGGYGVEKGVPTLLMAAGSFDDILAITGFNTCLGIAFSTGSTVFNVLRGVLEVVIGVATGSVLGFFIQYFPSRDQDKLVCKRTFLVLGLSVLAVFSSVHFGFPGSGGLCTLVMAFLAGMGWTSEKAEVEKIIAVAWDIFQPLLFGLIGAEVSIASLRPETVGLCVATVGIAVLIRILTTFLMVCFAGFNLKEKIFISFAWLPKATVQAAIGSVALDTARSHGEKQLEDYGMDVLTVAFLSILITAPIGSLLIGLLGPRLLQKVEHQNKDEEVQGETSVQV
Protein: Decorin-binding protein A (O50917)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Binds to decorin which may mediate the adherence of B.burgdorferi to collagen fibers in skin and other tissues.
Interaction partners:
Sequence:
MIKCNNKTFNNLLKLTILVNLLISCGLTGATKIRLERSAKDITDEIDAIKKDAALKGVNFDAFKDKKTGSGVSENPFILEAKVRATTVAEKFVIAIEEEATKLKETGSSGEFSAMYDLMFEVSKPLQKLGIQEMTKTVSDAAEENPPTTAQGVLEIAKKMREKLQRVHTKNYCTLKKKENSTFTDEKCKNN
Protein: Energy-coupling factor transporter transmembrane protein EcfT (ECF transporter T component EcfT) (Q9X2I1)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:23359690}; Multi-pass membrane protein {ECO:0000305|PubMed:23359690}.
Interaction partners:
- Energy-coupling factor transporter ATP-binding protein EcfA2
- Energy-coupling factor transporter ATP-binding protein EcfA1
- Biotin transporter BioY
- Oligopeptide ABC transporter, ATP-binding protein
- tRNA pseudouridine synthase A
- ATP-dependent protease LA, putative
- Riboflavin transporter RibU
Sequence:
MRLPTVLIGRYIPVDSIVHRLDPRAKLLGMIFLISAVLIVPNLLFYLVPGLAIFLLMFLSRTGFKIYLAGLRSLWFFLVFAVLVQFFSSSEGEKIFWMITDRAIWSAVYIMLRLVLIILLAENFSATTPPLLSARAIESIFSTFGARKIGHEIGMVMTIAMRFVPVLALEADRILKAQIARGANFERGKFFDRIRALVVIIVPLLISALRKAEELAVAMEARLYTGEPPKTRFKDIKWKPMDTLYVLLTAGVLVLVLFGRYFVDGVFQYGS