wanglab/gogpt-training-data huggingface dataset:
Protein: Probable AP endonuclease (APE) (EC 3.1.21.-) (pE296R) (Q65202)
Organism: African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)
Function: Endonuclease of the viral base excision repair system that catalyzes DNA cleavage reaction at the apurinic or apyrimidinic sites (AP sites). Cleaves phosphodiester bonds on the 5' side of AP sites. In addition to endonuclease activity, the AP endonuclease has a proofreading 3'-5' exonuclease activity that is considerably more efficient in the elimination of a mismatch than in that of a correctly paired base. Displays 3'-phosphatase and 3'-repair diesterase activities. The single nucleotide gaps generated by the AP endonuclease are filled by the viral repair DNA polymerase X and the DNA ligase (Probable).
Subcellular location: Host nucleus {ECO:0000269|PubMed:16641276}. Host cytoplasm {ECO:0000269|PubMed:16641276}. Virion {ECO:0000269|PubMed:30185597}. Note=The early enzyme is localized in the nucleus and the cytoplasm, while the late protein is found only in the cytoplasm (PubMed:16641276). Found in association with viral nucleoid (PubMed:30185597). {ECO:0000269|PubMed:16641276, ECO:0000269|PubMed:30185597}.
Interaction partners:
Sequence:
MFGAFVSHRLWSDSGCTTTCITNSIANYVAFGEQIGFPFKSAQVFIAGPRKAVINIQEDDKVELLKMIVKHNLWVVAHGTYLDVPWSRRSAFVTHFIQQELLICKEVGIKGLVLHLGAVEPELIVEGLKKIKPVEGVVIYLETPHNKHHTYKYSTMEQIKELFLRIRNTRLKQIGLCIDTAHIWSSGVNISSYNDAGQWLRSLENIHSVIPPSHIMFHLNDAATECGSGIDRHASLFEGMIWKSYSHKIKKSGLYCFVEYITRHQCPAILERNLGSSMQLQTALTAEFTTLKSLLK
Protein: V-type proton ATPase subunit d (V-ATPase subunit d) (V-ATPase 39 kDa subunit) (V-ATPase subunit M39) (Vacuolar proton pump subunit d) (O13753)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector (By similarity). Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores (By similarity).
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:P32366}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32366}.
Interaction partners:
- V-type proton ATPase subunit F
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit a
- V-type proton ATPase subunit c
- V-type proton ATPase subunit H
- Probable V-type proton ATPase 20 kDa proteolipid subunit
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- V-type proton ATPase subunit B
- V-type proton ATPase catalytic subunit A
Sequence:
MDALSFNTNSGYIEALVRGYESALLEQHIYSNLSQCESLEDFRLQLSSTDYGGFLANQSKLTSSIISAKATEKLLDEFDLIRRQADETLSKFMDYITYAYMIDNIMLLLTGTVNGQDTHDLLERCHPLGWFETLPALCVATNVEELYSVVLIETPLAPYFKDCLSADDLDEQHIEIIRNTLYKAYLEDFYNFCKKIGACTADTMLPILEFEADRRAITITINSFGTELSKEERAKMYPSFGRLYPFSTSILARAENAGDVENACSLVKEYSDFFDQNSQKSLDDHFNEKEVELNKLAFLQQFHYGIVYAFLKLREQEIRNLTWIAECISQNQRDRALNIVPIL
Protein: Mucolipin 1 variant (Q53HA8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004107}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004155}.
Interaction partners:
Sequence:
MTAPAGPRGSETERLLTPNPGYGTQAGPSPAPPTPPEEEDLRRRLKYFFMSPCDKFRAKGRKPCKLMLQVVKILVVTVQLILFGLSNQLAVTFREENTIAFRHLFLLGYSDGADDTFAAYTREQLYQAIFHAVDQYLALPDVSLGRYAYVRGGGDPWTNGSGLALCQRYYHRGHVDPANDTFDIDPMVVTDCIQVDPPERPPPPPSDDLTLLESSSSYKNLTLKFHKLVNVSIHFRLKTINLQSLINNEIPDCYTFSVLITFDNKAHSGRIPISLETQAHIQECKHPSVFQHGDNSFRLLFDVVVILTCSLSFLLCARSLLRGFLLQNEFVGFMWRQRGRVISLWERLEFVNGWYILLVTSDVLTISGTIMKIGIEAKNLASYDVCSILLGTSTLLVWVGVIRYLTFFHNYNILIATLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFAAMQAQQGRSSLVWLFSQLYLYSFISLFIYMVLSLFIALITGAYDTIKHPGGAGAEESELQAYIAQCQDSPTSGKFRRGSGSACSLLCCCGRDPSEEHSLLVN
Protein: Alpha-1,4 glucan phosphorylase (EC 2.4.1.1) (Q5ZME4)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MAAPLSDGERRKQISVRGIAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTVRDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIIDGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHSPEGVKWVDTQVVLAMPYDTPVPGYKNNTVNTMRLWSAKAPNDFNLQEFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCQDPVRTSFETFPDKVAIQLNDTHPALSIPELMRILVDVEKVDWDKAWEITKQTCAYTDHTVLPEALERWPVSMFEKLLPRHLEIIYALNQMHLDRVAALYPGDVDRLRRTSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSDIVKNTVFKDFYELEPEKFQNKTNGITPRRWLLLCNPGLADVIAEKIGEDFVTDLSQLKKLLDFINNETFIRDVAKVKQENKLKFSAYLEERYKVKINPSSMFDIQVKRIHEYKRQLLNCLHAITLYNRIRSDPSKSFVPRTIMIGGKAAPGYHMAKMIIKLITSIGEVVNNDPYVGDKLKVIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRVEEVEALDRRGYNAREYYDRIPELRQAIDQISSGFFSPRDPGCFRDVVNMLMHHDRFKVFADYEAYIKCQGQVDQLFMDPREWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSATKIPPPNLPRD
Protein: Cytosolic carboxypeptidase 1 (EC 3.4.17.-) (EC 3.4.17.24) (ATP/GTP-binding protein 1) (Nervous system nuclear protein induced by axotomy protein 1) (Protein deglutamylase CCP1) (Q641K1)
Organism: Mus musculus (Mouse)
Function: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of alpha-tubulin as well as non-tubulin proteins such as MYLK. Involved in KLF4 deglutamylation which promotes KLF4 proteasome-mediated degradation, thereby negatively regulating cell pluripotency maintenance and embryogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9UPW5}. Cytoplasm, cytosol {ECO:0000269|PubMed:11083920}. Nucleus {ECO:0000269|PubMed:11083920}. Mitochondrion {ECO:0000269|PubMed:20620870}. Note=Localizes in both the cytoplasm and nuclei of interphase and dividing cells. {ECO:0000250|UniProtKB:Q9UPW5}.
Interaction partners:
- Polyglutamylase complex subunit TTLL1
Sequence:
MSKLKVVGEKSLTNSSRVVGLLAQLEKINTDSTESDTARYVTSKILHLAQSQEKTRREMTTKGSTGMEVLLSTLENTKDLQTVLNILSILIELVSSGGGRRASFLVAKGGSQILLQLLMNASKDSPPHEEVMVQTHSILAKIGPKDKKFGVKARVNGALTVTLNLVKQHFQNYRLVLPCLQLLRVYSTNSVNSVSLGKNGVVELMFKIIGPFSKKNSGLMKVALDTLAALLKSKTNARRAVDRGYVQVLLTIYVDWHRHDNRHRNMLIRKGILQSLKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSSFHFQLPIIPVTGPVAQLYSLPPEVDDVVDESDDNDDIDLEVENELENEDDLDQSFKNDDIETDINKLRPQQVPGRTIEELKMYEHLFPELVDDFQDYELISKEPKPFVFEGKARGPIVVPTAGEEVPGNSGSVKKGVVMKERASPKGEEAKEDPKGHDRTLPQQLGGQSRVAPSAHSFNNDLVKALDRITLQNVPSQVASGLNAGMRKDFGLPLTVLSCTKACPHVAKCGSTLFEGRTVHLGKLCCTGVETEDDEDTESHSSTEQAPSVEASDGPTLHDPDLYIEIVKNTKSVPEYSEVAYPDYFGHIPPPFKEPILERPYGVQRTKIAQDIERLIHQNDIIDRVVYDLDNPTYTTPEEGDTLKFNSKFESGNLRKVIQIRKSEYDLILNSDINSNHYHQWFYFEVSGMRPGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALNARPWWIRMGTDICYYKNHFSRSSVAAGGQKGKSYYTITFTVNFPHKDDVCYFAYHYPYTYSTLQMHLQKLESAHNPQQIYFRKDVLCETLSGNICPLVTITAMPESNYYEHICQFRTRPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMYGCSIKETVWHTHDNSASCDIVEDMGYRTLPKILSHIAPAFCMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGCDQGRYKGLQIGTRELEEMGAKFCVGLLRLKRLTSSLEYNLPSNLLDFENDLIESSCKVTSPTTYVLDEDEPRFLEEVDYSAESNDELDVELAENTGDYEPSAQEEALSDSEVSRTHLI
Protein: beta-hydroxyaspartate dehydratase (EC 4.2.1.-) (A1B8Z2)
Organism: Paracoccus denitrificans (strain Pd 1222)
Function: Catalyzes the dehydration of (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate) into iminosuccinate. Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC).
Interaction partners:
- L-aspartate--glyoxylate aminotransferase
- Iminosuccinate reductase
- 3-hydroxy-D-aspartate aldolase
- Acetolactate synthase small subunit
- Threonine synthase
- 3-isopropylmalate dehydrogenase
- Tryptophan synthase beta chain
- Acetolactate synthase, large subunit
- Acetolactate synthase, large subunit
- Acetolactate synthase
Sequence:
MYIPTYEDMLAAHERIKPHIRRTPIRTSDYLNELTGAQLFFKCENFQEPGAFKVRGATNAVFGLDDAQAAKGVATHSSGNHASCLSYAAMLRGIPCNVVMPRTAPQAKKDTVRRYGGVITECEPSTSSREETFAKVQAETGGDFVHPYNDPRVIAGQGTCAKELVEQVDGLDAVVAPIGGGGMISGTCLTLSTLAPETRVIAAEPEQADDAYRSFKAGYIIADDAPKTVADGLLVPLKDLTWHFVKNHVSEIYTASDAEIVDAMKLIWKHLRIVMEPSSAVPLATILKNPEAFAGKRVGVIVTGGNVDLDKLPWN
Protein: Rho GDP-dissociation inhibitor 1 (Rho GDI 1) (GDI-1) (Rho-GDI alpha) (Q99PT1)
Organism: Mus musculus (Mouse)
Function: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23434736}.
Interaction partners:
- Transforming protein RhoA
- Cell division control protein 42 homolog
- Tumor necrosis factor receptor superfamily member 16
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 1
- Rho-related GTP-binding protein RhoC
- RIKEN cDNA 4930544G11 gene
- RAC-alpha serine/threonine-protein kinase
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVAVSADPNVPNVIVTRLTLVCSTAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPMEEAPKGMLARGSYNIKSRFTDDDKTDHLSWEWNLTIKKEWKD
Protein: Probable eukaryotic initiation factor 4A (EC 3.6.4.13) (ATP-dependent RNA helicase eIF4A) (Q384E1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Probable eukaryotic initiation factor 4A
- Pescadillo homolog
Sequence:
MRALRCVRRGVYRQSVRLCYFMSLECSLRPITGASARLLCRFTAPTWPRKNEVEEGDVGTTESTSQDVRSIFRSNIETHSEVSLESSASPALPPKTAALDVSVLDSKGNAVPVNPVKLFSDLDNLPDWLSKGLQSSGFSCTTPIQSYTIPVLDEGHDMIGLAPTGSGKTVAFAVPALKKFQWSPNGSPRIVVLAPTRELVQQTAKVFHQLSSGKVRVCEAYGGAPREAQARRLHNGCDVLVACPGRLKDFLQNGDVIFDEVSFLVFDEADRLLDMGFKVQLDDILGYFSSHRPAQTMMWSATWPPVVEQLAQEYLSQNRYVIRSGTAGTGLQVNENIKQHIFFADAPEERVKTLVSLIKEGKIDENTAKMMIFVERQTDTENAAYALARMLGIHSRCIGVVHGGMQQRQRDHIMGIFKEGRIRILVATDVASRGLDFPDVTCVVNLIAPKNIDSYCHRIGRTGRAGRTGESFTFIGRSDGSLAKDLINYLEKCGMDVPQRLVEFAEEHAQGEEIKRMKRPWRGRQQREGRSQSRGGREPAPRDSGW
Protein: Rifin (Q8I2B9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHYSKILLFSLPLNILVTSSYAHNKNKPSITPHHTPITTSRVLSECDLYMPKYDNDADMKSVKGTFDRQASQRFEEYEERIKDKRQKRKEERDKNIQEIIEKDRKDKSFAEKVEKGCLRCGCGLGGVAASIGLFGGLGIYAWRSAALVTAIQKGIEASVEAGEAAGTKAGKEFVIAALQKMGIFTVGDQRLVSYFSTTDYTSALKISSDIIQKYDPSSCFFDFSGARETFCTWVKVKSDAAVNVERSTVSTNALVEKAVGTIVTDAKTVVERAVETATDEAIQRSIGVVDAKYAICQTAIIASVVAILVIVLVMMIIYLILRYRRKKKMKKKDQYTKLLNE
Protein: Molybdopterin synthase catalytic subunit (EC 2.8.1.12) (MPT synthase subunit 2) (Molybdenum cofactor biosynthesis protein E) (Molybdopterin-converting factor large subunit) (Molybdopterin-converting factor subunit 2) (P30749)
Organism: Escherichia coli (strain K12)
Function: Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD.
Interaction partners:
- Cyclic pyranopterin monophosphate synthase
- Molybdopterin synthase sulfur carrier subunit
- Molybdenum cofactor biosynthesis protein B
- GTP 3',8-cyclase
- Molybdopterin adenylyltransferase
- Molybdopterin molybdenumtransferase
- Molybdopterin-synthase adenylyltransferase
- Sulfur carrier protein ThiS adenylyltransferase
- Molybdopterin-guanine dinucleotide biosynthesis adapter protein
- Sulfur carrier protein TusA
Sequence:
MAETKIVVGPQPFSVGEEYPWLAERDEDGAVVTFTGKVRNHNLGDSVNALTLEHYPGMTEKALAEIVDEARNRWPLGRVTVIHRIGELWPGDEIVFVGVTSAHRSSAFEAGQFIMDYLKTRAPFWKREATPEGDRWVEARESDQQAAKRW
Protein: Rho guanine nucleotide exchange factor 9 (Collybistin) (Rac/Cdc42 guanine nucleotide exchange factor 9) (A0A5F9ZHY9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MQWIRGGSGMLITGDSIVSAEAVWDHVTMANRELAFKAGDVIKVLDASNKDWWWGQIDDEEGWFPASFVRLWVNQEDEVEEGPSDVQNGHLDPNSDCLCLGRPLQNRDQMRANVINEIMSTERHYIKHLKDICEGYLKQCRKRRDMFSDEQLKVIFGNIEDIYRFQMGFVRDLEKQYNNDDPHLSEIGPCFLEHQDGFWIYSEYCNNHLDACMELSKLMKDSRYQHFFEACRLLQQMIDIAIDGFLLTPVQKICKYPLQLAELLKYTAQDHSDYRYVAAALAVMRNVTQQINERKRRLENIDKIAQWQASVLDWEGEDILDRSSELIYTGEMAWIYQPYGRNQQRVFFLFDHQMVLCKKDLIRRDILYYKGRIDMDKYEVVDIEDGRDDDFNVSMKNAFKLHNKETEEIHLFFAKKLEEKIRWLRAFREERKMVQEDEKIGFEISENQKRQAAMTVRKVPKQKGVNSARSVPPSYPPPQDPLNHGQYLVPDGIAQSQVFEFTEPKRSQSPFWQNFSRLTPFKK
Protein: Actin (Q2UUP3)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Actin-related protein 4
- Actin-related protein RO7
- CAP-Gly domain-containing protein
- Actin-related protein 2
- F-actin-capping protein subunit beta
- Actin/actin family protein
- RuvB-like helicase
- Uncharacterized protein
- Actin-related protein 2/3 complex subunit
- Actin-related protein 2/3 complex subunit 3
Sequence:
MAEATLHNAPIVIDNGSGTIRAGFAGEEVPSCFFPSFVGRPKHPRVMAGGLEGDVFIGSRAQELRGLLKIRYPLEHGIVTDWDDMEKIWHYVYENELKTLPEEHPVLLTEPPLNPRKNRDTAAQIMFETFNVPALYTSIQAVLSLYASGRTTGVVLDSGDGVSHAVPVYEGFAIPNSIRRIDVAGRDVTEQLQLLLRKNGHVLYTSAEKEVVRKIKEEVCYVSLDPKREEKEWMNSYHKSETKAVDYRLPDGHKIKIGQERYRAPEILFDPELIGLEYPGVHQIVQDAITRTDLDLRKDLYLNIVLSGGSTLCKNFPDRLMREIKRLAVEDMKIRISAPAERKYTTWIGGGILAGLSTFRKMWVSADEWHEDPEIIHRKFA
Protein: Cytochrome c oxidase subunit 3 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide III) (P14575)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00420}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00420}.
Interaction partners:
- ATP synthase subunit a
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome b
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
Sequence:
MNLSTKFQGHPYHIVSASPWPFFLSVVLFFNCLAATLYLHGYKHSSVFFGISFLGLLATMYLWFRDMSTEANIHGAHTKAVTKGLKIGFMLFLISETFLFASIFWAFFHSSLSPTFELGAVWPPVGIADKTIDPLEVPLLNTVILLTSGASLTYAHYSLIARNRENALKGLYMTIALSFLFLGGQAYEYWNAPFTISDSVYGASFYFATGLHGIHIIVGTILLLAATYNIYTYHLTNTHHNGFECGIYYWHFCDVVWLFLYLTIYIWGS
Protein: CHP-rich zinc finger protein-like (Cysteine/Histidine-rich C1 domain family protein) (Q9FHQ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEKIELPIHKHPLLPITRFFSRHGCNGCGSDGYIYGGYHCNELGCETPAFHRECAESLQEIKHFSHPDHPLNLRLNDKASTCNRCGIHLLRKTYIYVCSICDFKLDLHCAKDAAPLPILENYNLHEHPLKLFDVSKSLKRVRLRECKTCDSPFLIEKLCYICYQCKILFHASCAEFFPEANHTSHPQHPLKLLKFAEAPDYADKKCLLCDEKFDQDQGLHHCDVCNFSICRACMKNPPPVGVESPTTHEHQLHLVPRRIHFTCNACGTLGEQSPYFCLQCNFMIHRQCIDLPRVININRHDHRISYTRRIRHGKGICKVCRKMVDGFYGGYICVKCLSFAIHARCATREDVWEMVELEGTPEEDEIGPFEVIDDNTIKHFSHDHNLRINNDGDGQILHENIVCEACALQILSEPFYSCKQCNFKLHQKCANHPRKKHHVYRNLPFTLLTSGNEIFQCWLCLQEFNGFMYQSGHYVIDVRCAAISDTLEYKSHQHSLYYYSTTYTHCSRCGKKDSVFRCDECDYGLGGKCAILPGKVMNNRYDDHPLFLSFDEMNVDGEYWCEACETKVNSKEWFYTCNDCGTTLHISCVVGDFSYIKHGSHLMNTKVVSNTSICRPFCFVCNSRCKLPSILKLSKGGVNVYICSFKCRLETY
Protein: Carbonic anhydrase (EC 4.2.1.1) (Carbonate dehydratase) (P27134)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation, supplies CO(2) to RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) in the carboxysome (Probable). Loss of activity results in limitation of CO(2) availability to RuBisCO located in the cytoplasm.
Subcellular location: Carboxysome {ECO:0000269|PubMed:17675289, ECO:0000269|PubMed:20304968, ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:28616951, ECO:0000269|PubMed:31048338}. Note=This cyanobacterium makes beta-type carboxysomes (PubMed:22928045). Associates with the shell portion of carboxysomes (By similarity). {ECO:0000250|UniProtKB:Q54735, ECO:0000269|PubMed:22928045}.
Interaction partners:
- Carboxysome assembly protein CcmM
- carbonic anhydrase
- Cyanate hydratase
- Similar to plant sulfate transporter
Sequence:
MRKLIEGLRHFRTSYYPSHRDLFEQFAKGQHPRVLFITCSDSRIDPNLITQSGMGELFVIRNAGNLIPPFGAANGGEGASIEYAIAALNIEHVVVCGHSHCGAMKGLLKLNQLQEDMPLVYDWLQHAQATRRLVLDNYSGYETDDLVEILVAENVLTQIENLKTYPIVRSRLFQGKLQIFGWIYEVESGEVLQISRTSSDDTGIDECPVRLPGSQEKAILGRCVVPLTEEVAVAPPEPEPVIAAVAAPPANYSSRGWLAPEQQQRIYRGNAS
Protein: Growth-regulated alpha protein (C-X-C motif chemokine 1) (Cytokine-induced neutrophil chemoattractant 1) (CINC-1) (Platelet-derived growth factor-inducible protein KC) (P14095)
Organism: Rattus norvegicus (Rat)
Function: Has chemotactic activity for neutrophils. Contributes to neutrophil activation during inflammation.
Subcellular location: Secreted.
Interaction partners:
- C-X-C chemokine receptor type 2
- C-X-C chemokine receptor type 1
- C-X-C chemokine receptor type 4
- Macrophage inflammatory protein-1 alpha receptor
- C-X-C motif chemokine 10
- C-X-C motif chemokine 2
- C-C motif chemokine 2
- C-C motif chemokine 5
- C-X-C motif chemokine 5
- Transcription factor Jun
Sequence:
MVSATRSLLCAALPVLATSRQATGAPVANELRCQCLQTVAGIHFKNIQSLKVMPPGPHCTQTEVIATLKNGREACLDPEAPMVQKIVQKMLKGVPK
Protein: Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) (Protein zwischenferment) (P12646)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P11413}.
Interaction partners:
- 6-phosphogluconate dehydrogenase, decarboxylating
- Glucose-6-phosphate isomerase
- Probable 6-phosphogluconolactonase
- Phosphoglucomutase 1
- Pyruvate dehydrogenase E1 component subunit alpha
- Triosephosphate isomerase
- Probable transaldolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Glyceraldehyde-3-phosphate dehydrogenase 2
Sequence:
MATQKEDHTALDLIIKSLKSPTMVCEGTHFDGKIPHTFVIFGASGDLAKKKIYPTLWWLYRDDLLPKPTKFCGYARSMLTVDSIKEQCLPYMKVQPHEQKKYEEFWALNEYVSGRYDGRTGFELLNQQLEIMENKNKANRIFYLALPPSVFEEVTVNIKQICMSVCGWNRVIIEKPFGRDDASSQALSDHLAGLFQEDQLYRIDHYLGKEMVQNLMTIRFGNKILSSTWNRENIASVLITFKEPFGTQGRGGYFDEFGIIRDVMQNHLLQILSLVAMEKPVSCHPDDIRDEKVKVLKSIEALTLDDMVLGQYLGNPQGTNDDARTGYVEDPTVSNDSNTPTYALGVLKINNERWQGVPFILRCGKALNERKAEVRIQYQDVPGDIFEGNTKRNELVIRVQPGEALYFKMMTKSPGITFDIEETELDLTYEHRYKDSYLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPILHQIEKEHIRPITYQYGSRGPKEADRKCEENNFKYSGSYKWHGGKAATSNH
Protein: Deoxynucleotidyltransferase terminal-interacting protein 2 (Estrogen receptor-binding protein) (LPTS-interacting protein 2) (LPTS-RP2) (Terminal deoxynucleotidyltransferase-interacting factor 2) (TdIF2) (TdT-interacting factor 2) (Q5QJE6)
Organism: Homo sapiens (Human)
Function: Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein.
Subcellular location: Nucleus {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.
Interaction partners:
- rRNA-processing protein FCF1 homolog
- Probable U3 small nucleolar RNA-associated protein 11
- Something about silencing protein 10
- U3 small nucleolar RNA-associated protein 6 homolog
- Neuroguidin
- WD repeat-containing protein 46
- WD repeat-containing protein 36
- Protein AATF
- U3 small nucleolar ribonucleoprotein protein MPP10
- WD repeat-containing protein 43
Sequence:
MVVTRSARAKASIQAASAESSGQKSFAANGIQAHPESSTGSDARTTAESQTTGKQSLIPRTPKARKRKSRTTGSLPKGTEPSTDGETSEAESNYSVSEHHDTILRVTRRRQILIACSPVSSVRKKPKVTPTKESYTEEIVSEAESHVSGISRIVLPTEKTTGARRSKAKSLTDPSQESHTEAISDAETSSSDISFSGIATRRTRSMQRKLKAQTEKKDSKIVPGNEKQIVGTPVNSEDSDTRQTSHLQARSLSEINKPNFYNNDFDDDFSHRSSENILTVHEQANVESLKETKQNCKDLDEDANGITDEGKEINEKSSQLKNLSELQDTSLQQLVSQRHSTPQNKNAVSVHSNLNSEAVMKSLTQTFATVEVGRWNNNKKSPIKASDLTKFGDCGGSDDEEESTVISVSEDMNSEGNVDFECDTKLYTSAPNTSQGKDNSVLLVLSSDESQQSENSENEEDTLCFVENSGQRESLSGDTGSLSCDNALFVIDTTPGMSADKNFYLEEEDKASEVAIEEEKEEEEDEKSEEDSSDHDENEDEFSDEEDFLNSTKAKLLKLTSSSIDPGLSIKQLGGLYINFNADKLQSNKRTLTQIKEKKKNELLQKAVITPDFEKNHCVPPYSESKYQLQKKRRKERQKTAGDGWFGMKAPEMTNELKNDLKALKMRASMDPKRFYKKNDRDGFPKYFQIGTIVDNPADFYHSRIPKKQRKRTIVEELLADSEFRRYNRRKYSEIMAEKAANAAGKKFRKKKKFRN
Protein: Homologous-pairing protein 2 winged helix domain-containing protein (Q585V2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Mnd1 HTH domain-containing protein
Sequence:
MASKKGGKKANGEDLEAAILRWFECEGEPATVQSLTDALGSKFGKQLVQNTLEQCLKEQKLLAKDIKKARFYFLASPAPGSNDEGSDVGSHKIDIVKQLRQLRNGVSMLSSELSVLLQAQTSSKRATTIASLVSECAALRSRLQALHVIAGKESSCVSDDVSLLIHRYKRARELWRDRKRITVCVIDAVLGDSCGPQELEDIFGLSTDEQMNLCLSGTALTLPATVSS
Protein: Fcgbp protein (Q8R1G8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
AAYTAACQAAGAAVKPWRTDSVCPLQCPAHSHYSICTRSCQGSCAALSGLTGCTTRCFEGCECDDHFLLSHGVCIPAQDCGCVHNGQYMPVNSSLMSSDCSERCFCSPNNGLTCHEAGCPSGHVCEIQAGVRECQAARGLCSISVGANLTTFDGAHNAISSPGVYELSSRCPGLQKNVPWYRVLADVQPCHNNDKIVSKVHIFFQDGLVTVIPSKGAWVNGLRVDLPATVLTSVSVRRMPDGSMLVHQKAGVTVWLGKDGLLDVMVGDDLAAMLCGACGNFDGDQTNDAYGSQGKTPIEKWRAQDFSPCSN
Protein: Uncharacterized protein YnhF (A5A618)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:19121005, ECO:0000305|PubMed:21778229}; Single-pass membrane protein {ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:21778229}. Note=May be able to insert into the membrane in both orientations.
Interaction partners:
- Cytochrome bd-I ubiquinol oxidase subunit X
- Cytochrome bd-I ubiquinol oxidase subunit 1
- Cytochrome bd-I ubiquinol oxidase subunit 2
- Cytochrome bo
- Cytochrome bo
- Cytochrome bo
- Cytochrome bo
- Inner membrane transport protein YdhP
- Cytochrome bd-II ubiquinol oxidase subunit 2
- Uncharacterized protein YshB
Sequence:
MSTDLKFSLVTTIIVLGLIVAVGLTAALH