wanglab/gogpt-training-data huggingface dataset:
Protein: Echinoderm microtubule-associated protein-like 4 (EMAP-4) (Restrictedly overexpressed proliferation-associated protein) (Ropp 120) (Q9HC35)
Organism: Homo sapiens (Human)
Function: Essential for the formation and stability of microtubules (MTs). Required for the organization of the mitotic spindle and for the proper attachment of kinetochores to MTs. Promotes the recruitment of NUDC to the mitotic spindle for mitotic progression.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16890222, ECO:0000269|PubMed:31409757, ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16890222}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16890222, ECO:0000269|PubMed:25789526}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:16890222, ECO:0000269|PubMed:25789526}. Midbody {ECO:0000269|PubMed:25789526}. Note=Localizes to microtubules (MTs) during interphase with a significantly reduced affinity for MTs during mitosis. {ECO:0000269|PubMed:31409757}.
Interaction partners:
- ALK tyrosine kinase receptor
- GTPase KRas
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- GTPase NRas
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- GTPase HRas
- Tyrosine-protein kinase JAK3
- Tyrosine-protein kinase JAK2
- Proto-oncogene tyrosine-protein kinase ROS
- Tyrosine-protein kinase JAK1
Sequence:
MDGFAGSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKKSVSSKGQPSPRAVIPMSCITNGSGANRKPSHTSAVSIAGKETLSSAAKSGTEKKKEKPQGQREKKEESHSNDQSPQIRASPSPQPSSQPLQIHRQTPESKNATPTKSIKRPSPAEKSHNSWENSDDSRNKLSKIPSTPKLIPKVTKTADKHKDVIINQEGEYIKMFMRGRPITMFIPSDVDNYDDIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGKIVYFIASVVVLFNYEERTQRHYLGHTDCVKCLAIHPDKIRIATGQIAGVDKDGRPLQPHVRVWDSVTLSTLQIIGLGTFERGVGCLDFSKADSGVHLCIIDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKYEKPKFVQCLAFLGNGDVLTGDSGGVMLIWSKTTVEPTPGKGPKGVYQISKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNPEREIEVPDQYGTIRAVAEGKADQFLVGTSRNFILRGTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTRLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLYVVSENGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEILYWDIPNGCKLIRNRSDCKDIDWTTYTCVLGFQVFGVWPEGSDGTDINALVRSHNRKVIAVADDFCKVHLFQYPCSKAKAPSHKYSAHSSHVTNVSFTHNDSHLISTGGKDMSIIQWKLVEKLSLPQNETVADTTLTKAPVSSTESVIQSNTPTPPPSQPLNETAEEESRISSSPTLLENSLEQTVEPSEDHSEEESEEGSGDLGEPLYEEPCNEISKEQAKATLLEDQQDPSPSS
Protein: Resuscitation-promoting factor RpfB (EC 3.-.-.-) (A0R3E0)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Active in the pM concentration range. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity (By similarity).
Interaction partners:
- Ribosomal RNA small subunit methyltransferase A
- Peptidoglycan endopeptidase RipA
- Deoxyribonuclease
- Uncharacterized protein
- Penicillin-binding protein 1A
Sequence:
MLRGVVGAFLVSLTVAGSYAVASHKTVTLSVDGAPMTVTTMKSRVIDIVEENGFEVSDRDDLFPAATETVHQSDTIVLRRSRPLEVSLDGEGTKQVWTTASTVDEALAQLRMTDKAPAAASRGSRVPLAGMALPVVSPKTVQIDDGGKVSTVHLAAPNVAGLLEAAGVPLEQNDKVVPAASSPVVDGMQIQVTRMRIEKVTERVPLAPGNERIEDPTMNMSRQVVEDPGAPGLQDVTFAIAKVNGVETGRLPVANQVIEPARNGVLRVGAKPGTEVPPVSNGHTWDALAQCEAGGNWAINTGNGFYGGVQFDQNTWERNGGLRYAPRADLATREEQIAIATVTQSRQGWGAWPVCSGRIGAR
Protein: Histone deacetylase HOS1 (EC 3.5.1.98) (Q12214)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Histone deacetylase HOS3
- Structural maintenance of chromosomes protein 3
- Probable histone deacetylase HOS2
- N-acetyltransferase ECO1
- Transcriptional regulatory protein SIN3
- HDA1 complex subunit 3
- Cohesin subunit SCC3
- Histone deacetylase HDA1
- Sister chromatid cohesion protein PDS5
- Polyamine oxidase FMS1
Sequence:
MSKLVISTSIFQSQVADLLPCNNHQKSQLTYSLINAYDLLQHFDEVLTFPYARKDDLLEFHSKSYIDYLINGRFNKMMAQDVNNPMVESKWSELSELADNWNEKIDYNPSQDLQRFTTRENLYNYYLNHSQALENNMDCINNSEVPTNDKPTDTYILNSETKQYNLEGDCPIFSYLPMYCQVITGATLNLLDHLSPTERLIGINWDGGRHHAFKQRASGFCYINDVVLLIQRLRKAKLNKITYVDFDLHHGDGVEKAFQYSKQIQTISVHLYEPGFFPGTGSLSDSRKDKNVVNIPLKHGCDDNYLELIASKIVNPLIERHEPEALIIECGGDGLLGDRFNEWQLTIRGLSRIIINIMKSYPRAHIFLLGGGGYNDLLMSRFYTYLTWCVTKQFSNLRCGDNNSFQIDPFDVCDGDDSEQFIREHDLVEMYNEENYQYWIYEMEGSSRMKMLRNDNKDRDMVELMKFYEL
Protein: BCAS3 microtubule associated cell migration factor (Breast carcinoma-amplified sequence 3 homolog) (K20D4) (Protein rudhira) (Q8CCN5)
Organism: Mus musculus (Mouse)
Function: Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin (By similarity). Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy. Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H6U6}. Cytoplasm {ECO:0000269|PubMed:16099728, ECO:0000269|PubMed:22300583}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22300583}. Preautophagosomal structure {ECO:0000250|UniProtKB:Q9H6U6}. Note=Associates with chromatin. Recruited to estrogen receptor-induced promoters in a PELP1-dependent manner (By similarity). Localizes in the cytoplasm in stationary cells. Translocates from the cytoplasm to the leading edge in motile cells. Colocalizes with microtubules and intermediate filaments in both stationary and motile cells. The BCAS3:PHAF1 complex is recruited to the preautophagosomal structures adjacent to the damaged mitochondria upon mitophagy in a PRKN-PINK1 dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9H6U6, ECO:0000269|PubMed:22300583}.
Interaction partners:
- Phagosome assembly factor 1
Sequence:
MNETMATDSPRRPSRCTGGVVVRPQAVTEQSYMESVVTFLQDVVPQAYSGSPLTEEKEKIVWVRFENADLNDTSRNLEFHELHSTGNEPPLLVMIGYSDGMQVWGIPISGEAQELFSVRHGPVRAARILPAPQLGAQKCDNFAEKRPLLGVCKSIGSSGTTPPYCCVDLYSLRTGEMVKSIQFKTPIYDLHCNKRILVVVLQEKIAAFDSCTFTKKFFVTSCYPCPGPNMNPIALGSRWLAYAENKLIRCHQSRGGACGDNIQSYTATVLSAAKTLKSGLTMVGKVVTQLTGTLPSGVTEDDVALHCNSRRSPLVPGIITVIDTETVGEGQVLVSEDSDSDGIVAHFPAHEKPVCCMAFNTSGMLLVTTDTLGHDFHVFQILTHPWSSSQCAVHHLYTLHRGETEAKVQDICFSHDCRWVVVSTLRGTSHVFPINPYGGQPCVRTHMSPRVVNRMSRFQKSAGLEEIEQELTSKQGGRCSPVPGLSSSPSGSPLHGKLTSQDSYNNFTNNNPGNPRLSPLPSLMVVTPLAQIKQPMTLGTITKRTGPYLFGAGCFSIKAPCKVKSPPQISPSKSMGGEFCVAAVFGTSRSWFANNAGLKREKDQSKQVVVESLYIISCYGTLVEHMIEPRPISTAPKISDDTPLEIMTSPRASWTLVRTPQWNELQPPFNANHPLLLAAEAVQYYQLLLAGSLPPGSPGPITRHGSYDSLASDHSGQEDEEWLSQVEIVTHTGPHRRLWMGPQFHFKTIQTSGQTTVISTSSSVLQSHGPSDTPQPLLDFDTDDLDLNSLRIQPVRSDPVSMPGSSRAVSDRRGVSTVTDAASGTFDRSVTLLEVCGSWPEGFGLRHMSSMEHSEEGLRERLADAMAESPSRDVVGSGTELQREGSIETLSNSSGSTSGSIPRNFDGYRSPLPTNESQPLSLFPTGFP
Protein: Cytochrome c oxidase subunit 5A, mitochondrial (Cytochrome c oxidase polypeptide Va) (P55954)
Organism: Caenorhabditis elegans
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:P00427}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00427}; Matrix side {ECO:0000250|UniProtKB:P00427}.
Interaction partners:
- Cytochrome c oxidase polypeptide VIIc
- COX5B-domain-containing protein
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 1
- Cytochrome c domain-containing protein
- Cytochrome oxidase c subunit VIb
- Cytochrome c oxidase subunit 6A, mitochondrial
Sequence:
MASLTRAVTRLAIAGRQAVRTIATTTPVSGHGDDIMEKWPADKFDNHFINYLNRPEIDGWEVRKALSELHDYDVIPDPKVVEAALRACRRVNDFALAVRFLEAIKIKCGAQKNRDTVYAYIVKQVEPVLKELGIDTPEQLGYGEPEFFVPEPEYWWEKKWYKDYGYDKHPNIQI
Protein: ATP-binding cassette transporter abc2 (ABC transporter abc2) (EC 7.-.-.-) (ATP-energized glutathione S-conjugate pump abc2) (Glutathione S-conjugate-transporting ATPase abc2) (Q10185)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in vacuolar sequestration of glutathione S-conjugates. Together with abc4, required for accumulation of a red pigment (ade pigment) in the vacuole of a mutant affected in the adenine biosynthetic pathway.
Subcellular location: Vacuole membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- Vacuolar heme ABC transmembrane exporter abc3
Sequence:
MVLEQDLDPFVGGNWMNSAYKGFTFLSATWLAPNIYLLISGCLQYFYEVRKRSHYFHFRRFWTIWLKSLVIMVLLFTHIYDCYKTNESVWNVLSIITYFLALFLHVVEQPTLRIPMASLLMFWLFKFLASALVLLLRPNYTMFPMLNVVPSITFFCSLVCLLAEIYVPPANRVWYPDDAAELEETGLRPSRFTYANIFSRISFGWLSPLMKFGYRNYLTESDAWSLPPAERSSNLTIVFEKNWISHAKKKKSSLYMWGVLFLNHWKLTVVIIVLKLVQDVVAFIQPNLIRKIVIFVSSYSSEHPQPPQVGFSLAIAMFLTNVVQTALLQQYFQLGMVLGMRWRSELITAIYRKSLRLSSAARQSRSVGDIVNYMSVDTQKVCDLTMFLFVIVSGPFQIVLALTNLYHLVGYGALSGAFVTFLLFPCNVVIASIFKRFQNRQMKNKDARSQFMTEIINNIRSIKLYAWENIFLQKLLQLRNTRELRMLKKIGIVNTIGNFTWLFAPILVSAATFGTFIVLYGKTRVLSVDIVFACLSLFNLLQFPLTMLPIVVSSVLEASVAISRIYGFLTAGELDSNAVQRYPANKEPSGVCLEIKKGTFSWSGPGQNAAEPTLRDIDFVARRGELCCIVGKVGMGKSSLLEACLGNMQKHSGSVFRCGSIAYAAQQPWILNATIQENILFGLELDPEFYEKTIRACCLLRDFEILADGDQTEVGEKGISLSGGQKARISLARAVYSRSDIYLLDDILSAVDQHVNRDLVRNLLGSKGLLRSRCVILSTNSLTVLKEASMIYMLRNGKIIESGSFTQLSSSPDSQLFQLLSEFSKKDTASSTGADTPLSRSQSVITSSTDVTSSASRSSDTVSNYPKATIKGTGRIRKRLTDEDNVKATGQAAEKMERGKVKWKVYWTYFKACSLFLIFLYFLFIIGGIGMNVGTNVWLKHWSEVNTQLGYNPKPYFYLGIYTLFGLLSCALISLSSLTITVFCAIKSCRYLHDSMVKAVLRAPMSFFETTPTGRILNRFSSDVYRVDEVISRVFMFFFRNLFQIVFVLAVICYSSPMFMILIVPLFFLYRYNQVYYTQTSRELKRLDSVTRSPLYAHFQESLGGLSTIRAYDMEDTFISENDIRVDTNHRIWFLYFSSNRWQAIRVEAIGALVVFSSAFFGVLSAVRGNPNSGLVGLSLSYAVQITQSLTFVVRQSVDVETNIVSVERMLEYIGLPSEAPSIIPDHRPPEGWPSHGAIKFDHYSVRYRENLPLVLNDISVNIKPQEKIGIVGRTGAGKSTLTLALFRLIEPTSGDIQLDDINITSIGLHDLRSRLAIIPQENQAFEGTIRENLDPNANATDEEIWHALEAASLKQFIQTLDGGLYSRVTEGGANLSSGQRQLMCLTRALLTPTRVLLLDEATAAVDVETDAIVQRTIRERFNDRTILTIAHRINTVMDSNRILVLDHGKVVEFDSTKKLLENKASLFYSLAKESGLI
Protein: Annexin A9 (Annexin XXXI) (Annexin-31) (Annexin-9) (Pemphaxin) (O76027)
Organism: Homo sapiens (Human)
Function: Low affinity receptor for acetylcholine known to be targeted by disease-causing pemphigus vulgaris antibodies in keratinocytes.
Interaction partners:
Sequence:
MSVTGGKMAPSLTQEILSHLGLASKTAAWGTLGTLRTFLNFSVDKDAQRLLRAITGQGVDRSAIVDVLTNRSREQRQLISRNFQERTQQDLMKSLQAALSGNLERIVMALLQPTAQFDAQELRTALKASDSAVDVAIEILATRTPPQLQECLAVYKHNFQVEAVDDITSETSGILQDLLLALAKGGRDSYSGIIDYNLAEQDVQALQRAEGPSREETWVPVFTQRNPEHLIRVFDQYQRSTGQELEEAVQNRFHGDAQVALLGLASVIKNTPLYFADKLHQALQETEPNYQVLIRILISRCETDLLSIRAEFRKKFGKSLYSSLQDAVKGDCQSALLALCRAEDM
Protein: T. brucei spp.-specific protein (Q38EH3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKLCELSPIADFIGSEVTVEDAILSSATFHMWERLYGVTSASPTPDKMRLYILQRKECNGQHEETSMSPHKSGGVSTLLRPSSPPGDASSLGGQLSAAKQRVEGPNVLKHGAIFATCGILPPSHKRTSESGSASVEWQECNMESVNRLVDVDVSSSTGTQQKKRGRSTQVFRDNRTAVPEASPSSSCATATVQAPLHLTSLYSPKVSPEGDAECVLLAPDPLYRPEVEDVFVQSCGGDTELEKPRKCVPPSNIFESLGDLRGSQRSKVLSLSEDEADECNDNIARCSVTSSLAGGDCPPQPQVSDFVALSDVLPSNQTREDVMCKGASNSVEQGYGYEPEEAAPSVRATKAYRDREDFCPNVETLPVLPSDHLECFLDEKGLRSGGGGDLGNPSSSSYLPYFTEAEEVPAQKPEQKKIRRYRTPWFCGSRAAANAAVEEVAAVKEAVCGGDASVSVVIANNSSRKSLSSASSGHSIHSKMALKEMTPQSPPTTVVFPPQEGDELQSTMEEEHRVPSLSPSPLPEIPRCGRQPLPVARTAESGSAGRGNNNFLQDDITNVQLAASTCHVEREATGFSHSLDGRALPVKHGDDEVHSAPTALNYTDGEWITESCETLKRQGMHRSDRALSSSWSPPPTQAGEFGLPKLPKSRTPARKYTYQEGDTSGVSMTSRSAGLVRRAQGRPDGGQVSADALTAGGVIGTPASGSFSSLQNKKAKLQEREARADTAATAKGTRKYVAVRTTSPQQFPLPREVTPTAKPKVNRKRDREKSE
Protein: NACHT, LRR and PYD domains-containing protein 10 (Nucleotide-binding oligomerization domain protein 8) (Q86W26)
Organism: Homo sapiens (Human)
Function: Inhibits autoprocessing of CASP1, CASP1-dependent IL1B secretion, PYCARD aggregation and PYCARD-mediated apoptosis but not apoptosis induced by FAS or BID. Displays anti-inflammatory activity. Required for immunity against C.albicans infection (By similarity). Involved in the innate immune response by contributing to pro-inflammatory cytokine release in response to invasive bacterial infection. Contributes to T-cell-mediated inflammatory responses in the skin (By similarity). Plays a role in protection against periodontitis through its involvement in induction of IL1A via ERK activation in oral epithelial cells infected with periodontal pathogens. Exhibits both ATPase and GTPase activities.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22672233}. Cell membrane {ECO:0000269|PubMed:22672233}; Peripheral membrane protein {ECO:0000305}. Note=Cytoplasmic protein which is recruited to the cell membrane by NOD1 following invasive bacterial infection. {ECO:0000269|PubMed:22672233}.
Interaction partners:
- Apoptosis-associated speck-like protein containing a CARD
- NLR family CARD domain-containing protein 4
- Caspase-1
- Beclin-1
Sequence:
MAMAKARKPREALLWALSDLEENDFKKLKFYLRDMTLSEGQPPLARGELEGLIPVDLAELLISKYGEKEAVKVVLKGLKVMNLLELVDQLSHICLHDYREVYREHVRCLEEWQEAGVNGRYNQVLLVAKPSSESPESLACPFPEQELESVTVEALFDSGEKPSLAPSLVVLQGSAGTGKTTLARKMVLDWATGTLYPGRFDYVFYVSCKEVVLLLESKLEQLLFWCCGDNQAPVTEILRQPERLLFILDGFDELQRPFEEKLKKRGLSPKESLLHLLIRRHTLPTCSLLITTRPLALRNLEPLLKQARHVHILGFSEEERARYFSSYFTDEKQADRAFDIVQKNDILYKACQVPGICWVVCSWLQGQMERGKVVLETPRNSTDIFMAYVSTFLPPDDDGGCSELSRHRVLRSLCSLAAEGIQHQRFLFEEAELRKHNLDGPRLAAFLSSNDYQLGLAIKKFYSFRHISFQDFFHAMSYLVKEDQSRLGKESRREVQRLLEVKEQEGNDEMTLTMQFLLDISKKDSFSNLELKFCFRISPCLAQDLKHFKEQMESMKHNRTWDLEFSLYEAKIKNLVKGIQMNNVSFKIKHSNEKKSQSQNLFSVKSSLSHGPKEEQKCPSVHGQKEGKDNIAGTQKEASTGKGRGTEETPKNTYI
Protein: RE66796p (Q8SYD6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRDAETKVIKKSIGDGFKIKMDDTGNIFIKRYGKSSIYVNSTSQGNEETVIGGDIIQMPQMSLTAATSARLFDMKKFQTNINREFARTYPERGRLERQCLSAVSLVKSNNNLINSPVWILVVNVVAMDMLRSRLQTIPKSLDAMGMRVPLTNSSEDPYSTIESQVGLIYPTPAASDDSQNSQHSSNSSKGRRSIFSAAFLNEGPYVPKPDYESGGSLTPIYADKKRQKSSGSQQRKKQDDPYYCGLLARIPNFIKSSKQPCPGGASKPKKEPKISRKISAQHQQQQFLQPAQPIPIATFHHSYFPYKLYPPQHRLSQSQMSLWDARSLISAHE
Protein: AT5G14540 protein (Basic salivary proline-rich-like protein (DUF1421)) (B9DHK3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At3g26990
- At3g50040
- Uncharacterized protein At4g21930
- Uncharacterized protein
- At1g44770
- At1g73210
- At5g08360
- Elongation factor
- At1g05410/T25N20_5)
- AT3g13990/MDC16_11)
Sequence:
MQSFDLIKSALFSDKQIMDLMNDNSNNSQDGDHQNYRVGDNGLESKKEAIFPSYDFQPMRPNASAGLSHHALDLAGSVNSTAARVWDASDPKPVSASSARSYGSMDSLEPSKLFAEKDRNSPESAIISAIDRTMKAHADKLLHVMEGVSARLTQLETRTRDLENLVDDVKVSVGNSHGKTDGKLRQLENIMLEVQNGVQLLKDKQEIVEAQLQLSKLQLSKVNQQPETHSTHVEPTAQPPASLPQPPASAAAPPSLTQQGLPPQQFIQPPASQHGLSPPSLQLPQLPNQFSPQQEPYFPPSGQSQPPPTIQPPYQPPPPTQSLHQPPYQPPPQQPQYPQQPPPQLQHPSGYNPEEPPYPQQSYPPNPPRQPPSHPPPGSAPSQQYYNAPPTPPSMYDGPGGRSNSGFPSGYSPESYPYTGPPSQYGNTPSVKPTHQSGSGSGAYPQLPMARPLPQGLPMASAISSGGSGGGSDSPRSGNRAPVDDVIDKVVSMGFPRDQVRGTVRTLTENGQAVDLNVVLDKLMNGDRGAMMQQQQQQPPRGWFGGR
Protein: ATP synthase F(0) complex subunit C1, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 1) (ATP synthase proteolipid P1) (ATPase protein 9) (ATPase subunit c) (Proton-conducting channel, ATP synthase F(0) complex subunit c) (Q06645)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Subcellular location: Mitochondrion membrane; Multi-pass membrane protein.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
Sequence:
MQTTKALLISPVLIRSCTRGLIRPVSASLLSRPEAPSKKPSCCSSPLQVARREFQTSVISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM
Protein: N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase (EC 2.4.1.289) (Rhamnosyltransferase WbbL) (dTDP-Rha:alpha-D-GlcNAc-pyrophosphate polyprenol, alpha-3-L-rhamnosyltransferase) (P9WMY3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacterial cell wall. Catalyzes the transfer of the rhamnosyl moiety from dTDP-rhamnosyl (dTDP-Rha) onto the decaprenyl-pyrophosphoryl-GlcNAc (C50-PP-GlcNAc), yielding rhamnosyl-decaprenyl-pyrophosphoryl-GlcNAc (Rha-C50-PP-GlcNAc).
Interaction partners:
- dTDP-4-dehydrorhamnose reductase
- Decaprenyl-phosphate N-acetylglucosaminephosphotransferase
- Galactofuranosyltransferase GlfT1
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Conserved protein
- dTDP-glucose 4,6-dehydratase
- Probable O-antigen/lipopolysaccharide transport integral membrane protein ABC transporter RfbD
- Mannose-1-phosphate guanylyltransferase
- Glucose-1-phosphate thymidylyltransferase
- Probable O-antigen/lipopolysaccharide transport ATP-binding protein ABC transporter RfbE
Sequence:
MTDVLPVVAVTYSPGPHLERFLASLSLATERPVSVLLADNGSTDGTPQAAVQRYPNVRLLPTGANLGYGTAVNRTIAQLGEMAGDAGEPWVDDWVIVANPDVQWGPGSIDALLDAASRWPRAGALGPLIRDPDGSVYPSARQMPSLIRGGMHAVLGPFWPRNPWTTAYRQERLEPSERPVGWLSGSCLLVRRSAFGQVGGFDERYFMYMEDVDLGDRLGKAGWLSVYVPSAEVLHHKAHSTGRDPASHLAAHHKSTYIFLADRHSGWWRAPLRWTLRGSLALRSHLMVRSSLRRSRRRKLKLVEGRH
Protein: Drosophila CRumBs homolog (Q19350)
Organism: Caenorhabditis elegans
Interaction partners:
- FERM domain-containing protein
- Protein kinase C-like 3
- Cell division control protein 42 homolog
Sequence:
MKYQHFLIFCTLVTNALCNRACSRNTCLNGGTCTVNDETRMFQCECPKGFSGLLCQDNCSLHCLHGNCVKGTFGEETCQCSEGWMGSLCDNLVTDDDTAQKCSPQCGDDERCTKGADGSYICQSNEPSCATHTCQNNGTCVAENGNVKCACPPGFVGDHCETDEDECKENFCQNGADCENLKGSYECKCLKGFSGKYCEIQDKKQCTSDYCHNNGQCISTGSDLSCKCSPGFDGAFCELKAEVNECICENPAHVCSLVNGTSRTTQCECPSGFMGADCKELQARPCDREPCLNGGHCVDDGQNLFTCFCLPSFTGIYCGEPVDCLVNGSDCKNGGKCVFALAATTCQCPEGFNGSNCEISNSYRSHPTCSDIRCLNGGSCKLDAEGEPFCVCEEGFDGPFCEPKSGCTINPCQNGGTCQDADGQYFCHCTSGFGGVHCETVDEPSTPIPTLGTFPSFTTSGIDGFSQSKISCEDCVNSSNCLDVESGPVCICDDGYFGQKCDQKHDKCSKVSCPSGQTCSQVNDNVNITAQCGCEIGHFGQQCEMVTSATFSAKSLYIHQSSKFSLGTSSFENIAYELEFSFRTTVENTHLASSENILGEKILSIQLLSGYLVFNMTGNSLEHLLPMRVSDAQWYTVFVKGEDNKIQIEVSTENGFSLVQKSVNGQLEVFLTRFGKISGTHHFIGCMADVRVDGDLIIFADNKRAIDIRKGCTRSEQCTRAYCQNEGICIDHWESSSCKCKPPYLKPNCVYFLPKTTFGHLDQPSIVHLSTSESENHLLRNHIELSFLMHSGKPDAVLFYIGEKHAADVLTNYLVVKIAGGLITVRYRTGGRREIEFSSKNRVDDNQEHHVQIFLDKTTRQIIIDDLIECSEPIISRMSQEFYVDDIVIGASNVVATDSEFYKGYLQDIQINQKSVVIHPTSLTIDKIGKLERTQNVIEGAVSDPMCSSSTCKHGECSETFNDFTCRCSDGSTGKLCDKVDYCKDASCMKGSRCENADNGHYCIFPITISNGSMLTYSLAPTKFMTLPSIEFSIKAHSQNGHIFTLTIDKSTLSAYLFKKRLALATNSGSGTIQKFDSVIADGNWHQIILNPHKVLIDSVKFISDNQLYPAESKSGASLFVGEQEPQEVTFACLDLFKMGEYPTLSFTKVKIPTNSETWNLTDKASVGTGCMSTDQCGLYSTCLNGATCVDIWNKRKCVCPAGFAGENCEDNVNDCKFVDCGKHGYCLDGIDEAKCICNNGFHGEHCELAKDECEGVECHNGGKCVKNRSEKIVCQCGNSWMGDSCNVTKTTNCKDSPCQNFGQCMQKTDTFFECNCMDGYSGELCEQRDVNECNHYDCNRGHCVMTVSGPACQCEMGYTGRFCEKLLNQCSSNTCSSRGACSPVWNNTVCNCDNNWRGAHCQHQMDTCLDFPCNNDGVCRTNDENTFSCECQKFFMGTRCEIEGSCLKAQCVHGECIQLSPETHTCSCNIGYEGDACDKKIDYCKAGPCLNGANCENKLTGYKCTCAVGFEGADCEINIDECALEFCKNGAKCRDKINDYECVCDGTGFEGRNCTTDINECANPNNCINGECTNTLGNYKCACRNGFIGPRCSVRNPCTAQIASNNISSVTCVHGKCVNPVVQIEKNREVAKYECACDRGYTGPTCSQRIKESAMSNISYLFGPIIAVVIVFAILGCLLLFFVIRGNNAMHGHYSPSSHEFTQNRMAMPTVIKLPPQERLI
Protein: AT3g28220/T19D11_3 (TRAF-like family protein) (Q9LHA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ubiquitin fusion degradation UFD1 family protein
- At2g29070
- Putative ubiquitin-dependent proteolytic protein
- non-specific serine/threonine protein kinase
- Trihelix transcription factor DF1
- Probable E3 ubiquitin-protein ligase RHA1A
- Membrane-anchored ubiquitin-fold protein 4
Sequence:
MSEKGLIKKEDHMFQEEKRKTNYGAIGLACFISCFFAFQFMKIVTTQPSTTTTSSIAVIDSPMSSHKLSDRREIWRVIPPSTYCLKIESFIKFATSPNAEKYESRPFESGGYNWTLIVYPKGNIKEGAPLNYVSMYVQIDNSTLLNSPKEVYAEVKFFIYNRKEDKYLTYQETDAKRFFLFKPYWGYGNVRPYTDVANPNAGWLFDGDNVLFGVDVFVTEVFNKWEVFSFTKSLHDRLYKWTLPNFSSLEKQYYVSDKFVIGGRSWALKVYPSGDGEGQGNSLSLYVVAVDVKPYDKIYLKAKLRIINQRDSKHMEKKVESWSDQANSWGFQKFVPFADLKDTSKGLLVNDTLKMEIEFEDFSNTKYFPS
Protein: Protein ALUMINUM SENSITIVE 3 (ABC transporter I family member 16) (ABC transporter ABCI.16) (AtABCI16) (ybbM homolog protein) (Q9ZUT3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for aluminum (Al) resistance/tolerance, probably by translocating Al from sensitive tissues such as growing roots to tissues less sensisitive to the toxic effects of Al.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15659095}; Multi-pass membrane protein {ECO:0000269|PubMed:15659095}.
Interaction partners:
- ABC transporter I family member 17
- Protein SENSITIVE TO PROTON RHIZOTOXICITY 1
- Aluminum-activated malate transporter 1
- Protein DETOXIFICATION 42
- Protein SENSITIVE TO PROTON RHIZOTOXICITY 2
- ABC transporter-like protein
- At4g10470
- Magnesium transporter MRS2-10
- ABC transporter B family member 27
- ABC transporter I family member 1
Sequence:
MDLKWDDFFNDYEWLIVFLKGMVKPAAALVVVLLAVILSYSQNLSLEGEMIYSVSRSFLQLSVIGFVLQFIFNQENSGWIILAYLFMVSVAGYTAGQRARHVPRGKYVAGLSILAGTSITMFLLVLLNVFPFTPRYMIPIAGMLVGNAMTVTGVTMKQLRDDIKMQLNLVETALALGATPRQATLQQVKRALVISLSPVLDSCKTVGLISLPGAMTGMIMGGASPLEAIQLQIVVMNMMVGAATVSSITSTYLCWPSFFTKAYQLQTHVFSSD