wanglab/gogpt-training-data huggingface dataset:
Protein: Long chain acyl-CoA synthetase 2 (EC 6.2.1.3) (Protein Botrytis resistant 1) (Protein LATERAL ROOT DEVELOPMENT 2) (Q9XIA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Acts in the cutin pathway. Preferentially uses palmitate, palmitoleate, oleate and linoleate. Required for repression of lateral root formation through its role in cutin biosynthesis and subsequent aerial tissues permeability.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:20237894}.
Interaction partners:
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Cytochrome P450 86A2
- Glycerol-3-phosphate 2-O-acyltransferase 4
- Probable lysophospholipase BODYGUARD 1
- Probable acyl-CoA dehydrogenase IBR3
- Peroxisomal acyl-coenzyme A oxidase 1
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Acyl-coenzyme A oxidase 2, peroxisomal
Sequence:
MSLAADNVLLVEEGRPATAEHPSAGPVYRCKYAKDGLLDLPTDIDSPWQFFSEAVKKYPNEQMLGQRVTTDSKVGPYTWITYKEAHDAAIRIGSAIRSRGVDPGHCCGIYGANCPEWIIAMEACMSQGITYVPLYDSLGVNAVEFIINHAEVSLVFVQEKTVSSILSCQKGCSSNLKTIVSFGEVSSTQKEEAKNQCVSLFSWNEFSLMGNLDEANLPRKRKTDICTIMYTSGTTGEPKGVILNNAAISVQVLSIDKMLEVTDRSCDTSDVFFSYLPLAHCYDQVMEIYFLSRGSSVGYWRGDIRYLMDDVQALKPTVFCGVPRVYDKLYAGIMQKISASGLIRKKLFDFAYNYKLGNMRKGFSQEEASPRLDRLMFDKIKEALGGRAHMLLSGAAPLPRHVEEFLRIIPASNLSQGYGLTESCGGSFTTLAGVFSMVGTVGVPMPTVEARLVSVPEMGYDAFSADVPRGEICLRGNSMFSGYHKRQDLTDQVLIDGWFHTGDIGEWQEDGSMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIAQIWVYGNSFESFLVGVVVPDRKAIEDWAKLNYQSPNDFESLCQNLKAQKYFLDELNSTAKQYQLKGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLQHYKGIVDQLYSEAKRSMA
Protein: Facilitated trehalose transporter Tret1 (BmTRET1) (A9ZSY3)
Organism: Bombyx mori (Silk moth)
Function: High-capacity facilitative transporter for trehalose. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20035867}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:20035867}.
Interaction partners:
Sequence:
MEMEIKDENLRNSVPFVRQLSTDSVKTKTEYDNEDGTPYKSTTQKLFLWTQLLAAFAVSVGSMNVGFSSGYTSPAVLTMNITLDITKEEITWVGGLMPLAALVGGIVGGPLIEYLGRKKTIMGTAVPFTIGWMLIANAINVVMVFAGRVICGVCVGIVSLAFPVYIGETIQPEVRGALGLLPTAFGNTGILLAFLVGSYLDWSNLAFFGAAIPVPFFLLMILTPETPRWYVSKARVQEARKSLRWLRGKNVNIEKEMRDLTISQTESDRTGGNAFKQLFSKRYLPAVMISLGLMLFQQLTGINAVIFYAASIFQMSGSSVDENLASIIIGVVNFISTFIATMLIDRLGRKVLLYISSVAMITTLLALGAYFYLKQNHIDVTAYGWLPLACLVIYVLGFSIGFGPIPWLMLGEILPSKIRGTAASLATGFNWTCTFIVTKTFQNIIDAIYMHGTLWLFAVICIGGLLFVIFFVPETKGKSLEEIEMKLTSGSRRVRNISKQPENIC
Protein: P protein (Melanocyte-specific transporter protein) (Pink-eyed dilution protein homolog) (Q04671)
Organism: Homo sapiens (Human)
Function: Contributes to a melanosome-specific anion (chloride) current that modulates melanosomal pH for optimal tyrosinase activity required for melanogenesis and the melanosome maturation. One of the components of the mammalian pigmentary system. May serve as a key control point at which ethnic skin color variation is determined. Major determinant of brown and/or blue eye color. Seems to regulate the post-translational processing of tyrosinase, which catalyzes the limiting reaction in melanin synthesis (By similarity).
Subcellular location: Melanosome membrane {ECO:0000269|PubMed:25513726, ECO:0000269|PubMed:7601462}; Multi-pass membrane protein {ECO:0000269|PubMed:7601462}.
Interaction partners:
- Myosin-binding protein H
- Tyrosinase
- Aminomethyltransferase, mitochondrial
- Membrane-associated transporter protein
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Sodium/potassium/calcium exchanger 5
- Glycine cleavage system H protein, mitochondrial
- Melanocyte-stimulating hormone receptor
- Glycine dehydrogenase
- Low molecular weight phosphotyrosine protein phosphatase
Sequence:
MHLEGRDGRRYPGAPAVELLQTSVPSGLAELVAGKRRLPRGAGGADPSHSCPRGAAGQSSWAPAGQEFASFLTKGRSHSSLPQMSSSRSKDSCFTENTPLLRNSLQEKGSRCIPVYHPEFITAEESWEDSSADWERRYLLSREVSGLSASASSEKGDLLDSPHIRLRLSKLRRCVQWLKVMGLFAFVVLCSILFSLYPDQGKLWQLLALSPLENYSVNLSSHVDSTLLQVDLAGALVASGPSRPGREEHIVVELTQADALGSRWRRPQQVTHNWTVYLNPRRSEHSVMSRTFEVLTRETVSISIRASLQQTQAVPLLMAHQYLRGSVETQVTIATAILAGVYALIIFEIVHRTLAAMLGSLAALAALAVIGDRPSLTHVVEWIDFETLALLFGMMILVAIFSETGFFDYCAVKAYRLSRGRVWAMIIMLCLIAAVLSAFLDNVTTMLLFTPVTIRLCEVLNLDPRQVLIAEVIFTNIGGAATAIGDPPNVIIVSNQELRKMGLDFAGFTAHMFIGICLVLLVCFPLLRLLYWNRKLYNKEPSEIVELKHEIHVWRLTAQRISPASREETAVRRLLLGKVLALEHLLARRLHTFHRQISQEDKNWETNIQELQKKHRISDGILLAKCLTVLGFVIFMFFLNSFVPGIHLDLGWIAILGAIWLLILADIHDFEIILHRVEWATLLFFAALFVLMEALAHLHLIEYVGEQTALLIKMVPEEQRLIAAIVLVVWVSALASSLIDNIPFTATMIPVLLNLSHDPEVGLPAPPLMYALAFGACLGGNGTLIGASANVVCAGIAEQHGYGFSFMEFFRLGFPMMVVSCTVGMCYLLVAHVVVGWN
Protein: Protein GPR107 (Q8BUV8)
Organism: Mus musculus (Mouse)
Function: Has been proposed to act as a receptor for neuronostatin, a peptide derived from the somatostatin/SST precursor (By similarity). Involved in blood sugar regulation through the induction of glucagon in response to low glucose (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:26561648}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q5VW38}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAVPVPLGRFGSFCLRLLRLLALLELLVHPVLGRVHHLALKDDVRHKVHLNTFGFFKDGYMVVNVSSLSVNEPEGATDKDAEIGFSLDRTKNDGFSSYLDEDVNYCILKKKSMSSVTLVILDISGSIVKVRSPPEAGKQLPEIVFSKDEKILSQSQEPAVSSNPKDSEARRTLDGFKAGRSTVDSKAITERSFSIHKNDGVVSFQFFFNISTDDQEGLYSLYFHKCSGNNVKPGEQASFSLNIAITEKNPNSYLSAGEIPLPKLYVSMALFFFLSGTIWIHILRKRRNDVFKIHWLMAALPFTKSLSLVFHAIDYHYISSQGFPIEGWAVVYYITHLLKGALLFITIALIGTGWAFIKHILSDKDKKIFMIVIPLQVLANVAYIIIESTEEGTTEYGLWKDSLFLVDLLCCGAILFPVVWSIRHLQEASATDGKAAINLAKLRLFRHYYVLIVCYIYFTRIIAFLLKFAVPFQWKWLYQLLDETATLVFFVLTGYKFRPASDNPYLQLSQEDDDLEMESVVTTSGVMENMKKVKKVSNGAVEPQGSWEGTA
Protein: Opacity protein opA51 (Q04874)
Organism: Neisseria gonorrhoeae
Function: Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation.
Subcellular location: Cell outer membrane.
Interaction partners:
Sequence:
ASEGNGRGPYVQADLAYAYEHITHDYPEQTGTKKDKISTVSDYFRNIRTHSIHPRVSVGYDFGGWRIAADYARYRKWNDNKYSVDIKELENKNQNKRDLKTENQENGTFHAVSSLGLSAVYDFKLNGKFKPYIGARVAYGHVRHSIDSTKKTTKFLTSSYGGLNPTVYTEENTQNAHHQSNSIRRVGLGVIAGVGFDITPKLTLDTGYRYHYWGRLENTRFKTHEASLGVRYRF
Protein: E3 ubiquitin-protein ligase CCNB1IP1 homolog (EC 2.3.2.27) (RING finger-containing protein HEI10) (RING-type E3 ubiquitin transferase HEI10) (F4HRI2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin E3 ligase required for class I crossover (CO) formation during meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:22844245}. Chromosome {ECO:0000269|PubMed:22844245}. Note=Dynamic localization on the meiotic chromosomes. Present as numerous foci on the chromosome axes and the synaptonemal complex central element until pachytene. From pachytene to diakinesis, restricted to a limited number of sites that correspond to class I crossovers.
Interaction partners:
- DNA mismatch repair protein MSH4
- DNA mismatch repair protein MSH5
- ATP-dependent DNA helicase homolog MER3
- Meiosis-specific protein ASY1
- Protein SHORTAGE IN CHIASMATA 1
- ATPase family AAA domain-containing protein FIGL1
- Crossover junction endonuclease MUS81
- DNA mismatch repair protein MLH1
- DNA mismatch repair protein MLH3
- Protein MHF2 homolog
Sequence:
MRCNACWRDLEGRAISTTCGHLLCTEDASKILSNDGACPICDQVLSKSLMKPVDINPNEEWINMAMAGISPQILMKSAYRSVMFYIAQRDLEMQYKMNRVVAQCRQKCEGMQAKFSEKMEQVHTAYQKMGKRCQMMEQEVENLTKDKQELQEKFSEKSRQKRKLDEMYDQLRSEYESVKRTAIQPANNFYPRHQEPDFFSNPAVNMMENRETIRKDRSFFSPATPGPKDEIWPARQNSSNSGPFDISTDSPAIPSDLGNRRAGRGHPVYGGGGTANPQSTLRNLILSPIKRSQLSRSRPQLFTL
Protein: B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Lymphocyte antigen 57) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (Slp-65) (Q9QUN3)
Organism: Mus musculus (Mouse)
Function: Functions as a central linker protein, downstream of the B-cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR-mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR-induced B-cell apoptosis.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=BCR activation results in the translocation to membrane fraction. {ECO:0000250}.
Interaction partners:
- Proto-oncogene vav
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Tyrosine-protein kinase BTK
- Tyrosine-protein kinase SYK
- Tyrosine-protein kinase Lyn
- Growth factor receptor-bound protein 2
- B-cell antigen receptor complex-associated protein alpha chain
- Lymphocyte cytosolic protein 2
- Guanine nucleotide exchange factor VAV3
- Guanine nucleotide exchange factor VAV2
Sequence:
MDKLNKITVPASQKLRQLQKMVHDIKNNEGGIMDKIKKLKVKGPPSVPRRDYALDSPADEEEQWSDDFDSDYENPDEHSDSEMYVMPAEETGDDSYEPPPAEQQTRVVHPALPFTRGEYVDNRSSQRHSPPFSKTLPSKPSWPSAKARLASTLPAPNSLQKPQVPPKPKDLLEDEADYVVPVEDNDENYIHPRESSPPPAEKAPMVNRSTKPNSSSKHMSPPGTVAGRNSGVWDSKSSLPAAPSPLPRAGKKPATPLKTTPVPPLPNASNVCEEKPVPAERHRGSSHRQDTVQSPVFPPTQKPVHQKPVPLPRFPEAGSPAADGPFHSFPFNSTFADQEAELLGKPWYAGACDRKSAEEALHRSNKDGSFLIRKSSGHDSKQPYTLVAFFNKRVYNIPVRFIEATKQYALGKKKNGEEYFGSVVEIVNSHQHNPLVLIDSQNNTKDSTRLKYAVKVS
Protein: Peroxidase (EC 1.11.1.7) (Q8RVW0)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362060}.
Interaction partners:
Sequence:
MKGAYTNPRFFLAMTFMLAMAAALVQAQGTRVGFYARTCPRAESIVRSTVQSHFRSNPNIAPGLLRMHFHDCFVQGCDASILIDGPNTEKTAPPNRLLRGYEVIDDAKTQLEATCPGVVSCADILTLAARDSVFLTRGINWAVPTGRRDGRVSLASDTTILPGFRESIDSQKQKFAAFGLNTQDLVALVGGHTIGTSACQLFSYRLYNFTNGGPDPTINPAFVPQLQALCPQNGDGSRLIDLDTGSGNRFDTSFFANLRNVRGILESDQKLWTDPSTRTFVQRFLGERGSRPLNFNVEFARSMVKMSNIGVKTGTNGEIRRICSAIN
Protein: Pyramus (Q6Q7J0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFHKFMPNVRTYIILMSFVAAIAWSASAAKNVLTLSKHSELALHINSHGKVTAENILRTYQYFNMEAVNDVFSLDFKITIYSADVDYYLCFHHGRLVGKRNATKECHFKEGIFMGNQNFSSAYNPVLRVGFKGNFKPIGLNDFSKPKVMKKAILFFFPLNEEKFNLHLAEVLSSSTTTTTTTTTTTSTTTTTTTPPPSTTTTTTTTTTTPASPVAVTKRTRSKSRRPTSINSNSSNSNIPDKISRHNSNSLKSYNQANSNNNNSSNNNELDLQQQQVILQRNRKLHRRHRLQQKKRQLQLQQQQRRRQRKYGTMGVMAQPQPKNLVGRHHHNN
Protein: Sodium/hydrogen exchanger (Q9VM99)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.
Interaction partners:
Sequence:
MLLIVGFALCVLAPGCSATDTDIALDAKATLNHRIQSLDLLVFVFLLALTVLTIWLFKHHRVSWLHETGLAVIYGLIVGAIIRYAGTSATLVHMQVEPQGVPTYSDKLPPDTLWFRYPVNQTNGTKPPEGIKTYAYVFRGQVHDVDENEIDLKATFDPEVFFNIILPPIIFYAGYSLKKKYFFRNLGAILTFAIVGTTLSAFLIGGFMYGCVKLMPKYLSSSFTFLDSLYFGALISPTDPLTILAIFNDLRVDVNLYALVLGESVLNDAVAIVLSGAIQNYGEHYSNTGEFETTAFLRSLSDFFSIFLLSLMIGAAMGCLTALMTKFTRVRDFPLLESALFVLMSYSTFLLAEATELTGVVAVLFCGICQAHYTYNNLSEDSRQRTKQIFELLNFLAENFIFSYIGVSMFTFPKHHFDAGFIITAFICAAIGRAVNVYPLSWLLNIKRKPKISTNFQHMLFFAGLRGAMSFALAIRNTVSDERQTMLTATSLIVIFTVVIQGGAANFLLNWLKIPVGVDDETEQLNNYQVHSSDGYLQDVEGGGVNRNKMRLSGGTDTNLDTPVDGTNGSLGGASGGRRRNSHEKAILARIWGNFDTKYMKPLLTHSRPTLLETLPVCCNPIARLLTTTQQLTQDGSEFRRVDSDSDICIDNDTGNGLSQDGSGAAPGVGRRNSLSRVGGDHRNAYI
Protein: Integrator complex subunit 13 (Cell cycle regulator Mat89Bb homolog) (Germ cell tumor 1) (Protein asunder homolog) (Sarcoma antigen NY-SAR-95) (Q6GLY5)
Organism: Xenopus laevis (African clawed frog)
Function: Crucial regulator of the mitotic cell cycle and development. At prophase, required for dynein anchoring to the nuclear envelope important for proper centrosome-nucleus coupling (By similarity). At G2/M phase, may be required for proper spindle formation and execution of cytokinesis (By similarity). Probable component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing (By similarity). Plays a role in gastrulation and early embryogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NVM9}. Cytoplasm {ECO:0000250|UniProtKB:Q9NVM9}. Note=Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9NVM9}.
Interaction partners:
Sequence:
MKTFSESHKTVFVVDHCPYMSESCRQHVEFDMLTKNRTQGIIPLAPISKSLWTCAVEASMEYCRIMYDIFPFRKLVNFIVSDSRSRTLNSWNREDQNLQELMAALAVIGPPNPRADPECCSILHGLVEAVESLCKITDFQHESRTALMGNADWVANRGRIICITNAKSDSHVQMLEDCVNETIHEHNKMAAGSDHLMQIQKCHLVLLHTYPVGEDSLVSDRPKKELSNVLVSEVHSVKAGRHLSTKLNQLVQLHFDLASTTITNIPMKPTLSVCDQEEQHANTSANYDVELLHHKEAHVDFIKSGEGYTGSSSIRENSLKETVTLKWCTPRTNSVELHYCTGAFRISPVDVNSRPSSCLTNFLLNGRSVLLEQPRKSGSKVISHMLSSHGGEIFLHVLSSSRSILEDPPSISEGCGGRVTDYRITDFGEFMRENRLMPFPEQSYQMDGGPEVPLERAKEQLERHTRYWPMIISQTTIFNMQAVVPLASVIVKESLSEEDLLNCQKTIYNLVDMERKNDPLPISTAGTRGKGPKRDEQYRIMWNELETLVRAHVSGSERHQRVMECLMACRSKPPEEEERKKRGRKREDKEEKGEKLNKDHEHDKKGQESERIKSVLDQEKEDLAEAEVIKDSPDSPEPPNKKPHIVIEDTGPAEKSKGPMSLLSLWSSRINTANSRKHQEFVGRLNSVNNKAELYQHLKEENGGEGVENGKASRQ
Protein: Tryptophan-rich protein TspO (Translocator protein TspO) (Q8KBX2)
Organism: Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Function: Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX. Can bind the benzodiazepine receptor agonist PK-11195 (in vitro); this interferes with photooxidative tetrapyrrole degradation. May play a role in the transmembrane transport of tetrapyrroles and similar compounds (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:23651039}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MNKQILTLALCIGLCLAVGFAGSTFTPKPASWYYTTLVKPSWNPPDWLFPPVWTILFIMMGTALAKVLGTGWKKNEVNVGVVLFAIQLMLNLGWSASFFGMQSPLAGLVDIVLLWIFIVLTMLAFARVSKPASLLLVPYLCWVSFASYLNFTILQLNP
Protein: Fructose-like permease IIC component 2 (PTS system fructose-like EIIC component 2) (P32672)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996}.
Interaction partners:
- PTS system fructose-like EIIB component 2
- PTS system fructose-like EIIB component 3
- 1-phosphofructokinase
- Multiphosphoryl transfer protein 2
- PTS system fructose-like EIIB component 1
- PTS system fructose-like EIIA component
- ATP-dependent 6-phosphofructokinase isozyme 2
- Multiphosphoryl transfer protein
Sequence:
MNELVQILKNTRQHLMTGVSHMIPFVVSGGILLAVSVMLYGKGAVPDAVADPNLKKLFDIGVAGLTLMVPFLAAYIGYSIAERSALAPCAIGAWVGNSFGAGFFGALIAGIIGGIVVHYLKKIPVHKVLRSVMPIFIIPIVGTLITAGIMMWGLGEPVGALTNSLTQWLQGMQQGSIVMLAVIMGLMLAFDMGGPVNKVAYAFMLICVAQGVYTVVAIAAVGICIPPLGMGLATLIGRKNFSAEERETGKAALVMGCVGVTEGAIPFAAADPLRVIPSIMVGSVCGAVTAALVGAQCYAGWGGLIVLPVVEGKLGYIAAVAVGAVVTAVCVNVLKSLARKNGSSTDEKEDDLDLDFEIN
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) (Q9CR84)
Organism: Mus musculus (Mouse)
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 (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
Sequence:
MQTTKALLISPALIRSCTRGLIRPVSASLLSRPEAPSKQPSCSSSPLQVARREFQTSVISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM
Protein: Uncharacterized protein C15A10.12c (O13732)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Transport protein particle subunit trs31
- Transport protein particle 20 kDa subunit
- Uncharacterized protein C13G6.05c
- Transport protein particle subunit trs23
- Transport protein particle subunit bet5
- Transport protein particle subunit trs120
- Transport protein particle subunit bet3
- Uncharacterized protein CC285.14
- Transport protein particle subunit trs85-2
- Uncharacterized protein C14F5.02
Sequence:
MVKPRLVFLSIAGPKDEQLYLEIIDPKEKHLLARYQYLGELSLDVINDLVNDGERTSNDCFLGLLGVEEDISTYAFYSNTKVKFILAVKAPDYVVKETEIRQLLRRIYTIHTHAVCNPFSMDLTPETLKTSIYFKESLHQLISDWNIH
Protein: adenylate cyclase (EC 4.6.1.1) (Q57Z02)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSDEAPPNKWETPESASAARAVGVYGGGCTPGTYLKTATGVQRGEELFHRPELERPWRTTAEQRHVMSIALREKEIEALMRKCSSLRTKLGNAKHEAKCIEFAMTEKSKEEIGELRDEVKRLEGLLKGENEQHLKLKETMEHQLRMQKLQHEKEQMMLKNECRVLNERVENLTKIYQQQVDDVKKAAAQELDHVESLCNARVEELTKELEAVRATNRVAEERHTEGQALMKNLVHRIESEYKERSTETERRIGDMRARLEDEKKKLSEEREEAVKEAATAAERLVLANAASQEVEQRFKQWDIYILRILDDIYSAFVSCAPEQAVEPHSLEVQEAALLYAPRCIVEDPEAKLVVERIVTRLLQLKTIDTNCEAPVSKESDFDCLLAKLDAKQERLSRALVEIEGKCSEASVSLNRALSRLYFFCDDLENAISHSGSVPPPQRNVVFACLRVFNGDLMWVEDAEKAQAAVSLMNCVLRPKMAQYGAYECYCDGTSMLLAFDDPVAACRFCTETQKWLMTLPWSQSLLESSWGSEVRCQGTNEVVFRGLRLAMAVHTGDTFVEPLSIPVGDSYRCHYYGRAVSQTVHACSTARGGQILVSQAVWERCGPRKHELGALVVRELGVIPTAFFDAEKNSYEKEPIQFFQVFAETLKNRSFNDAGDADVCETDPLGDLNKFLFQSELKGMEGRCVALKRAISAAQEEFGVIDGSIRSLTIKVREAKSHFQLIPPVEMVMHLNNMYTVMERIALRASELRDTIVTLERRQEDLSAQTKGLRSQCSHMISSSARLKEIQIKADVIESSYREQIRGMTAGHREKVEQLHRELQERDQKIRDLCRNVGHVGSGGN
Protein: 3-hydroxyacyl-CoA dehydrogenase C-terminal domain-containing protein (Q38BJ2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- BTB domain-containing protein
- Profilin
- Uncharacterized protein
Sequence:
MRRFAPTVASALSGPPTGCLFAVTGNAVRRYQTEPLKKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPAAPELQKAAPVNFMTSTRRSRGRFTGDDRASGLDEERGRLQRSGGAKEGRNSRREVGYSKKEKIRSRGDTYKGNRDMSLSNVVEDIQDIKIVFASHNPSPSKRQVPFAPKAAPRAPDPPKAPLAPPAAPSMPSDFVASSKPVSGSRNGTRTTIAPPTASGDPQDTVWAKSSALSLDEEIERARATRPLVRSPVIVGREIEGLSLNFEHCEKSEPIVELADKGGLKELSEKEATLIDNHMVPDDFSGGAFMQKHTGVTHDVVGEKELSELSINNTVTAASLETSLYGMEEQQPKESDGRSNLSSTVSSCITEHPPLAPWTCGAFTAQSGSALLKLSFDESSQHIVTITLWEPLVSTISAVGALNEAITAIENHSVTMSGPVTHVVLTSLPGIAFFQPKHSPLELSCSERIELIREKERLFLRMAKTPPLNFVAIVNGGSLDDFAAELFLACHYRVFLDATHTTFGFPSCMLGDFPTSHAVRQLCRYFGAQRTLAASQQQYRFTAATLLDAGVARHARDTREGLTALRLSYVDHSKASPPTSLLLRLENALLALLNRPALRDFVLRRFFLTRSTGGSSVEVYSNPITQAWRRYCLAAMASGGCTHNVGESGNASAAVETGTLRSEGIYSEFLFSPSALNAARIYGHGCEIQRRVLSSPPDGGYLRFKADEAELWPRKVRALSAESCNQVTVLLDCGKSNIEAIKSLVKDQSGVLTKANVVLIGDEYVARPLIPEFNCVATISPVSAYAVSPLRDLQEVRLFGREGCPEHLRASTLSAALAYLQQEYRPYVVCRHSCSGRLIAAFVTEACRIAMHCDIEKVERVSTGVLRLLGGPFRLADHLGTSTVSRLIEETSHMNDHRNPLIHDWLPSIGYQVLRSMSNDGFGGIRTRRGGFYTYGADGSSVALNTVVQKQYLRRHLTDTELSDRLLSVVVNECCELLLSGHLLTAADANALTIATLGFSETTGGALTLADAMGAGLMLQKMEELAVWHGAHLQPSPLLKCMAHSRVSFANLSEAVIQSARM
Protein: 3-methylmercaptopropionyl-CoA dehydrogenase (MMPA-CoA dehydrogenase) (EC 1.3.99.41) (Q5LLW7)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Function: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl-CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).
Interaction partners:
- Methylthioacryloyl-CoA hydratase
- 3-methylmercaptopropionyl-CoA ligase
- Enoyl-CoA hydratase/isomerase/3-hydroxyacyl-CoA dehydrogenase
- Electron transfer flavoprotein subunit alpha
- Fatty oxidation complex, alpha subunit
- Enoyl-CoA hydratase/isomerase/3-hydroxyacyl-CoA dehydrogenase
- Electron transfer flavoprotein subunit beta
Sequence:
MTYQAPVRDIMFAIEHLSQWPQVEALQTYSEIELDDARAALEEFGRFCGEMIAPLSTIGDTEGARLENGRVVLPEGYKTAYDQFVDMGWQSLSHPAEHGGMGLPKVVGAAATEIVNSADMSFGLCPLLTNGAIDALSITGSDAQKAFYLDKLITGRWSGTMNLTEPQAGSDLSRVRCTAVPQDDGTYAISGTKIFITFGEHDLSENIVHLVLARTPDAPEGVRGLSLFVVPKLLAGEGGETSQRNTLGCVSLEHKLGVRASPTAVMEYDNATGYLVGEENSGLRYMFIMMTSARYAVGVQGVAIAERAYQHALSYARDRIQSRPVDGSAQDAVPIIQHPDVRRMLLRMRALTEGGRALAIATGGWLDLAEHGPEEARAEAQSMAEFLVPLVKGFCTERAVEVASLGVQIHGGMGFIEETGVAQFYRDARILPIYEGTTAIQANDLLGRKVLRDGGRTARRFAEMIAATEGELSKGGAAAQRIAQRLAEARAAFAAGLDHLLATAGQDPNRAYAGSVPFLMLTGNLATGWQLGLSALAAEAELAKGGDAEFLQAKIATADIFAQQVLVECSAEHSRITDTGDSLLTASL
Protein: Restriction endonuclease (O25041)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Cag pathogenicity island protein
- site-specific DNA-methyltransferase
Sequence:
MQFLNQSLGFFNKGCFEPIDRNFITESYQALKPIEEIQNKYNKHDNDSFLNELRDSMVALYLDYELINIQKHGLDAKRSSSDEFLEIKQVSFQSQLIKEFEFKMKPIDSKEQELINLFNLKFGHFSWENYLA
Protein: Basic-leucine zipper transcription factor B (Q54ER9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Transcriptional regulator involved in DIF-1 signaling. DIF-1 (Differentiation Inducing Factor-1) is a signal molecule involved in the differentiation of pstO (prestalk-O) cells (By similarity). May be a direct activator of ecmA.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:16396914, ECO:0000269|PubMed:16410410}. Note=In response to DIF-1, it accumulates rapidly in the nucleus.
Interaction partners:
- Myb domain-containing protein
- Des-methyl DIF-1 methyltransferase A
- Extracellular matrix protein A
- Prestalk protein
- Signal transducer and activator of transcription C
- Transmembrane protein
- Polyketide synthase 37
Sequence:
MNQFYQSTTGGQQNNNNGNQFQQYQPQQQQQFQQYSPSNANNNNTTTTTTTSTSKKGKNKDNQSKQQQIQQQQIQQQQQQQQQQQQQIQQQSVDTPSSYNGDGSDDGSDTERENKKNRNRVNQNLASRNYRQRKKEYIKEIEEKLAVLALENDQLKKENINLKKGGGVEIMKPDPAFITMMMEAKQIIIQLDVAIKKNDERSLIYLLQLFHLSIEKRHTIVEREVEKMVHPYTQAKLAAMGYVPSLENPMISSISGPSSDGWWTMYISEAQITEEQAKAIKQLRSNHWKADIELRNEREKLDRSIKEFYLNRVMVFPTNERLNKSFATNLSLSDGPNPTSPNSSSVTQSTLVRPSPGLTLLNNLNEENNNSNNSSNSSNNNTTTNNNNNNSLTPTPNQNNNISNIAVNGTISVVNELGFSPINGNIDISEILEFTRKLEALKKNFVKQRTLMEDTHSALSSILTPKQEAMLLVRVHSSTRYDFANMEMLKNVWGSVIAKDTTSYPQPPTFSQQTQQLQQAQLQLQNQTKQQQQQLQNNNNNNNNNNNNNNSFNNSNNNNVQNNSSNPSTPGGNNDQQNIYYTSSPSIPSSPYNHHQQQPSRQ