wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc metalloproteinase leucurolysin-B (Leuc-B) (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP) (P86092)
Organism: Bothrops leucurus (Whitetail lancehead)
Function: Snake venom zinc metalloproteinase that acts as a potent hemorrhagic toxin. Hydrolyzes the insulin B chain at the 14-Ala-|-Leu-15 bond but not the 16-Tyr-|-Leu-17 bond. Degrades the alpha-chain of fibrin and hydrolyzes the Aalpha-chain of fibrinogen (FGA) while leaving the beta and gamma chains unaffected. Degrades type-I collagen and its gelatin. Degrades the alpha-1 chain of type-IV collagen and its gelatin but not the alpha-2 chain. Degrades plasma fibronectin, plasma vitronectin and basement membrane enactin. It inhibits collagen-induced platelet aggregation.
Subcellular location: Secreted {ECO:0000269|PubMed:17963685}.
Interaction partners:
Sequence:
DTVLLNRISHDNAQLLAIVFNENVIGKAYTGGMCDPRYSVGVVMDHSPINRLVADTMAHEMGHNLGIHHDTGSCSCGGHSCIMSRVISHQPLQYFSNCSYIEYWDFITKLNPQCILNEPLRTDIVSPPVCGNELLEMGEECDCGSPRNCRDLCCDAATCKLHSWVECESGECCDQCRFIKAGNVCRPPRKECDVAEACTGQSAQCPTDDFKRNGQPCLNNYAYCYQGNCPIMYHQCYALFGSDATMAQDSCFQVNKKGNEYFYCRLENGINIPCAQEDVKCGRLFCHNMKYEQDCNYSDRGMVDNGTKCAEGKVCNSNRQAYQR
Protein: Putative oligopeptide transporter YGL114W (P53134)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Regulator of V-ATPase in vacuolar membrane protein 1
Sequence:
MPQSTPSQEVQRVPWDNKPALKQITLRATIAGIAIGSLVLTSNFQFGLQTGWVSMMSLPSALLACAFFKNIWPLIFPNDRPFSDVENVYVQSMAVAVGTGPLAFGFVGVIPAIEKFLTNDESGGLREQGQSFTFRELLIWSTALAFFGIFFAVPLRKQVIVREKLPFPSGSATATLISVLNGTEILQEVSKSELLEMRQRRLNECPEVLQPNRDPEEADYLMNSSHSELGDYTATSQDGSSILSTGSENYRANIIILLKTFVVSSLYTMVSYFVPVIRSIPVFGKYLSNNYLWNFQPSPAYIGQGIIMGLPTVSYMLIGCFLGWGVLAPLARYKRWVPPDADVHDWEEGVQGWILWSSLSIMVADSVVAFIVVTVKSIVKFILIDDKAALLNNIIDDTFQSMLLEEERAINSSRRNTYVDGRQDTVRLVSRDNEIEVDSKHLVRYTTVISGCLVSSIICIVSIIYLFGIQVIPLYAIITALILALFLSILGIRALGETDLNPVSGIGKISQLIFAFIIPRDRPGSVLMNVVSGGIAEASAQQAGDLMQDLKTGHLLGASPRAQFCAQLIGACWSIILSSFMYLCYNKVYSIPSEQFRIPTAVVWIDCARLVTGKGLPDKALECSMILGVIFAVLSLIRNTYRDYGYGWILYIPSGVAVGVGIFNSPSFTIARFIGGWASHFWLKNHRGDLNAKTKMIVFSSGLVLGEGIFSVINMLFICLNVPHY
Protein: Acyl-acyl carrier protein thioesterase ATL3, chloroplastic (EC 3.1.2.-) (Acyl-ACP thioesterase ATL3) (Acyl-lipid thioesterase 3) (Q8W583)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acyl-ACP thioesterase involved in the production of fatty acids and beta-keto fatty acids. Can produce fatty acids of long chain (14:1 and 16:1) and beta-keto fatty acids of medium to long chain (8:0, 10:0, 12:0, 12:1, 14:0 and 16:0) when expressed in a heterologous organism (E.coli). Possesses thioesterase activity for lauroyl-ACP (12:0-ACP) in vitro. May play a role in the generation of long fatty acids in the chloroplast.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:24214063}.
Interaction partners:
- TRF-like 6
- RING-H2 finger protein ATL3
- Sequence-specific DNA binding transcription factor
- Pre-mRNA-processing protein 40C
Sequence:
MFLQVTGTATPAMPAVVFLNSWRRPLSIPLRSVKTFKPLAFFDLKGGKGMSEFHEVELKVRDYELDQFGVVNNAVYANYCQHGRHEFLESIGINCDEVARSGEALAISELTMKFLSPLRSGDKFVVKARISGTSAARIYFDHFIFKLPNQEPILEAKGIAVWLDNKYRPVRIPSSIRSKFVHFLRQDDAV
Protein: Probable transcriptional regulatory protein (O53151)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible nitrogen fixation related protein
- Iron-sulfur cluster assembly SufBD family protein Rv1462
- Probable conserved ATP-binding protein ABC transporter
- Probable cysteine desulfurase
- Conserved protein
- Probable transcriptional regulatory protein
- Zinc uptake regulation protein
- Iron-sulfur cluster assembly SufBD family protein Rv1461
- Possible transcriptional regulatory protein NadR
- Probable ECF RNA polymerase sigma factor SigI
Sequence:
MTSTTLPHRASLVDRSTEFCHTDVVKIPAVSTTVPAAVSDGHTRRAIVRLLLESGSITAGEIGDRLGLSAAGVRRHLDALIEAGDAEASAAAPWQQVGRGRPAKRYRLTAAGRAKLDHSYDDLASAAMRQLREIGGEEAVRTFARRRIDAILADVAPADGPDDAALEAAAERIATALSKAGYVATTTRVGGPIHGVQICQHHCPVSHVAEEFPELCETEQQAMAEVLGTHVQRLATIVNGDCACTTHVPLSPAPSPRPPATSTEGASR
Protein: Echinoderm microtubule-associated protein-like 5 (EMAP-5) (Q05BV3)
Organism: Homo sapiens (Human)
Function: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
Sequence:
MAARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSPREHRQKFYRGHSDDIISLALHPERVLVATGQVGKEPYICIWDSYTVQTISVLKDVHTHGIACLAFDLDGQRLVSVGLDSKNAVCVWDWKRGKMLSMAPGHTDRIFDISWDLYQPNKLVSCGVKHIKFWSLCGNALTPKRGVFGKTGDLQTILCLACARDELTYSGALNGDIYVWKGINLIRTIQGAHAAGIFSMNACEEGFATGGRDGCIRLWDLTFKPITVIDLRETDQGYKGLSVRSVCWRGDHILVGTQDSEIFEIVVQERNKPFLIMQGHCEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCNMEEPIRCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQRYKKVGECLGSLSFITHLDWSSDSRYLQTNDGNGKRLFYRMPGGKEVTSTEEIKGVHWASWTCVSGLEVNGIWPKYSDINDINSVDGNYIGQVLVTADDYGIIKLFRYPCLRKGAKFRKYIGHSAHVTNVRWSHDYQWVISIGGADHSVFQWKFIPERKLKDAVHIAPQESLADSHSDESDSDLSDVPELDSEIEQETQLTYRRQVYKEDLPQLKEQCKEKQKSATSKRRERAPGNSIRLHFVHGYRGYDCRSNLFYTQIGEIVYHVAAVGVIYNRQQNTQRFYLGHDDDILCLTIHPLKDYVATGQVGRDPSIHIWDTETIKPLSILKGHHQYGVSAVDFSADGKRLASVGIDDSHTVVLWDWKKGEKLSIARGSKDKIFVVKMNPYVPDKLITAGIKHMKFWRKAGGGLIGRKGYIGTLGKNDTMMCAVYGWTEEMAFSGTSTGDVCIWRDIFLVKTVKAHDGPVFSMHALEKGFVTGGKDGIVALWDDSFERCLKTYAIKRAALAPGSKGLLLEDNPSIRAISLGHGHILVGTKNGEILEVDKSGPITLLVQGHMEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDMISDIRFSPGSGKYLAVASHDSFIDIYNVMSSKRVGICKGATSYITHIDWDIRGKLLQVNTGAKEQLFFEAPRGKKQTIPSVEVEKIAWASWTSVLGLCCEGIWPVIGEVTDVTASCLTSDKMVLATGDDLGFVKLFRYPTKGKFGKFKRYVAHSTHVTNVRWTYDDSMLVTLGGTDMSLMVWTNEMEGYREKRPCDSEESDIDSEEDGGYDSDVTRENEISYTIRALSTNIRPMLGIKPHLQQKEPSIDERPPVSRAPPQPEKLQTNNVGKKKRPIEDLVLELIFGYRGRDCRNNVHYLNDGDDIIYHTASVGILHNVATGSQSFYQEHNDDILCLTVNQHPKFINIVATGQVGDSADMSATAPSIHIWDAMNKQTLSILRCYHSKGVCSVSFSATGKLLLSVGLDPEHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTQFVSVGVKHVKFWTLAGRALLSKKGLLSTLEDARMQTMLAIAFGANNLTFTGTISGDVCVWKDHILCRIVARAHNGPVFAMYTTLRDGLIVTGGKERPSKEGGAVKLWDQELRRCRAFRLETGQATDCVRSVCRGKGKILVGTRNAEIIEVGEKNAACNILVNGHVDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLNKVNLGHAARTVCYSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRRCAIHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRISYCKDIPSFVIQMDFSADSSYLQVSSGCYKRHVYEVPSGKHLMDHAAIDRITWATWTSILGDEVLGIWSRHAEKADVNCACVSHSGISLVTGDDFGMVKLFDFPCPEKFAKHKRFLGHSPHVTNIRFTSGDRHVVSAGGDDCSLFVWKCVHTPH
Protein: Double-Strand Break factor (D2Y8W2)
Organism: Caenorhabditis elegans
Interaction partners:
- Double-Strand Break factor
- Meiotic recombination protein spo-11
- Cyclin N-terminal domain-containing protein
- Sun domain-containing protein 1
- HORMA domain-containing protein
- X chromosome NonDisjunction factor
- DNA repair protein RAD51 homolog
- High Incidence of Males
- Serine/threonine-protein kinase chk-2
- HORMA domain-containing protein
Sequence:
MSARGLKVEMYYKLAEKNEAETSDVSILIDGHKRKFAVICNGIGREMVDLHYDSKKFPRIFSRERHLYVMFSESTSDGFRLTFGATEREQFLRIMHSLGCLLDTAIVKFSQQSSSSQPPPMRRDSTAVFNNSYNQYTSFQQASQPRVFSTIKLELSGDSCNSAFQPSQPTGFPDNQLLTIKKSSSNQISLSVEVADKCIQTEDLVDLLADDEYCMRKALRKMIENPSFIKAVAAAENTLQYIPQAEQEGLEDVTEPPINDIFFDRFHQPQLEQHDSVPED
Protein: Phosphatidylinositol-binding clathrin assembly protein (Clathrin assembly lymphoid myeloid leukemia protein) (rCALM) (O55012)
Organism: Rattus norvegicus (Rat)
Function: Cytoplasmic adapter protein that plays a critical role in clathrin-mediated endocytosis which is important in processes such as internalization of cell receptors, synaptic transmission or removal of apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the cytoplasmic side of plasma membrane leading to clathrin-coated vesicles (CCVs) assembly. Furthermore, regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature. In addition to binding to clathrin, mediates the endocytosis of small R-SNARES (Soluble NSF Attachment Protein REceptors) between plasma membranes and endosomes including VAMP2, VAMP3, VAMP4, VAMP7 or VAMP8. In turn, PICALM-dependent SNARE endocytosis is required for the formation and maturation of autophagic precursors. Modulates thereby autophagy and the turnover of autophagy substrates such as MAPT/TAU or amyloid precursor protein cleaved C-terminal fragment (APP-CTF).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q13492}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q13492}. Golgi apparatus {ECO:0000250|UniProtKB:Q13492}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q13492}. Nucleus {ECO:0000250|UniProtKB:Q13492}. Note=Colocalized with clathrin in the Golgi area. Interaction with PIMREG may target PICALM to the nucleus in some cells. {ECO:0000250|UniProtKB:Q13492}.
Interaction partners:
- Epidermal growth factor receptor pathway substrate 15
- Epidermal growth factor receptor substrate 15-like 1
- Clathrin heavy chain 1
- Cyclin-G-associated kinase
- AP-2 complex subunit alpha
- Epsin-2
- AP-2 complex subunit mu
- AP2-associated protein kinase 1
- Clathrin light chain A
- Disabled homolog 2
Sequence:
MSGQSLTDRITAAQHSVTGSAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSYRQVAFDFTKVKRGADGVMRTMNTEKLLKTVPIIQNQMDALLDFNVNSNELTNGVINAAFMLLFKDAIRLFAAYNEGIINLLEKYFDMKKNQCKEGLDIYKKFLTRMTRISEFLKVAEQVGIDRGDIPDLSQAPSSLLDALEQHLASLEGKKIKDSTAASRATTLSNAVSSLASTGLSLTKVDEREKQAALEEEQARLKALKEQRLKELAKKPHTSLTTAASPVSTSAGGIMTAPAIDIFSTPSSSNSTSKLPNDLLDLQQPTFHPSVHAMSAAPQVASTWGDAVDDAIPSLNPFLTKSSGDVHLPISSDVSTFTTRTPTHEMFVGFSPSPVTQPHPSAGLNVDFESVFGNKSTNVAVDSGGGLLKPTVASQNQSLPVAKLPPNKLVSDDLDSSLANLVGNLGIGNGTTKNDVSCSQPGEKKLTGGSNWQPKVAPTTAWSAATMAPPVMAYPATTPTGMIGYGIPPQMGSVPVMTQPTLIYSQPVMRPPNPFGPVPGAQIQFM
Protein: Trk system potassium uptake protein TrkH (Q87TN7)
Organism: Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Function: Low-affinity potassium transport system. Interacts with trk system potassium uptake protein TrkA and requires TrkE for transport activity. Selective for permeation of potassium ion and rubidium ion over smaller ions such as natrium or litium.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P23849}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23849, ECO:0000303|PubMed:21317882}.
Interaction partners:
Sequence:
MQFRSIIRIVGLLLALFSVTMLAPALVALLYRDGAGVPFVTTFFVLLFCGAMCWFPNRRHKHELKSRDGFLIVVLFWTVLGSAGSLPFLIADNPNISVTDAFFESFSALTTTGATVIVGLDELPKAILFYRQFLQWFGGMGIIVLAVAILPVLGIGGMQLYRAEIPGPVKDTKMTPRIAETAKALWYIYLSLTIACAVAFWLAGMTPFDAISHSFSTIAIGGFSTHDASMGYFDSYAINLITVVFLLISACNFTLHFAAFASGGVHPKYYWKDPEFRAFIFIQVLLFLVCFLLLLKHHSYTSPYDAFDQALFQTVSISTTAGFTTTGFADWPLFLPVLLLFSSFIGGCAGSTGGGMKVIRILLLTLQGARELKRLVHPRAVYTIKVGGSALPQRVVDAVWGFFSAYALVFVVCMLGLIATGMDELSAFSAVAATLNNLGPGLGEVALHFGDVNDKAKWVLIVSMLFGRLEIFTLLILLTPTFWRS
Protein: Coenzyme Q-binding protein coq10, mitochondrial (Q9USM9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Matrix side {ECO:0000250|UniProtKB:Q08058, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized FAD-binding protein C17H9.12c
Sequence:
MAFRCTLRRLECYRASRLMPYKPSFLFSLISNVNEYERFVPFCQKSKVTEYDPKTGYPTKADLTVGFKGLCETFDSKVVCDPVALTVLADASHHRLFRRLKTHWSIEEASRGRVRVDLEVDFEFASKLHGMMSKFVGSSVASEIIQGFVQQAKIKHKLESENEK
Protein: Origin of replication complex subunit 1 (OsORC1) (Q10CI8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O43913}.
Interaction partners:
- Origin of replication complex subunit 3
- Origin of replication complex subunit 6
- Cell division control protein 6 homolog
- Origin of replication complex subunit 1
- Origin of replication complex subunit 2
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM5
- Probable DNA helicase MCM8
- DNA replication licensing factor MCM3
- Origin of replication complex subunit 4
Sequence:
MSQPVTPRRTTRSSASASPSPAPASPTSPPKSRPKPSPRRQLLAAAAAPPKEDGSSADALLAELPGRRAQAMDILRLLAPAPALPLMLHGGAATGKTRALLLALRYLRPSQRLVYAALRSLPSPRALFASLLSQLSATPFSTSSRHRVPDKPSDFVAALRDALNGIVSQGEVVYLVFDNLEVVRSWDKGGQLLPLLLRLHDLLQLPQVVLVYVSSATPDAYYSMTGSVEPNYVYFPDYTVDEVRDILMHDHPNPKLYSSFLSVALKPLFRVTRRVDELSAVLEPLFRRYCEPLGDLKAVPDEGMKRRLFEHVQSHLAVALNETFNVPMRASMDEIKDGGSAGKGSAKRQFAGKDGLSSELEFHMSVSAKYLLLSAFLASRNPATLDAALFDSTGGLDNRKRKRKSSQASMHMKDTIVEEMLMKGPGTFPLERLLAIFQCITSVSEDILDEIDCPGNMASESGTTGLMSDVLLQLSTLCNSNFLSKSRSCPLEGSARYRSNIDEDLALKVARSVNFPLSKYMYRR
Protein: D-allose-binding periplasmic protein (ALBP) (P39265)
Organism: Escherichia coli (strain K12)
Function: Part of the binding-protein-dependent transport system AlsBAC for D-allose.
Subcellular location: Periplasm.
Interaction partners:
- D-allose transport system permease protein AlsC
- D-allose import ATP-binding protein AlsA
- Ribose import permease protein RbsC
- L-arabinose transport system permease protein AraH
- Probable ABC transporter permease protein YphD
- Xylose transport system permease protein XylH
- Autoinducer 2 import system permease protein LsrD
- Galactofuranose transporter permease protein YtfT
- Galactose/methyl galactoside import permease protein MglC
- D-allulose-6-phosphate 3-epimerase
Sequence:
MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLMVDAEKSGKVIPLDKAPEFKLVDSILVTQ
Protein: Beta-1,3-glucan-binding protein (BGBP) (Beta-1,3-glucan recognition protein) (BetaGRP) (Gram-negative bacteria-binding protein) (GNBP) (PibetaGRP) (Q8MU95)
Organism: Plodia interpunctella (Indianmeal moth)
Function: Involved in the recognition of invading microorganisms causing their aggregation. Activates the phenoloxidase cascade. Binds specifically to beta-1,3-glucan. Binds to curdlan, a linear water-insoluble beta-1,3-glucan polysaccharide, and to laminarin, a water-soluble beta-1,3-glucan polysaccharide containing beta-1,6 branches. Binds also to lipopolysaccharide and lipoteichoic acid.
Subcellular location: Secreted {ECO:0000269|PubMed:12770576}.
Interaction partners:
Sequence:
MFVTFICFLACLTCSYGQPRAQQYVVPSAKLEAIYPKGLRVSIPDDGFSLFAFHGKLNEEMDGLEAGHWARDITKPKEGRWTFRDRNVKLKLGDKIYFWTYVIKDGLGYRQDNGEWTVTEFVNEDGTPADTSLEPTTAPTPVRPDQPNQPIPTHRPDPPCTVSATMVDGRKSVCQGTLLFSEEFEKANLKDLANWEAEVKFPEEPDYPFNVYMVDGTLELEDGSLVLTPKLLESRFHAGILNDALDLTNRCSGQVDTTECRRQASGAQILPPVMTGKITTKNKFTFKFGRVEVRAKLPAGNWLLPEINLEPKDNVFGSRRYESGLMRVAFAKGNAVFAKKLNGGPVLADTEPFRSLLMKEKIGIDNWNRDYHNYTLIWKQDGIDMLVDGEKYGSISPGEGFYALGREHAVPHAAHWLRGSVMAPLDQYFFLSLGLRVGGVHDFADSPDKPWKNRSNKAVLNFWNDRDNWFPTWFDANLKVDYVRVYAL
Protein: Sperm vesicle fusion protein fer-1 (Q17388)
Organism: Caenorhabditis elegans
Function: Required for the fusion of the membranous organelles (MOs) with the plasma membrane, a process essential in spermiogenesis.
Subcellular location: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Palmitoyltransferase spe-10
- C2 domain-containing protein
- C2 domain-containing protein
- WD_REPEATS_REGION domain-containing protein
- C2 domain-containing protein
- Myosin motor domain-containing protein
- Sperm transmembrane protein 9
- C2 domain-containing protein
- C2 domain-containing protein
- Uncharacterized protein
Sequence:
MTVKEKLLKVKQKFKRGDSSSDVDSGPERDRDEDDSDNESRNTSKTSKSSKKSKSGKSTGTSEMTELSDDGGSDIELLPDDGKSFGKRKLQDTDKPCTWNVLVRIIEAKDVSTGSARVRTIFDGNSKMTRTVTHAIPKWRQNILYTIKNQPLEKLAAKVLTLRLVRPTALGESSVGEFSCYLSEVIHSPDRSVIAKWVALGFPGMDDEEPDDIAYENCGFLKVTLSVYRIDESPPTLIDDDGKEQIWSGAHLIDYTLKIRVFSVEQLIRQMINERKIKKKQRFYVMVQCGAHKTETTMESAFLDEDANIASVKFEQEIYLPIQWPTVISEIIFSLFDKKGRGKTCIGKATLPMKMIYEPGETGYLPTFGPAFLNVFDCERVTRFSIFSRKMRGSQQDGSRFVGRLFIAIDCVEYMEKANAQIMHLDHSPIMEAESICKNLEWYNCFCSMSGLNMINPQFASDPVCIMMSIGSFGSTSNEFRSCNSSTLPAEPNWDGCKYFTMPWGNLRPVAEVNAPWEVIEHRIEMSNVLMKMTNMLDTMIWEVRRIGNKAIDHVSSVGMEALECLEQQIDSASKYLGRINPVSSNALDRHILDYRKEKILKLREHFEKEAFSIDYSDGEVDAKLLRMLLKIRSMTLELAEDVQMTIPPVLIKMMSHGKLIGFAKIPISEIFQSDDEAQSGEWCGRTRAINIQWPTLVDQRNRKREHVAVLHAKMWFGRTDQLTKWKEHVQPADIRRFMEMYEVQTKGLALKWKDEADIYDGKWEKTNEVPLENGWNAVGHWIVMNTRHMFVPKLGQHTVHDKAFEIQKRTEDGTWKHFKYTDCYADELKPKDLDKHAKGWEVGSWAQDKFRNNGDEKGWVYSTNGVFFGSGVLTDREEKVHHNFRKRCIKRPRKHEGYNKELEDFEHFRTTMGNENWEYSPSKKEGPYHDLEDRTDRIRRRRYVREVENKDPDSEDPRFRVYEYQMQTGKWQLRCYIMWGNDLLPVVKNSSRAFVRISFAQYSKQTLLVDNSQNPIWNETVMFKSVLIAGGTRDIMKYPPVVSVEVVGECSNNEEANLGHFETKPNVICGNTDVRGTPQWFPLKFSNGRTRGAVLACFELYSEEDKDLIPLEPKCKHNYKERSEIPTEFRPQFDKFHVQFLCWGVRNLKKHKLLAVRRPFVGLTIGDQEFTLQPLKDVRRDPNFPEPMIVFGEVILPSALELSPPLIINLFDARAFNRQPLVGSCLVSDLHKYVSHIVPKVKSDHAERWEQLDLVITEEFDQIIRMVRVPTLTTDPMVPLDWWSRYYASMSQFHRSPGYPESGMEYVRIFRRPLEQMNGYNNFSDFLDTFPFVKSMKGDFDDPEEKEKAGELKCRLLISKLKKGKPPAAINTVVDFVGPTRCLVRVYIIEANGLISNARKGRVDSYVKLHCGKQNVNLKKNYRSECCDPIFGERVDMTVTIPLEKDLKITVMGKRRILSDQEIGSTTIDLENRLLTKWRATGGLSGQFTVQGELQWRDQMTPMEILKSYCYKMMLSVPKIESRQTERGEEKGITIEKITFWFSEVLHVFENEEIAMLNSQRQKAGKENFSDGSDQQNEDVSDGSWDEEDLEREKEKLKWEKHRSKGKPLKKVTTEKAETADGELRKKAKMRIMGSQLQTIALFILRQMNLVPEHVESRPLFSDKGGRTQKGELRMFVDIFPMEYGAIPAPFNIAPRKPINYQLRIAVMDVRGAIPVKRSFAEPVSDLYVKAFINGMTKGHKTDTHFRVLDGTGEFNWRFLLNFDYNPWEKKVVAYTKNRFFCKPVEELVDPILVIELWDKNKFRKDRLLGDIELDLLDFIEGIGSPSDVGVYSTKKRQRGVKCPKCCTRRGCLCKCCIFCFETKCLCGKRKVKKKPFPKPVLFVEPEGYDDTVNIFESRNLYGWWPMLTEEYPHEEPQNAKKKNDDVGKDPKWIMGLVEMDMLLLTKQEADQEPAGKKRSEPNHSPFLEKPDRKSWANSWLVSRIKPCIKYFWHYYGLQILLWLIIIVILILTIFVLLHTWPTILAEIIKAIF
Protein: Transcription factor MBP1 (MBF subunit p120) (P39678)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. Transcriptional activation by MBF has an important role in the transition from G1 to S phase. It may have a dual role in that it behaves as an activator of transcription at the G1-S boundary and as a repressor during other stages of the cell cycle.
Subcellular location: Nucleus.
Interaction partners:
- Regulatory protein SWI4
- Regulatory protein SWI6
- G1/S-specific cyclin CLN1
- G1/S-specific cyclin CLN3
- Protein BCK2
- G1/S-specific cyclin CLN2
- Transcription factor NRM1
- Protein STB1
- G1-specific transcriptional repressor WHI5
- Pheromone receptor transcription factor
Sequence:
MSNQIYSARYSGVDVYEFIHSTGSIMKRKKDDWVNATHILKAANFAKAKRTRILEKEVLKETHEKVQGGFGKYQGTWVPLNIAKQLAEKFSVYDQLKPLFDFTQTDGSASPPPAPKHHHASKVDRKKAIRSASTSAIMETKRNNKKAEENQFQSSKILGNPTAAPRKRGRPVGSTRGSRRKLGVNLQRSQSDMGFPRPAIPNSSISTTQLPSIRSTMGPQSPTLGILEEERHDSRQQQPQQNNSAQFKEIDLEDGLSSDVEPSQQLQQVFNQNTGFVPQQQSSLIQTQQTESMATSVSSSPSLPTSPGDFADSNPFEERFPGGGTSPIISMIPRYPVTSRPQTSDINDKVNKYLSKLVDYFISNEMKSNKSLPQVLLHPPPHSAPYIDAPIDPELHTAFHWACSMGNLPIAEALYEAGTSIRSTNSQGQTPLMRSSLFHNSYTRRTFPRIFQLLHETVFDIDSQSQTVIHHIVKRKSTTPSAVYYLDVVLSKIKDFSPQYRIELLLNTQDKNGDTALHIASKNGDVVFFNTLVKMGALTTISNKEGLTANEIMNQQYEQMMIQNGTNQHVNSSNTDLNIHVNTNNIETKNDVNSMVIMSPVSPSDYITYPSQIATNISRNIPNVVNSMKQMASIYNDLHEQHDNEIKSLQKTLKSISKTKIQVSLKTLEVLKESSKDENGEAQTNDDFEILSRLQEQNTKKLRKRLIRYKRLIKQKLEYRQTVLLNKLIEDETQATTNNTVEKDNNTLERLELAQELTMLQLQRKNKLSSLVKKFEDNAKIHKYRRIIREGTEMNIEEVDSSLDVILQTLIANNNKNKGAEQIITISNANSHA
Protein: PPi-type phosphoenolpyruvate carboxykinase (PPi-PEPCK) (PfPEPCK) (EC 4.1.1.38) (Diphosphate-dependent phosphoenolpyruvate carboxykinase) (PEP carboxyphosphotransferase) (A0A0C5URS1)
Organism: Propionibacterium freudenreichii subsp. freudenreichii
Function: Inorganic pyrophosphate (PPi)-dependent phosphoenolpyruvate carboxykinase, which regulates the carbon flow of the central metabolism by fixing CO(2) to phosphoenolpyruvate to produce oxaloacetate. Can also produce pyruvate and diphosphate from phosphoenolpyruvate and phosphate.
Interaction partners:
Sequence:
MSVVERRQINAAINLRLSLLGLPHPDSNAESPDAILVEPLLARQRELSRRLKDRLSAPDLRIQRFLDDYLADCDEHPQLPRTTLVLDEPGLARGLSLPVDGDEFHSDIVASYRLVNGVLHNPKHDRRTTAGVFHISTGGLPIPQDKVEVDKNVYARILARAFQAPDEELALPYTANLPEQAHCWASLLMRPTVLPAVPGRTTEKSYEVHFIVPGGLMCNLDFVEGIFGNAGDPYLPENDASLDPDSWTGHTGCVILAPHLTTMTKKSLGMPHYDDATERQRRDGQCWRHEDDLYNDGKAFKVCARDERGVIVTVIADNYFGYCKKEVKTQISYSANLLGGAEEEHSGGAEVYPAWNLNQDFTDRTPDDFTLADVISTNRELLDVRPEGYAVYKPEPNIVFIPEHSHYSMRTQTISWTAHGAEQTIKLLAGKHYLSPDGYRIHAKHREMDATQWHLIGTSSRAVTCHKPATVSGGGKSEISKSISDAFVFGNAFSHDIDSAMDQVQALFDTDFTNRFADASRNGTDHRPVLSIDRSLGSVIKLLTPSIQYNDEYNAFLEGIEPDVKELAFTVKRYYLPEWGEDWRSHFTVGIMNGRHGNMVRLDGKKIITNMLRVGFREDGSWRLFTLRPDYSPAVKVQTEDDITASTVTPPWEDAEGLPRKYVTNCEHLLFQRPDDAIHRGYDKQAEFDLASGTDTFISNFEPLTHEQARDLLTDVQAYSEFTKPVRKLIERVAAMPDDQSPEFWVCSDDPRHLPDGGRSKNPRYLQVRPTDSNPELTTVADVAGKLARKLPLAGHAPQPIDVVAAGRRNNPPEDKVPALCAYNPLHYMELPELFMEYISSMTGKSPSTTGAGSEGALTKGPFNALPAVYDLNAALLSYALTDYDGWLSSAGYIGPNARVDHDISMLIPELFSHMGPNDRNTKRLISEGYLEKMQDFDFDGHRVLASRLGYRINDRFVTHYFGRIFLHPDVVFSEEMLRPELQDEKIFADSIDVIVKTHQRVAQMYFDDGTVSLACPPIRALLEIMAHGASAEGWTLDSPEFRKLFERESVLASDWYAQRLDAKQAEDVKQAEEGVERLKEYIGRSDSGSVTGRLHLADRLRELEAQLTYERSPEYRQSLVGTLGRQPRFV
Protein: Glycosyltransferase family 92 protein At1g27200 (EC 2.4.1.-) (Q94K98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTEYENGKKRKVRNKQQVKVQFLSQRYLILCFCCFFVLLFFLSSDRISTLSVRSDSLRPSLRVPTLSVLSSSMDSFHRGRFPPLSVEDRVQFPDHLLLILSHGIGKGEKNLVCVYRGVKEETLVLPSISSDEFDEFRSIVRCPNAPLNYSSSVDLQFRGDLVKKKMKKQSRRVHNWEKVGYEAVIDGDTVVVFVKGLTRRPHKESDPSYYKCQFEIENSEEKEVTQAIAAAQEVVRCGLPESLKLNPEMMFRVSVIHIDPRGRTTPALPSVARIYGSDSIEKKEKKSGVKHELCVCTMLWNQAPFLREWIMYHSWLGVERWFIYDNNSDDGIQEEIELLSSENYNVSRHVWPWIKTQEAGFSHCAVRAKEECNWVGFFDVDEFYYFPTHRSQGLPSKNALKSLVSNYTSWDLVGEIRTDCHSYGPSGLTSVPSQGVTVGYTCRQANPERHKSIIRPELLTSSLLNEVHHFQLKEGVGHMSLVESVAVVNHYKYQVWDTFKAKFYRRVATYVVDWQENQNQGSKDRAPGLGTEAIEPPDWKRRFCEVWDTGLKDLVMSNFADQVTGYLPWQRQQQE
Protein: Acid-activated urea channel (Urease accessory protein UreI) (Q09068)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Functions as a specific, H(+)-activated urea channel that increases the rate of urea entry into the cytoplasm, resulting in activation of cytoplasmic urease at acidic medium pH. Is essential for H.pylori gastric survival and colonization. Is necessary for the adaptation of urease activity to the extracellular pH, as in the presence of urea, UreI rapidly enhances the production of ammonia in the extracellular medium when the pH of the medium was decreased to pH5 or below.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Urease accessory protein UreE
- Urease accessory protein UreF
- Urease accessory protein UreH
- Urease accessory protein UreG
- Urease subunit beta
- Urease subunit alpha
- Phosphoglucosamine mutase
- Inorganic pyrophosphatase
- Tryptophan biosynthesis protein TrpCF
- ATP synthase subunit alpha
Sequence:
MLGLVLLYVGIVLISNGICGLTKVDPKSTAVMNFFVGGLSIICNIVVITYSALHPTAPVEGAEDIAQVSHHLTSFYGPATGLLFGFTYLYAAINHTFGLDWRPYSWYSLFVAINTIPAAILSHYSDMLDDHKVLGITEGDWWAIIWLAWGVLWLTAFIENILKIPLGKFTPWLAIIEGILTAWIPAWLLFIQHWV