wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c oxidase subunit 5A, mitochondrial (Cytochrome c oxidase polypeptide Va) (P00424)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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 COX2 and heme A of COX1 to the active site in COX1, 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:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 9, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 2
Sequence:
MLRNTFTRAGGLSRITSVRFAQTHALSNAAVMDLQSRWENMPSTEQQDIVSKLSERQKLPWAQLTEPEKQAVWYISYGEWGPRRPVLNKGDSSFIAKGVAAGLLFSVGLFAVVRMAGGQDAKTMNKEWQLKSDEYLKSKNANPWGGYSQVQSK
Protein: Inactive serine/threonine-protein kinase TEX14 (Protein kinase-like protein SgK307) (Sugen kinase 307) (Testis-expressed sequence 14) (Testis-expressed sequence 14 protein) (Q8IWB6)
Organism: Homo sapiens (Human)
Function: Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Midbody {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Detected in the intercellular bridges that connect male germ cell daughter cells after cell division. {ECO:0000250}.
Interaction partners:
- Centrosomal protein of 55 kDa
- RNA-binding protein 44
Sequence:
MSRAVRLPVPCPVQLGTLRNDSLEAQLHEYVKQGNYVKVKKILKKGIYVDAVNSLGQTALFVAALLGLRKFVDVLVDYGSDPNHRCFDGSTPVHAAAFSGNQWILSKLLDAGGDLRLHDERGQNPKTWALTAGKERSTQIVEFMQRCASHMQAIIQGFSYDLLKKIDSPQRLVYSPSWCGGLVQGNPNGSPNRLLKAGVISAQNIYSFGFGKAMPWFQFYLTGATQMAYLGSLPVIGEKEVIQADDEPTFSFFSGPYMVMTNLVWNGSRVTVKELNLPTHPHCSRLRLADLLIAEQEHSSKLRHPYLLQLMAVCLSQDLEKTRLVYERITIGTLFSVLHERRSQFPVLHMEVIVHLLLQISDALRYLHFQGFIHRSLSSYAVHIISPGEARLTNLEYMLESEDRGVQRDLTRVPLPTQLYNWAAPEVILQKAATVKSDIYSFSMIMQEILTDDIPWKGLDGSVVKKAVVSGNYLEADVRLPKPYYDIVKSGIHVKQKDRTMNLQDIRYILKNDLKDFTGAQRTQPTESPRVQRYGLHPDVNVYLGLTSEHPRETPDMEIIELKEMGSQPHSPRVHSLFTEGTLDPQAPDPCLMARETQNQDAPCPAPFMAEEASSPSTGQPSLCSFEINEIYSGCLILEDDIEEPPGAASSLEADGPNQVDELKSMEEELDKMEREACCFGSEDESSSKAETEYSFDDWDWQNGSLSSLSLPESTREAKSNLNNMSTTEEYLISKCVLDLKIMQTIMHENDDRLRNIEQILDEVEMKQKEQEERMSLWATSREFTNAYKLPLAVGPPSLNYIPPVLQLSGGQKPDTSGNYPTLPRFPRMLPTLCDPGKQNTDEQFQCTQGAKDSLETSRIQNTSSQGRPRESTAQAKATQFNSALFTLSSHRQGPSASPSCHWDSTRMSVEPVSSEIYNAESRNKDDGKVHLKWKMEVKEMAKKAATGQLTVPPWHPQSSLTLESEAENEPDALLQPPIRSPENTDWQRVIEYHRENDEPRGNGKFDKTGNNDCDSDQHGRQPRLGSFTSIRHPSPRQKEQPEHSEAFQASSDTLVAVEKSYSHQSMQSTCSPESSEDITDEFLTPDGEYFYSSTAQENLALETSSPIEEDFEGIQGAFAQPQVSGEEKFQMRKILGKNAEILPRSQFQPVRSTEDEQEETSKESPKELKEKDISLTDIQDLSSISYEPDSSFKEASCKTPKINHAPTSVSTPLSPGSVSSAASQYKDCLESITFQVKTEFASCWNSQEFIQTLSDDFISVRERAKKLDSLLTSSETPPSRLTGLKRLSSFIGAGSPSLVKACDSSPPHATQRRSLPKVEAFSQHHIDELPPPSQELLDDIELLKQQQGSSTVLHENTASDGGGTANDQRHLEEQETDSKKEDSSMLLSKETEDLGEDTERAHSTLDEDLERWLQPPEESVELQDLPKGSERETNIKDQKVGEEKRKREDSITPERRKSEGVLGTSEEDELKSCFWKRLGWSESSRIIVLDQSDLSD
Protein: Vomeronasal 2, receptor 74 (E9PW21)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Vomeronasal type-1 receptor
- Olfactory receptor
- Olfactory receptor
Sequence:
MFFLNSVFWLLKISFNFGHLSDPRCFWRIKDTENKLGDKETYCFFTISTKHGYVKNDYFRWNLDKKVTPKTRHLIFSVYLALEEINKNCHILPNISLVVNIECVLDKHDEKTDFLFKSEDLIPNYYCKNERRYLIVLTAPLWAVSSSIGPYLFMSRIPEVSQLYCGHFHLPLSDNEQYPHLHQISRKDTFLPLAMVSLVVHFRWNWIGVIVTNDDHGIQFLSEFRGEMQNKIVCLSFAIIIKTGKFLAVTELHMNYKQILMSSAKVVIVYGYRDSPIIYAFIVWKSQDLFRIWVSVSQLDMITFLGDFLLYASTGTFIFSHQKPEISGFEQFIQRIHPSNYSSEFSLAKQWWTYFRCSLPPSNCKKLKNCSTKTVFKWLFMTPLGLAMSDTCYNIYNAMYAVAHSLHGMLLQQVDTWSKNAGKELEFDSWKMFSILKTLKFVNPAGDLVNMNQNLKQDVEFDVFYIMDFQKDYGLKMKIGRFSEHLPSGQQIYMSKEMIEWATDIDQILPSICTMPCRPGLRKSPQEGKDICCFDCKPCSENEVSNMTNMDQCVKCPEDQYANEDHTVCLQKVVTILDYRDPLGKALAGFALCFSVLTSLVLVVFLKHRDTPIVKANNQTLSFVLLISLIFCFICSLLYIGHPTMAICILQQTTFAIVFTVATSTILSKTVIVILAFKITVPGRRMRWLLESGTPKYIIPICTIIQLILCGIWLGTSPPFVDADLHMVHGHILIVCNKGSVIAFYCVLGYMGSVALASFTVAFLARNLPDTFNEAKLLTFSMLVFCSVWITFIPVYHSTKGKTMVAVEVFCILASSAGLLLCIFAPKCYIILLRPQKNYFYKFRKRRELNLTT
Protein: Protein-L-isoaspartate O-methyltransferase (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl methyltransferase) (Protein-beta-aspartate methyltransferase) (PIMT) (P0A7A5)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. This enzyme does not act on D-aspartyl residues.
Subcellular location: Cytoplasm.
Interaction partners:
- 5'/3'-nucleotidase SurE
- Murein hydrolase activator NlpD
- tRNA pseudouridine synthase D
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- RNA polymerase sigma factor RpoS
- Cell division protein FtsB
Sequence:
MVSRRVQALLDQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQLDEGGILVLPVGEEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA
Protein: Mushroom body defect protein (Q1KN24)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDTRSWRKVLLQWIGECHFIESNYITLEQSDLDSFFSVFIQKIQETETVKGKNELQDQPPEQSPLVQEFLAHNYPEFIAQQDDKEVDLPLDCLYVYTLLLHYSCVKKPSLFFHNICNKLPELTQTCIASFFRETVDRLLTREYLSQAIANVAVVYRQGVSTSVSPCLPSSSLSPDPRSDDAPCPSTPSSSSSQQSSSTPQLRNHREQLRLNGCEMPPPSTPKTELLEQRTKELRGIRTQLEVVRYEKALLEEQQMEKDELIKVLNKEKMMAKMELEKLRNVKLTEEHHDNESHHIMPYEFEHMKGCLLKEIGLKESLIAEITDKLHDLRVENSELSEKLNLAGKRLLEYTDRIRFLESRVDDLTRIVSSRDVMISSLESDKQELDKCLKEARDDLHNRIEVLNASSDLLDCSLSPNTTPENLASSVIDKQLREKEHENAELKEKLLNLNNSQRELCQALSSFLQKHNIDHEFPVEWTSSSLLSTISAIESKFVNTLEKSTQMKKECDVQSVCVEKLLEKCKLLSVSLGCQPKELDGFEATIPEAMESGFESSRECETILSCCHMKVVDIASKNNDLELDNERLNDKCAELKSIIDRGDQHLADINLQLTEKEKQIKDVGAEIQELRKRNINLENMLSQITDKEASAASHAQHLKQCGELLRAKYEVCRNELIAKNAAQDELVRMMMVPDGETLNGRVRQLIDLEMMHDEHNKMYAQMLKQLNELSAKHDNMTHSHLDFVKRTEIELETKNAQIMAFDEHNNHFDRFLTRIFTLLRSRNCPKSTTMGSATNFLESMHIEKRFENIEMLIEGQLLSADDLKRELDDLRSKNEELAKQNINGIIKRNKFITSLEVNTEKVKQYITDLEEEAFKRKQKVVQLENTLSKEQSNAKEMAQRLDIAQQEIKDYHVEAIRFINTIRDRLQQDFNGVNTPQQLGTCMTEFLKMYDQMEVRYEESSSLVEKLTESQAKLEMQVAELQVELENKDTNQHSGALIKQLNDTIQNLEKVNAKLSEDNTVSHTVHSKLNESLLKAQKELDLRAKIIENLEASERNLSMKLCELKDLKNKLKSSDEKIAQIKETYEEQIKALQAKCDMEAKKNEHLERNQNQSLTQLKEDALENCVLMSTKLEELQAKLQEGQQLVDSQKLELDMNRKELALVKSAYEAQTKLSDDLQRQKESGQQLVDNLKVELEKERKELAHVNSAIGAQTKLSDDLECQKESGQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESALQLVDNLKVELDKERKELAKVTSVIEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKMELDKERKELAQVKSAIGAQTKLSDDLECQKESVQQLVDNLKVELEKERKELAKVNSAFEAQTKLSDDLKLQKEDAQREVFLVKERLVKEKREFEVKLATLEDLIETMEMRCTQMEEERATAYEQINKLENRCQEKDNVKSNQLQVETFKVECLHHQLKSEMATHNSLVEDLNRKLAEKVSKLDFVQSRLMTEIAEHNQVKDQLAQITDIPKVVELQHRLEAETAEREEAQNKLAVVTGRLDEITRELDNARLEHGAQILRMEETAREVGNKNAELCELIEFYRNRVEALERLLLASNQELEELNSIQSNQAEGVRDLGDTYSAAEGRQTESDQDKERYQKLALDCKILQAKYRDAKDEIKRCEKKIKDQRLEMEGKLEKMKNKMRSLYTAEVTRMKEKQERDAAKSASELEALTAQNAKYEEHTRKLSNQIVRLNEKILEQQKQHAIISTNLRHLQMQPISETKPSSTTLTVSSSSSAPNDDWQPFKRPNVPSSNLAMEDEEGEVFNNTYLTDLKLGRVPADMTAEELIYRNSLQPPHLKSTYAAQYDLGSQDEDLKDGPHSLDDSMSALLSSSSTGTRKKSMGTHYKRPGPPTPSKNGGRLSFGSSEPPREILREFGDHNNTSKTPARFKFLTQRFSVGSSGLPRDELPRRKRPNLLTGIHRRRLRHAVDIFCTSTPRKSRSYYDQQRLIGATDADKSEAIETEDEVIEVEPDAVPELEPLEDADQQGTPHLSTAALLALTKGNTRRLTGTTKSKKGRVSLSLHGNIFAKSRPASFVAGKRVQLRRKLRRDRIMGRFDEARHLDQMRLSHSAQAAKSPENNNYSLHNRNEEEHLPSENNVMGKTVVLVGKRRLSPVVSTTFNVEERSETSLLQQQFEHENCVTWAMHGGESVMMEETQNDWYFEQLCKETESTAPFQLQPLDYKPLDEEQIEPKFTQLVAASCSNITTTSCATNMTGASSCTVYSIGSVHMQPLPQINITYVQQPSDLQQRRPTRHRSLMAQCRRFLRHLSLGQRLVMGFALLVMVGLSLHLADKLVLVITGILSGMGLVFLTYSCPGRN
Protein: Metalloendoproteinase 5-MMP (At5-MMP) (EC 3.4.24.-) (Q9ZUJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (By similarity). Active on Mca-KESAbuNLFVLKDpaR-NH(2) (QF75) and, to some extent, on McaPLGLDpaAR-NH(2) (QF24), myelin basic protein (MBP) and beta-casein.
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}; Extracellular side {ECO:0000305}.
Interaction partners:
- Carboxypeptidase SOL1
- RHOMBOID-like protein 2
- Protein IQ-DOMAIN 22
- non-specific serine/threonine protein kinase
- SKU5 similar 3
Sequence:
MRTLLLTILIFFFTVNPISAKFYTNVSSIPPLQFLNATQNAWETFSKLAGCHIGENINGLSKLKQYFRRFGYITTTGNCTDDFDDVLQSAINTYQKNFNLKVTGKLDSSTLRQIVKPRCGNPDLIDGVSEMNGGKILRTTEKYSFFPGKPRWPKRKRDLTYAFAPQNNLTDEVKRVFSRAFTRWAEVTPLNFTRSESILRADIVIGFFSGEHGDGEPFDGAMGTLAHASSPPTGMLHLDGDEDWLISNGEISRRILPVTTVVDLESVAVHEIGHLLGLGHSSVEDAIMFPAISGGDRKVELAKDDIEGIQHLYGGNPNGDGGGSKPSRESQSTGGDSVRRWRGWMISLSSIATCIFLISV
Protein: DNA topoisomerase (EC 5.6.2.1) (Q38C52)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RecQ mediated genome instability protein 1 OB-fold domain-containing protein
- DNA 3'-5' helicase
- DNA 3'-5' helicase
- Crossover junction endonuclease MUS81
- DNA repair protein, putative
- Uncharacterized protein
- Replication protein A subunit
- DNA repair protein RAD50
- DNA repair protein RAD51 homolog
- BRCT domain-containing protein
Sequence:
MFRQTVTSLEKLVIVESPNKVIKIEGLLSNPKVIPDWSFKQGHLKCVGIGAEKAVAMATTGHFMALKEITWITHPLPPSSAGGKPQEYDGEAFPSSGTLAEYTLEWEPLPGRRIQETLERYIEGKVENVSEIILATDPDREGELIAVHALQTIKRLYPKLKVPFSRAYMHSITEDGIRKAMKERSLNICDYDLASAAETRHVMDRFFGFLGSSVVRAANSQMRSIGRVQTPALILINEREDKISAFLERNKSTFVVEATCQFPVPHGTTFSQVVDIHSDRRGAPSQWNTAAEANNCLEHWKLDGCHSFSIPHDPIVTPSKVPPPQPLTMAAAITKLNRQMKLSSEMVSGYLQDLFQLGHITYPRTDSTRIDESALKDIYNAVKKNFGKEFLYRLEDRPASGGDGKRGKKQTKKKTAKRGKNSGTPVGNVEDAHEAIRPTNINVQGDSLSLSPETRAVYELVRRQTLAAFMIPQVVEKIVADVKFVSGSGEKLTLTLGGKRVVEPGWTRAFHKGDSGNLSLHVGAEEGADAGDEGAPTMCSLSQEEFYAILNLRRVLNSPNQQHLFELRSPTIRENRPVPPMPHSEGTLIEELKRNGVGRPSTYPLIVKTLLARGYIQVNAKGRCETTPVGRMLVETAKSTFPSIVDLGFTASFEKQLDTVAKPHPNKRPAFLRSTKISQADYVLSMFLSTFLNYVSEAACTQRARIIERSMRLKRDQEGGSGIGDAEFEESVVAARRKVTLASTDLVTLPKTYNNFSTLQRNLNEYLRHNFPPSQVNGSPAPSPTVDAPRSRRGGAGTSRGVAGGG
Protein: Zinc-specific metallo-regulatory protein (P54479)
Organism: Bacillus subtilis (strain 168)
Function: Acts as a negative controlling element, employing Zn(2+) as a cofactor to bind the operator of the repressed genes. Required for the zinc-specific repression of two operons implicated in zinc uptake, yciC and ycdHIyceA. Also represses the expression of rpmE2, the gene for ribosomal protein L31B, which is expressed only after the end of exponential growth.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Manganese transport system membrane protein MntC
- Zinc chaperone YciC
Sequence:
MNVQEALNLLKENGYKYTNKREDMLQLFADSDRYLTAKNVLSALNDDYPGLSFDTIYRNLSLYEELGILETTELSGEKLFRFKCSFTHHHHHFICLACGKTKEIESCPMDKLCDDLDGYQVSGHKFEIYGTCPDCTAENQENTTA
Protein: Alpha-1-syntrophin (59 kDa dystrophin-associated protein A1 acidic component 1) (Pro-TGF-alpha cytoplasmic domain-interacting protein 1) (TACIP1) (Syntrophin-1) (Q13424)
Organism: Homo sapiens (Human)
Function: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate (By similarity).
Subcellular location: Cell membrane, sarcolemma {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions. {ECO:0000250}.
Interaction partners:
- Dystrophin
- Caveolin-3
- Dystroglycan 1
- Dystrobrevin alpha
- Nitric oxide synthase 1
- Delta-sarcoglycan
- Alpha-sarcoglycan
- Gamma-2-syntrophin
- Sodium channel protein type 5 subunit alpha
- Utrophin
Sequence:
MASGRRAPRTGLLELRAGAGSGAGGERWQRVLLSLAEDVLTVSPADGDPGPEPGAPREQEPAQLNGAAEPGAGPPQLPEALLLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKGLAADQTEALFVGDAILSVNGEDLSSATHDEAVQVLKKTGKEVVLEVKYMKDVSPYFKNSTGGTSVGWDSPPASPLQRQPSSPGPTPRNFSEAKHMSLKMAYVSKRCTPNDPEPRYLEICSADGQDTLFLRAKDEASARSWATAIQAQVNTLTPRVKDELQALLAATSTAGSQDIKQIGWLTEQLPSGGTAPTLALLTEKELLLYLSLPETREALSRPARTAPLIATRLVHSGPSKGSVPYDAELSFALRTGTRHGVDTHLFSVESPQELAAWTRQLVDGCHRAAEGVQEVSTACTWNGRPCSLSVHIDKGFTLWAAEPGAARAVLLRQPFEKLQMSSDDGASLLFLDFGGAEGEIQLDLHSCPKTIVFIIHSFLSAKVTRLGLLA
Protein: Cell cycle protein kinase spo4 (EC 2.7.11.1) (Sporulation-specific protein 4) (Q9UQY9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the initiation of meiosis II and progression through anaphase II.
Subcellular location: Nucleus {ECO:0000269|PubMed:11739743}.
Interaction partners:
- Sporulation-specific protein 6
- DNA replication licensing factor mcm5
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm2
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm6
- DNA replication licensing factor mcm7
- Hsk1-interacting molecule 1
- Cell cycle serine/threonine-protein kinase hsk1
- Serine/threonine-protein kinase cds1
Sequence:
MLSMLLPFGNSGVYASDVDREDRPEIAKLVQAFPTIEEDYHVVKLVGAGSFSSVFKAVDRHFDSYDNSYWISSQIEDQMPHDKTKRPKNHFVALKRIYATVLPSRIQTELEMLHELRGSDCVLNMITAVRHQDQVLIVLPFIQHAEFRDFYMKYSLPEIGAYLRDLLKGLAHIDAKGIIHRDIKPGNFAWNPYTQRGVILDFGLAQWQEADAPTENCCVDKLRKLKQEGKYYDYFPFEKTIADPPEGYLLHDPRPTKRADRAGTRGFRAPEVLFRCQNQTSSIDVWSVGVILLCFLTHRYPFFRCEDDIDAIVELAHIFGRNGMSNCALLHGQIWSDNIPTLLDQKHNWLDLIASITKNDENLILETSSDYQVALAIDLLDKLLELHPSKRVKAKTALQHEFFNACGVTRSGFEAENPFRSDFPSTVEQ
Protein: Eukaryotic translation initiation factor 3 subunit H (eIF3h) (Eukaryotic translation initiation factor 3 subunit 3) (eIF-3 gamma) (eIF3 p40 subunit) (Q6IB98)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03007}.
Interaction partners:
Sequence:
MASRKEGTGSTATSSSSTAGAAGKGKGKGGSGDSAVKQVQIDGLVVLKIIKHYQEEGQGTEVVQGVLLGLVVEDRLEITNCFPFPQHTEDDADFDEVQYQMEMMRSLRHVNIDHLHVGWYQSTYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLKAYRLTPKLMEVCKEKDFSPEALKKANITFEYMFEEVPIVIKNSHLINVLMWELEKKSAVADKHELLSLASSNHLGKNLQLLMDRVDEMSQDIVKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEEDLSKLFKPPQPPARMDSLLIAGQINTYCQNIKEFTAQNLGKLFMAQALQEYNN
Protein: Uncharacterized protein, isoform C (Q7PLP5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ras-related protein Rab5
- LD29542p
- Receptor-mediated endocytosis protein 6 homolog
Sequence:
MKTGSNETFSVLKMEKILAVQSDEYTKLQRCYVELQRKYNENIASSENEESGLSSFLSRLSLTVASLFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQNDGLALDLLKAAHRFGLPSLLGICERALVTSVGVRSCIRFYCVAEEVGASTLLEYCSSIISTHWDDLTTDDFQHMSGPLLFEMLKTKTKHPLHAAVRLLREDVVSLCIQKYGNSLVNTFSENGILPLEMALSSKNAKIAKSLVDNGMANINAVNMEGFSLLKSALKNGDAFSANFLLDQNCLLDLPSKPSSDTALHIICNYGPDNTPEIMEVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVPNIDINLRTYDEKCALELSLSMGDHEFLIASILLSMGARTDRTNSKTGDSLLQVFALDRHRGEKSAIFLADFADLDHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKHIDCGLKSALHIAVEANAIDALEAFVELKNKSHDIDFNCQDINGDSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRGIALSINKNGESPLWSALEKGYEDVAKILVRHGIDTDCWDEGPEGCRQTLLHRAIDENKESVAIFLIQSQCDLDSSRQPGPNGEGGDEAQDKASPLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDIDLKLRDKSGNTPFATALDFRNHNAAQRILDRFPTAAEQMDIRGRNFLHLAILKDDLESVLFLLAIQVDVNSRVHDANQSSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRELLTESRVNAEATNLKGRNPLHELCRVVEDSTAGLICELFLESMPKYPINIPDMDGNTPLLLSFMRGQSPLCKILVKAGACLGTENKDGINIFNFKLATDQLLHNLLDQLPQESPWAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCFNVLQCGNGSLS
Protein: Poly(rC)-binding protein 3 (Alpha-CP3) (P57722)
Organism: Mus musculus (Mouse)
Function: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MGEGDAIWAPPILPHSTLGTLSHHPELHFGGKMESKVSEGGLNVTLTIRLLMHGKEVGSIIGKKGETVKKMREESGARINISEGNCPERIVTITGPTDAIFKAFAMIAYKFEEDIINSMSNSPATSKPPVTLRLVVPASQCGSLIGKGGSKIKEIRESTGAQVQVAGDMLPNSTERAVTISGTPDAIIQCVKQICVVMLESPPKGATIPYRPKPASTPVIFAGGQAYTIQGQYAIPHPDQLTKLHQLAMQQTPFPPLGQTNPAFPGEKLPLHSSEEAQNLMGQSSGLDASPPASTHELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGTPANISLAQYLINARLTSEVTGMGAL
Protein: Cold sensitive U2 snRNA suppressor 2 (P53830)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: U2 snRNP protein which helps to refold U2 into a structure favorable for its binding to SF3b and SF3a prior to spliceosome assembly. Mediates functional interactions between U2 RNA and PRP5. Enforces ATP dependence during formation of the prespliceosome by brokering an interaction between PRP5 and the U2 snRNP that depends on correct U2 RNA structure.
Interaction partners:
- U2 snRNP component HSH155
- Pre-mRNA-splicing factor CLF1
- Pre-mRNA-processing ATP-dependent RNA helicase PRP5
- Cold sensitive U2 snRNA suppressor 1
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-splicing factor PRP11
- Pre-mRNA-splicing factor PRP21
- Pre-mRNA-splicing factor RDS3
- Small nuclear ribonucleoprotein F
- Protein HSH49
Sequence:
MDADELELKGHLKKLKKEELLRRKQLKESNLQKRELEYNNASKNTSIYISGLPTDKTTKEGLTEQFCKYGMIRTNRDGEPLCKLYVNDKGAFKGDALITYSKEESVTLAIEMMNESIFLGKQIRVERAQFQNKEGDNMHGKENDLKEFNGPEPPIKRLKKAKSEGEGEVIDYNDDESLAKADRTVIFANVFNIYKSYTNDDINDIQEDLLEGCEEIGQVDSISVSPNKGEATVVFKNNKVALQCCKIMTGRYFDGQKLLAFISGDENTSSTSDKNEDSEVEDDLI
Protein: M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B) (P30305)
Organism: Homo sapiens (Human)
Function: Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Directly dephosphorylates CDK1 and stimulates its kinase activity. The three isoforms seem to have a different level of activity.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15311285, ECO:0000269|PubMed:15908796}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15908796}.
Interaction partners:
- Cyclin-dependent kinase 1
- 14-3-3 protein beta/alpha
- 14-3-3 protein epsilon
- Cyclin-dependent kinase 2
- 14-3-3 protein zeta/delta
- 14-3-3 protein theta
- 14-3-3 protein eta
- 14-3-3 protein gamma
- Serine/threonine-protein kinase Chk1
- Cyclin-A2
Sequence:
MEVPQPEPAPGSALSPAGVCGGAQRPGHLPGLLLGSHGLLGSPVRAAASSPVTTLTQTMHDLAGLGSETPKSQVGTLLFRSRSRLTHLSLSRRASESSLSSESSESSDAGLCMDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHSPVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ
Protein: NAC domain-containing protein 75 (ANAC075) (Q9M0F8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator involved in xylem formation. Promotes the expression of the secondary wall-associated transcription factor MYB46. Functions upstream of NAC030/VND7, a master switch of xylem vessel differentiation. Acts as upstream regulator of NAC101/VND6 and LBD30/ASL19.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
- LOB domain-containing protein 15
- LOB domain-containing protein 30
- GATA transcription factor 5
- NAC domain-containing protein 104
- GATA transcription factor 12
- NAC domain-containing protein 12
Sequence:
MNKSNPAGSVTGSDIIDAKIEEHQLCGSKKCPSCGHKLEGKPQDWVGLPAGVKFDPTDQELIEHLEAKVLAKDFKSHPLIDEFIPTIEGEDGICYTHPEKLPGVTRDGLSRHFFHRPSKAYTTGTRKRRKIQTECDNNLQGSSSSGETRWHKTGKTRPVMVNGKQKGCKKILVLYTNFGKNRKPEKTNWVMHQYHLGTHEEEKEGELVVSKIFYQTQPRQCNWSSSTSSLNAIGGGGGEASSGGGGGEYHMRRDSGTTSGGSCSSSREIINVNPPNRSDEIGGVGGGVMAVAAAAAAVAAGLPSYAMDQLSFVPFMKSFDEVARRETPQTGHATCEDVMAEQHRHRHQPSSSTSHHMAHDHHHHHHQQQQQRHHAFNISQPTHPISTIISPSTSLHHASINILDDNPYHVHRILLPNENYQTQQQLRQEGEEEHNDGKMGGRSASGLEELIMGCTSSTTHHDVKDGSSSMGNQQEAEWLKYSTFWPAPDSSDNQDHHG
Protein: Amine oxidase [copper-containing] gamma 2 (AtCuAOgamma2) (EC 1.4.3.21) (Q9M2B9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Copper amine oxidase that can use putrescine and spermidine as substrates.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:Q8H1H9}.
Interaction partners:
- Polyamine oxidase 1
- Probable polyamine oxidase 5
- Tyrosine decarboxylase 2
- Phenylacetaldehyde synthase
- Probable polyamine oxidase 4
- Polyamine oxidase 2
- Polyamine oxidase 3
- Histidinol-phosphate aminotransferase 1, chloroplastic
- Precursor of CEP12
- Probable aminotransferase TAT4
Sequence:
MVELSFSQLLVLLLSLLFLFTTLASSSKTPRFKYSLEKPHHPLDPLTTPEIKRVQTILSGHDPGFGSGSTIIHAMALDEPDKQRVIRWKKGDRLPPRRAEILAMSNGESHVLTVDLKSGRVVSDLVNPTFGYPILTMKDIIAVSQVPYKSVEFNRSIEARGIPFSGLICITPFAGWYGPDEEGRRVIKIQCFSKQDTVNFYMRPIEGLYLTVDMDKLEIIKIVDNGPVPVPKSTGTEYRYGFLNETVYMDRVNPMSMEQPDGPSFQVEDGYLVKWANWKFHIKPDQRAGMIISQATVRDSKTGEARSVMYKGFASELFVPNMDPGEGWYSKAYMDAGEFGLGPSSMPLVPLNDCPRNAYYIDGFFASPEGIPILQPNMICLFERYAGDTSWRHSEILLPGVDIRESRAKVTLVARMACSVGNYDYIFDWEFQMDGVIRVTVAASGMLMVKGTAYENVEDLGEKEDDSGPLISENVIGVVHDHFISFHLDMDIDGSANNSFVKVHLEKQRLPPGESRRKSYLKVKKYVAKTEKDAQIKMSLYDPYEFHLVNPNRLSRLGNPAGYKLVPGGNAASLLDHDDPPQMRGAFTNNQIWVTRYNRSEQWAGGLLMYQSRGEDTLQVWSDRDRSIENKDIVLWYTLGFHHVPCQEDFPVMPTIASSFELKPVNFFESNPVLGISPFFEKDLPVC