wanglab/gogpt-training-data huggingface dataset:
Protein: Abl interactor 1 S homeolog (MGC84356 protein) (Q66IV2)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cell projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MAELQMLLEEEIPAGKKALIESYHNLTRVADYCESNYIQAPDKRKALEETKAYTTQSLASVAYQINALANNVLQLLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNAARSHKIIAPASIERPVRYIRKPVDYTVLDDVGHGIKWLKAKHGGNQAARTGTLTRTNPPTQKPPSPPMPSRGTLGRNTPYKTLEPVKPPTVPNDYMTSPARLGSQHSPGRTASLNQRPRTHSGSSGGSGSRENSGSSSIGIPIAVPTPSPPTVGQGISGGPPPPPAPPPPPPPPPPPVGTGSAPASQFGSMTRQISRHNSTTSSASSGGYRRTPSVTSQFSGQPHVNGGPLYSQNSISIASPPPPMLQLTPQIPLTGFVARVQENIADSPTPPPPPPPDEIPMFDDSPPPPPPPPVDYEEEEAAVVQYNDPYADGDPTWAPKIYLEKVVAIYDYSKDKADELSFMEGSIIYVIKKNDDGWYEGVSNGVTGLFPGNYVEAVMHYAD
Protein: Exo-beta-D-glucosaminidase (EC 3.2.1.165) (Q82NR8)
Organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Function: Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has no beta-mannosidase activity.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q56F26}.
Interaction partners:
Sequence:
MFHRPASVRRFVTTAVALGLLSTLSTGARAGARTHEPPPRPTTVSSTAGSTTALTGYAIQSTAKVTDPAAAVSSPGYPASGWYPAGARSTVLAALLAGGKYADPFYSTNQQKIPKADFQVPWWYRSDFTVADTSARTYLDFSGVISAADVFVNGRQIARSADVAGAYTRHELDVTSLVREGANTVAFRIQPNNPNKNLTMGWIDWLEPPPDQNMGIVRDVLVRRGGPVALRDAHVITRLDVPSLATADLTVKARARNDSDAAITATVSGSVGATSFRRSVALAAHETKTVTFTPADTPGLHLTSPRVWWPAGMGGQPLYALDLSASVSETVSDTVHESFGIRDVKAPLNSDGARQYSVNGRRLLIKGGGWSPDEFLRWDSTYVEDRLRYALDLGLNTIRLEGHIEPDEFFDLADRYGILTLPGWECCNKWEGNVNGSGSGDEWTAADYPVAKASMAAEAARLRDHPSVVSFLIGSDFAPDAKIEKTYLDALKAADWPTPVVAAASDKSSPVSGSSGMKMTGPYDWIPPNYWYAKREGGATGFNSETSAGPDIPTLDTLRRMMTPAELDTLWKNPGAKQYHRSPSSVFGTLKIYDAALAGRYGAPTGLTDYVRKAQLAQYENVRAQFEAYGRGATDASKPATGVIYWMFNSGWTSLHWQLLDRYLDQGGAYFGAKKANEPLHVQYSYDDRSVVVVNNRPAAVSGLTARVTLFNTDGTQKYDKSATGLSVAGDGAHSTALTLPSSVSGLSTTYLARLVLTDSAGKEVSRNVYWLSTRPDTLDWAHTDWYYTPTTSYADLKGLGSMARVPVSATASTTAGTDGASTTTVTVRNTGSGRTPSLFTDVHLVDSKGKPVLPVQWSDNEVSLWPGESATLTVTYRTADLHGSAPRVRVSGWNTAEQTVPAA
Protein: Autophagy-related protein 13 (Q6CWK2)
Organism: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Function: Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06628}. Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
Interaction partners:
- Serine/threonine-protein kinase ATG1
- Autophagy-related protein 17
- Autophagy-related protein 29
- Autophagy-related protein 9
- Putative lipase ATG15
- KLLA0A10637p
- Vacuolar protein 8
- Serine/threonine-protein kinase TOR
- KLLA0A09471p
- KLLA0D04840p
Sequence:
MSEGEVQVIELINNFFLKSALLLEQSKVAHNFDTEEALRDGNHLFNIETRGDPLLEAQIQPWITFDGVKTMPPLVIETYLDLRALQPNHMVYLHDADGNPWMVCKGGKKTEIVLERWLVELDKQTIDDSIDSNDPENLHKQLVLLFRYLYTLTQLLPANDIITKPHNSQQPALINVQTRLLDGSKPILSKGRVGLSKPIIASYSNTMNETNIASHLEQRKITPIKTTFGSLRITVSYRKDVDFYVIDSDDLQKRYMTPSLSNETTTVPDRRASSNCSRSMSVSPKTNTINATLFPLEGSSARRQSISSKLQPFKVGSVGSGSFVQSGSAQSTTSLVPSLSRNVSSSSVVAALKVQRGSAGSTIVNGDVPPELSSVGSGSKYSSSFGRIRRHSSIRRSESFDRTAKPRKSTENPPEDLLEFVKLLEDKKELNMKPNTILPQQDISNSLMRFQSMKSNNDALSDNLSMSMSIDQPNVRFGSNSHSPIPSFSPNYGSIPSRLSQGSRNNSNAELITSRKSSLDRHKHNLLSRTGSNVDINRRGSVGTMETTNEDSKEDEQSHMKGMHFSNEATINKDDDEDEMLMKRSFNAGTSTTEQVMGSPRSIRSISVSSYPRNQLPLKHLNLSHPTTSATTTHAKFHKSEMSPDPLHTEGAQPHTSSQHHNSSQKNDEDDDLLFVMSDMNLTN
Protein: Oxygen-independent coproporphyrinogen III oxidase (CPO) (EC 1.3.98.3) (Coproporphyrinogen III dehydrogenase) (CPDH) (P77915)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P32131}.
Interaction partners:
- Oxygen-dependent coproporphyrinogen-III oxidase
- Cytochrome c oxidase, cbb3-type, CcoO subunit
- Uroporphyrinogen decarboxylase
- cytochrome-c oxidase
- Outer membrane protein OprG
- Protoporphyrinogen IX oxidase
- Bacteriohemerythrin
- Acetyltransferase PA5475
- Metallo-beta-lactamase domain-containing protein
- Cbb3-type cytochrome c oxidase subunit
Sequence:
MLDTIRWDADLIRRYDLSGPRYTSYPTAVQFHEGIGPFDQLHALRDSRKAGHPLSLYVHIPFCANICYYCACNKVITKDRGRSAPYLARLVREIEIVSRHLSREQVVEQLHFGGGTPTFLSPGQLRELMSQLRTHLNLLDDDSGDYGIEIDPREADWSTMGLLRELGFNRVSLGVQDFDMEVQKAVNRMQTPEETRTIVEAARTLQYRSINLDLIYGLPKQTPDSFARTVDEVIALQPDRLSVFNYAHLPERFMPQRRINADDLPSPGQKLEMLQRTTEQLAAAGYRYIGMDHFALPDDELASAQEDGTLQRNFQGYTTHGHCDLVGLGVSAISQIGDLYSQNSSDINDYQTSLDNGQLAIRRGLHCNSDDRVRRAVIQQLICHFELAFEDIETEFGIDFRSYFAELWPDLERFAADGLIRLDAKGIDITSSGRLLVRSICMLFDRYLPSLNRQRFSRVI
Protein: Large ribosomal subunit protein eL14z (60S ribosomal protein L14-1) (Q9SIM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein eL34z
- Large ribosomal subunit protein eL8z
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein eL21z/eL21y
- Large ribosomal subunit protein uL22y
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL6x
- Large ribosomal subunit protein eL33w
- Small ribosomal subunit protein eS24z
- Large ribosomal subunit protein uL23z
Sequence:
MGFKRFVEIGRVALVNYGEDYGKLVVIVDVVDQNRALVDAPDMERIQMNLKRLSLTDIVIDINRVPKKKVLIEAMEKADVKNKWEKSSWGRKLIVQKRRAALNDFDRFKIMLAKIKRAGIVRQELAKLKREIAA
Protein: Growth hormone d12 (Prolactin family 8, subfamily A, member 2) (Q4QRA1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLPLSQPRFSGALLMLVISNLLLWEKTASVPACHLEEGGCWDPLVNTFNSAIQRAEVIQNLAEQIHEEFYHNPFSSAQFVTLVARMYRHDQAVYRARYHCPSNSTNPPLHGPEHENIKTKKYLKMMINFVGSWISPLFHLVLELRGMQNVPEVILSKAKDIEENNREILEDLRWILTKVYPTAKMKEKIISWDYLSSIKSNEKSEKFLAIFNISHCLRVDIFYTKFHLRALMCRITGKEC
Protein: Huntingtin-interacting protein 1-related protein (HIP1-related protein) (Q9JKY5)
Organism: Mus musculus (Mouse)
Function: Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis.
Subcellular location: Cytoplasm, perinuclear region. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Note=Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region.
Interaction partners:
- Cyclin-G-associated kinase
- Clathrin heavy chain 1
- Src substrate cortactin
- Epsin-3
- Epsin-1
- Huntingtin
- Src-like-adapter 2
- Disabled homolog 2
- Phosphatidylinositol-binding clathrin assembly protein
- Clathrin light chain A
Sequence:
MNSIKNVPARVLSRRPGHSLEAEREQFDKTQAISISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLSSSSILSWKFCHVLHKVLRDGHPNVLHDYQRYRSNIREIGDLWGHLRDQYGHLVNIYTKLLLTKISFHLKHPQFPAGLEVTDEVLEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLMFKLHSCLPADTLQGHRDRFHEQFHSLKNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEEEEPENLIEISSAPPAGEPVVVADLFDQTFGPPNGSMKDDRDLQIENLKREVETLRAELEKIKMEAQRYISQLKGQVNGLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLREEAERKASATEARYSKLKEKHSELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQAKRESEMKMEEQSDQLEKLKRELAARAGELARAQEALSRTEQSGSELSSRLDTLNAEKEALSGVVRQREAELLAAQSLVREKEEALSQEQQRSSQEKGELRGQLAEKESQEQGLRQKLLDEQLAVLRSAAAEAEAILQDAVSKLDDPLHLRCTSSPDYLVSRAQAALDSVSGLEQGHTQYLASSEDASALVAALTRFSHLAADTIVNGAATSHLAPTDPADRLMDTCRECGARALELVGQLQDQTVLPRAQPSLMRAPLQGILQLGQDLKPKSLDVRQEELGAMVDKEMAATSAAIEDAVRRIEDMMSQARHESSGVKLEVNERILNSCTDLMKAIRLLVMTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVGWGATQLVESADKVVLHMGKYEELIVCSHEIAASTAQLVAASKVKANKNSPHLSRLQECSRTVNERAANVVASTKSGQEQIEDRDTMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERVRLGELRKQHYVLAGGMGTPSEEEPSRPSPAPRSGATKKPPLAQKPSIAPRTDNQLDKKDGVYPAQLVNY
Protein: Alanine--tRNA ligase (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (O28029)
Organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- TPR domain-containing protein
- Uncharacterized protein
- Isoleucine--tRNA ligase
- Glycine--tRNA ligase
- Histidine--tRNA ligase
- Valine--tRNA ligase
- Leucine--tRNA ligase
- Threonine--tRNA ligase
- Tyrosine--tRNA ligase
- Methionine--tRNA ligase
Sequence:
MTLDEEYLDITFLTENGFVRKRCPKCGKHFWTADPEREICGDPPCESYSFIGNPVFKKPFELDEMREYYLNFFERRGHGRIERYPVVARWRTDIYLTIASIADFQPFVTSGVAPPPANPLTISQPCIRLDDLDSVGRTGRHLTLFEMMAHHAFNYPGKEIYWKNETVAYCTELLNELGVKKEDIVYKEEPWAGGGNAGPCLEAIVGGLEVATLVFMNLEEHPEGDIEIKGARYRKMDNYIVDTGYGLERFVWASKGTPTVYDAIFPEVVDTIIDNSNVSFNREDERVRRIVAESSKLAGIMGELRGERLNQLRKSVADTVGVSVEELEGIVVPLEKVYSLADHTRCILFMLGDGLVPSNAGAGYLARLMIRRSLRLAEELELGLDLYDLVEMHKKILGFEFDVPLSTVQEILELEKERYRTTVSKGTRLVERLVERKKKLEKDDLIELYDSHGIPVELAVGIAAEKGAEVEMPKDIYAELAKRHSKAEKVQEKKITLQNEYPATEKLYYDDPTLLEFEAEVIGVEGDFVILNRSAFYPESGGQDNDVGYLIANGGKFEVVDVLEADGVVLHVVKGAKPEVGTKVKGVIDSDVRWRHMRHHSATHVLLYSLQKVLGNHVWQAGARKEFSKARLDVTHFRRPSEEEIKEIEMLANREILANKPIKWEWMDRIEAERKFGFRLYQGGVPPGRKIRVVQVGDDVQACGGTHCRSTGEIGMLKILKVESIQDGVIRFEFAAGEAAIEAVEEMERLLREASSILRVEPAKLPKTVERFFEEWKDQRKEIERLKSVIADLWADILMERAEEFDSMKVVAEVVDADMQALQKLAERLAEKGAVGCLMAKGEGKVFVVTFSGQKYDARELLREIGRVAKGSGGGRKDVAQGAVQQLLDREEMLDVIFRFLSEHEG
Protein: Centaurin beta 1A, isoform B (Q7KS50)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQNRHMSVNRYCDSNTNSTSNKIEGYLFKKKSKGFKTWCRRWFYLSDNQLVYSDLDSHCRKRSNEDSFSVMEEDLRICSVRPVNEGDRRFCFEVISPTKSHILQADSADMLSLWISALQHSIGAAIQHDSTHHSRPQSTNAPNNSLPAKRRIHWEEFLKIPGNAYCCDCRSPEPRWASINLGITLCIECSGVHRSLGVHYSKVRSLTLDAWESENVKVMMELGNEVVNRIYEARIGDDCGLKKPTEQCEIGVREAWIKAKYVERRFVCGMPKPQELLASETAEVLSIDSGGVVEDGESGGSGIAKRATLSLGGTRKWAVKKLRRRQKQRSIPKTLSDDPSIYNTAKTGDELEDDDDDESINIPSMSLSISRDDLLVIGDDLALDRLETPGILGSDQESTDGESDAESPEELPFSQLDANQLLYMASVVHNLPVMCMAFALGADKMWKNPQDRQRSFLHQAVISGSVMACEFLLLNGAAIDAVDEMGYSALHISTAKGHIAQVYLLLKHKAAYDLSSSDGKKALDIAVDQENADIVTLLRLTQLNDEIGPNDEYNGEDETYKNVMKDFSKLPASQTRVLRQRHDSNTLESQRSSLTNSD
Protein: MutL C-terminal dimerisation domain-containing protein (Q3TRU3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
KRIATLENKTRQNPGDSETIRKKTVGSLYTDASDGPCYSKSVESVLQDSNNSAYLEPRVSEEEVAKTSHSGENEKWKKSFLENKTSGRIHETSPKMFSSPIQMHHLLEEREADLEMQTISSTVNVMAANIPQNNDIPSQLEKWKDAPEVGCQPLPFETTLLRVRGTQRKKERRKKEPSSRGRVNVFSYGQVKLCSTGFITHVVQSEHAKSTETEHSFKNYARPGPVSAQETFGKRTHHAIETPDSSDLTSTLSKESSQPPNKRFCRTNTGYGTENKPVATDDNLALFQESCKESHTDRLLPDASSFPWCRYVSDGCRKIDKRGSFKQVVRRKLSLRSQVGSLEKFKRQYGKVSSSLDTEKDNNTEVRTHLEPQNEPDVLLKDKSHLDMSDGCEITTVEHSETCQPLSPILYPEKILFSKEDRLEQMPHLRESPITLEELSHCNRKADVEKSAASLASKLSKLKDSEKEMQTVGMTGHTSELPDSNPSWKDNSQCTRLDLDFCELLKNKLEKIESDMLPMADSATEDGPINKNSELHPNNTTDDTEKPETPLLFPCNDSKISRDSDVLIRTSEQPTGNPDSVGKVIMSQVEDGIGSQGGVCPQGDESKARSCSKNEPNAHCMDWQQHFDVTLGRMVYINRMTGLSTFVAPTDDLHTACTKDLTTVAVDVLLGNDAVDAAAAAVSEPLQSLFSEWSNPVFARYPEVAVDVSSGQAESLAVKIHNVLYPYRFTKEMIHSVKVLQQVDNKFIACLMSTRMDEDGRTGGNLLVLVDQHAAHERIRLEQLITDSYEKQDPQSAGRKKLLSSTIIPQLAITVSEEQRRLLRSYHKHLEDLGLELLFPDASDSLILVGKVPLCFVEREASELRRGRSTVTKSIVEELIREQVELLQTTGGIQGTLPLTVQKVLASQACHGAIKFNDRLSLEESCRLIEALSLSQLPFQCAHGRPSMLPLADLDHLEQEKQVKPNLAKLRKMVRAWHLFGKTEQNLQQPIRPCEPP
Protein: Protein psiF (Discoidin-inducing complex subunit A) (Q7YSJ4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Acts as a quorum sensing protein regulating discoidin gene expression during growth and development. D.discoideum is a single-celled amoebae and switches to multicellular development when food becomes limited. As the growing cells reach a high density, they begin expressing discoidin genes. The ability of psiF/dicA to induce discoidin gene expression when present in conditioned medium, suggests that it allows cells to sense their local density.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:15947191}.
Interaction partners:
- Discoidin-inducing complex subunit B
Sequence:
MKYLFIAIILILYCSFTKADQKKFLVNMYDNDPLFSPDFENANGAQTGLVKKKLGSDGKPIPANYDMKDPNGNYYIKNATTFKSWFNEVAGVSILVPFELVLTQTAGSQNYYSYSNTSFFPLNELGWYNPSIKGDYEFKKYQDSNKKEQNFHFCMHASFIMSTNCKEVFKFKGDDDVWVFINDVLVLDIGGVHGVQDGTVDMANLPEKIHDSTNSKLGNCKNGTYPFDFFYCERHTKASNCLFETNMGFTCSYYDYCGICNGKGECCTDVKLNQCYTKKCPLPNSLPNGATNYQDYMTIVPTNTCGGTDKCKIYSCNNSTGCEFKQKSCDDGDKCTKDACDSKTGYCSNIPTNPSVVTSCLKSGCDSTTGNYSTPTNCDDKDPCTIDSCINGQGCVHTKACDDEDPCTTDSCSADGKCTHTAIAKCNSDCPSCPSKKCKITSCSEDSGACNYVDMVFASPSECYKATCDPETEEAIYSPIDSSCDTSDSCFTAQCNLNKTCTRVPAINCDDNNECTTDSCSGGSCSNTAIACDDNDPCTIDTCSPSEGCIFTPIVCEQTSLCNTFTCSVGKCVPTPITCSSSVKCQDSICREGVGCVYFNRTCPPDDDCSSAYCSMETGKCISKAYDPLPFSCQSTAVKVGVGIGAAAAAGIAIGGAVAAGLAIFGGKKAYDTWKTSRGNVMTGSQSNPLYTQNQNNGNNPLYSAPAE
Protein: T-cell surface antigen CD2 (LFA-2) (LFA-3 receptor) (OX-34 antigen) (T-cell surface antigen T11/Leu-5) (CD antigen CD2) (P08921)
Organism: Rattus norvegicus (Rat)
Function: CD2 interacts with lymphocyte function-associated antigen CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.
Subcellular location: Cell membrane {ECO:0000269|PubMed:3102667}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- CD48 antigen
- T-cell surface glycoprotein CD4
- T-cell surface glycoprotein CD5
- Intercellular adhesion molecule 1
- T-cell surface glycoprotein CD3 epsilon chain
- T-cell surface glycoprotein CD3 delta chain
- T-cell-specific surface glycoprotein CD28
- T-cell surface glycoprotein CD8 alpha chain
- Proto-oncogene tyrosine-protein kinase LCK
- CD2-associated protein
Sequence:
MRCKFLGSFFLLFSLSSKGADCRDSGTVWGALGHGINLNIPNFQMTDDIDEVRWERGSTLVAEFKRKMKPFLKSGAFEILANGDLKIKNLTRDDSGTYNVTVYSTNGTRILNKALDLRILEMVSKPMIYWECSNATLTCEVLEGTDVELKLYQGKEHLRSLRQKTMSYQWTNLRAPFKCKAVNRVSQESEMEVVNCPEKGLPLYLIVGVSAGGLLLVFFGALFIFCICKRKKRNRRRKGEELEIKASRMSTVERGPKPHSTQASAPASQNPVASQAPPPPGHHLQTPGHRPLPPSHRNREHQPKKRPPPSGTQVHQQKGPPLPRPRVQPKPPCGSGDVSLPPPN
Protein: Pumilio homology domain family member 4 (P25339)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Is not essential for haploid growth, but may affect diploid formation.
Interaction partners:
- Pumilio homology domain family member 6
- Suppressor protein MPT5
- Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1
- Homothallic switching endonuclease
- mRNA-binding protein PUF3
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Poly
- ATP-dependent RNA helicase DHH1
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
Sequence:
MSTKGLKEEIDDVPSVDPVVSETVNSALEQLQLDDPEENATSNAFANKVSQDSQFANGPPSQMFPHPQMMGGMGFMPYSQMMQVPHNPCPFFPPPDFNDPTAPLSSSPLNAGGPPMLFKNDSLPFQMLSSGAAVATQGGQNLNPLINDNSMKVLPIASADPLWTHSNVPGSASVAIEETTATLQESLPSKGRESNNKASSFRRQTFHALSPTDLINAANNVTLSKDFQSDMQNFSKAKKPSVGANNTAKTRTQSISFDNTPSSTSFIPPTNSVSEKLSDFKIETSKEDLINKTAPAKKESPTTYGAAYPYGGPLLQPNPIMPGHPHNISSPIYGIRSPFPNSYEMGAQFQPFSPILNPTSHSLNANSPIPLTQSPIHLAPVLNPSSNSVAFSDMKNDGGKPTTDNDKAGPNVRMDLINPNLGPSMQPFHILPPQQNTPPPPWLYSTPPPFNAMVPPHLLAQNHMPLMNSANNKHHGRNNNSMSSHNDNDNIGNSNYNNKDTGRSNVGKMKNMKNSYHGYYNNNNNNNNNNNNNNNSNATNSNSAEKQRKIEESSRFADAVLDQYIGSIHSLCKDQHGCRFLQKQLDILGSKAADAIFEETKDYTVELMTDSFGNYLIQKLLEEVTTEQRIVLTKISSPHFVEISLNPHGTRALQKLIECIKTDEEAQIVVDSLRPYTVQLSKDLNGNHVIQKCLQRLKPENFQFIFDAISDSCIDIATHRHGCCVLQRCLDHGTTEQCDNLCDKLLALVDKLTLDPFGNYVVQYIITKEAEKNKYDYTHKIVHLLKPRAIELSIHKFGSNVIEKILKTAIVSEPMILEILNNGGETGIQSLLNDSYGNYVLQTALDISHKQNDYLYKRLSEIVAPLLVGPIRNTPHGKRIIGMLHLDS
Protein: Cytochrome c oxidase subunit 6C (Cytochrome c oxidase polypeptide VIc) (Q9CPQ1)
Organism: Mus musculus (Mouse)
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:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000269|PubMed:34616041}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 7B, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit 9
- Cytochrome c oxidase subunit 1
Sequence:
MSSGALLPKPQMRGLLAKRLRVHIAGAFIVALGVAAAYKFGVAEPRKKAYAEFYRNYDSMKDFEEMRKAGIFQSAK
Protein: NAD(P) transhydrogenase subunit beta (EC 7.1.1.1) (Nicotinamide nucleotide transhydrogenase subunit beta) (Q72GS0)
Organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
Sequence:
MDLIQAAYFVVAILFIVGLKRMAHPTTAKSGIVWAGWGMVLAVLATFFWPGMGNFALILLALLLGSVVAWWAAVRVAMTDMPQMVAIYNGMGGGAAATIAAVELLKGAFENTGLMALAILGGLIGSVAFTGSLIAFAKLQGIMKSRPILFPGQKAVNALVLALTVVIGLSLLWNDATASIVLFFLLALLFGVLMTLPIGGGDMPVAISFYNAFTGMAVGFEGFAVGNPALMVAGTLVGAAGTLLTVLMARAMNRSVWSVLVGGFGVEQEAGEVKGSLKPIDVEDAAVMLAYAGKVVFVPGYGMALSQAQHKLKELADLLEARGVEVKFAIHPVAGRMPGHMNVLLAEAGVDYDKLKDLEEINPEFPTVDVAVVIGANDVVNPAARRPGSPLYGMPILDVDKAKNVIVIKRGQGKGFAGVENELFYAENTRMLYGDAQKVLTELIQALKRL
Protein: Phosphatidylinositol 4-kinase beta 1 (PI4-kinase beta 1) (PtdIns-4-kinase beta 1) (EC 2.7.1.67) (Phosphatidylinositol 4-OH kinase beta1) (AtPI4Kbeta1) (PI-4Kbeta1) (Q9FMJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5-trisphosphate. Necessary for proper organization of the trans-Golgi network (TGN) and post-Golgi secretion in root hairs. Together with PI4KB2, required during polarized root hair expansion and pollen tube elongation. Functions redundantly with PI4KB2 upstream of the cold response phosphoinositide-dependent phospholipase C (PI-PLC) pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16649109, ECO:0000269|PubMed:21134079}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:16567499, ECO:0000269|PubMed:21134079}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12805633}; Peripheral membrane protein {ECO:0000269|PubMed:12805633}; Cytoplasmic side {ECO:0000269|PubMed:12805633, ECO:0000269|PubMed:18433157}. Note=Associated to tip-localized membranes in growing root hairs. {ECO:0000269|PubMed:16567499}.
Interaction partners:
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Phosphoinositide phosphatase SAC7
- Phosphatidylinositol 4-phosphate 5-kinase 1
- Phosphatidylinositol 4-kinase alpha 1
- Phosphatidylinositol 4-kinase alpha 2
- 1-phosphatidylinositol-3-phosphate 5-kinase FAB1B
- 1-phosphatidylinositol-3-phosphate 5-kinase FAB1A
- Phosphatidylinositol 4-phosphate 5-kinase 2
- Ras-related protein RABA4b
Sequence:
MPMGRFLSLVRGDSAESPREITSQSNIIGDTGSNGWLIRFFDSAFFCEWIAVSYLYKHPHAGVRDYLCNRMYTLPLSGIESYLFQICYMMVHKPSPSLDKFVIDICGKSLKIALKVHWFLLAELEDADDNEGISRIQEKCQIAATLMGEWSPLMRPQNEVSTPGSKNQVLNRLLSSKQKLFSLKLSPPTQKSLSFSPSPGTNVQDDGSQLPAEDNKIFKKLIPSPKVRDALMFRKSADKDDEESEKEGFFKRLLRDSKGEGDEPIPNSEGFFKRLLKDNKSEDEDITNSSEGFFKRLLSSKGESEELTSSSDGLFKRLLRDNKGDEEELGANSDSFFKRLLRESKNEDEESNPNSEGFFKKLFRDSKPEDDKVPKEVDDEDKDGFLKKLFREKNDDKRHGSEKNEANGTVYADKKSGEEDEREGFFKKFFKEKSDDKKDIVKVDDGNESEGDESPEFSLFKRLFRIHPEDAKPTSENENSSNGLVESSPGTENFFRKLFRDRDQSVEDSELFGSKKHKEKRPGSPKQRDDTPSGKPPLPNNTASQFRKGAYHESLEFVQALCETSYGLVDIFPIEDRKIGLRESLAEINFHLSEAEITGGICFPMGRGVFRVVHIPEDECILLNSREKAPYMISVEVLKAETPSAKESSNSQKLSKGGIPLANGDAFLQKPPPWAYPLWTTQEVYRNSADRMSLSTAQAIDQAMTPKSEVKVKLVNVSLSVEDRTSALESFGDPIDDVLGEAPRTGLNNDLEWVRVVVTADPGLRMESIPDPSVPRKKEHRRVPSTVAMEEVRAAAAKGEAPPGLPLKGAGQDSSDAQPRANGGMLKEGDALSGELWEGKRDRIRKASIYGKLPGWDLRSIIVKSGDDCRQEHLAVQLISHFYDIFQEAGLPLWLRPYEVLVTSSYTALIETIPDTASIHSIKSRYPNITSLRDFFVAKYKENSPSFKLAQRNFVESMAGYSLVCYLLQVKDRHNGNLLLDEEGHIIHIDFGFMLSNSPGGVNFESAPFKLTRELLEVMDSDADGVPSEFFDYFKVLCIQGFLTCRKHAERIILLVEMLQDSGFPCFKGGPRTIQNLRKRFHLSLTEEQCVSLVLSLISSSLDAWRTRQYDYYQRVLNGIL