wanglab/gogpt-training-data huggingface dataset:
Protein: Choline-phosphate cytidylyltransferase (EC 2.7.7.15) (CTP:phosphocholine cytidylyltransferase) (CCT) (CT) (Phosphorylcholine transferase) (P13259)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis.
Subcellular location: Membrane. Note=Most of its activity is membrane-associated.
Interaction partners:
- Cholinephosphotransferase 1
- Choline kinase
- Importin subunit alpha
- Vesicle-associated membrane protein-associated protein SCS2
- Ethanolamine kinase
- SEC14 cytosolic factor
- Importin subunit beta-1
- Vesicle-associated membrane protein-associated protein SCS22
- Choline/ethanolaminephosphotransferase 1
- Inositol-3-phosphate synthase
Sequence:
MANPTTGKSSIRAKLSNSSLSNLFKKNKNKRQREETEEQDNEDKDESKNQDENKDTQLTPRKRRRLTKEFEEKEARYTNELPKELRKYRPKGFRFNLPPTDRPIRIYADGVFDLFHLGHMKQLEQCKKAFPNVTLIVGVPSDKITHKLKGLTVLTDKQRCETLTHCRWVDEVVPNAPWCVTPEFLLEHKIDYVAHDDIPYVSADSDDIYKPIKEMGKFLTTQRTNGVSTSDIITKIIRDYDKYLMRNFARGATRQELNVSWLKKNELEFKKHINEFRSYFKKNQTNLNNASRDLYFEVREILLKKTLGKKLYSKLIGNELKKQNQRQRKQNFLDDPFTRKLIREASPATEFANEFTGENSTAKSPDDNGNLFSQEDDEDTNSNNTNTNSDSDSNTNSTPPSEDDDDNDRLTLENLTQKKKQSAN
Protein: At5g03545 (Expressed in response to phosphate starvation protein) (Q9LZD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g21930
- Uncharacterized protein F28O16.11
- Uncharacterized protein
- soluble epoxide hydrolase
- Exocyst complex component SEC8
- Exocyst complex component SEC6
- Purple acid phosphatase 17
- Protein PHOSPHATE STARVATION RESPONSE 1
- Pectinesterase inhibitor 10
Sequence:
MVMMMMMRIVCEWSDEDCMKVDEDKLDVSFVIPRLGNFDPLASFGSPRNQQIMITIALICLCSVFTLFPV
Protein: Transcription factor GATA-4 (GATA-binding factor 4) (A0A087WZ09)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYQSLPWPPTTGRPPVPTRRAAPAPSCTARAPRPRQSTCPHRGALLRAGPVLPPGRRRGLCVRRASGGSSGGAASGAGPGTQQGSPGWSQAGADGAAYTPPPVSPRFSFPGTTGSLAAAAAAAAAREAAAYSSGGGAAGAGLAGREQYGRAGFAGSYSSPYPAYMADVGASWAAAAAASAGPFDSPVLHSLPGRANPAARHPNLDMFDDFSEGRECVNCGAMSTPLWRRDGTGHYLCNACGLYHKMNGINRPLIKPQRRLSASRRVGLSCANCQTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMRKEGIQTRKRKPKNLNKSKTPAAPSGSESLPPASGASSNSSNATTSSSEEMRPIKTEPGLSSHYGHSSSVSQTFSVSAMSGHGPSIHPVLSALKLSPQGYASPVSQSPQTSSKQDSWNSLVLADSHGDIITA
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.27) (E7ET89)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367105}.
Interaction partners:
Sequence:
MRAVRRHLFPQHSAPGRGVVWEWLSDDGSWTAYEASVCDYLEQQVARGNQLVDLAPLGYNYTVNYTTHTQTNKTSSFCRSVRRQAGPPYPVTTIIAPPGHTGVACSCHQCLSGSRTGPVSGRYRHSMTNLPAYPVPQHPPHRTASVFGTHQAFAPYNKPSLSGARSAPRLNTTNAWGAAPPSLGSQPLYRSSLSHLGPQHLPPGSSTSGAVSASLPSGPSSSPGSVPATVPMQMPKPSRVQQALAGMTSVLMSAIGLPVCLSRAPQPTSPPASRLASKSHGSVKRLRKMSVKGATPKPEPEPEQVIKNYTEELKVPPDEDCIICMEKLSTASGYSDVTDSKAIGSLAVGHLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYGEKTGTQPQGKMEVLRFQMSLPGHEDCGTILIVYSIPHGIQGPEHPNPGKPFTARGFPRQCYLPDNAQGRKVLELLKVAWKRRLIFTVGTSSTTGETDTVVWNEIHHKTEMDRNITGHGYPDPNYLQNVLAELAAQGVTEDCLEQQ
Protein: Cytochrome c (P00046)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Subcellular location: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 7
- Elongation factor Tu
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase polypeptide 5, mitochondrial
- Cytochrome b-c1 complex subunit 9
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 4, mitochondrial
Sequence:
MPYAPGDEKKGASLFKTRCAQCHTVEKGGANKVGPNLHGVFGRKTGQAEGFSYTEANRDKGITWDEETLFAYLENPKKYIPGTKMAFAGFKKPADRNNVITYLKKATSE
Protein: ATP-dependent RNA helicase (Q38DJ1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MASAPRLGRKGGKITASPIIPTHALTPGSSTSPVSLHTPGEGTTIIGDPNAAHPFGSDMLTVTKKQTSAEANVLQFDVGAIQLLGKGVVVGRAKQARTRTYQPQSDATEVRQRLHGVFSTRRSKVPHRAASAGLDALQESEVVATRKSQDTLSLVAALLSADRMANILVVVSKYYELSHVRSSVEAILREEGEDTQSVGVLFGQTFEGSKSTRAWVMTADMALLYMTQLGSPAPFTHVVVPCCVDTTSSLSCFLKMLGGWMMSNTPRSQSVRLVVTTDCSSDGHVARTIGVPRVKILDDKVIRLHEFSYNEVCALLGKQTMEMDKDAAGKFPSPPKRLVDYTADVAAELVRYVVTHTPTAQIFSIFTADVREVLTALQGAKIEDCTVYSTLKSAADKVETKHRVHVINHVSHALDTENEFTMVLDMGTIRRSSVQHKSESFIAASTTEWESKAEQAERKSILGENTTCCYFALFQDDVGASFQDEAQFLPDIFNVENAFVQCARLNLSVCEVGRLLPSVPRDVVDQVMQKVAEKCMISTPDSLDITFLGEIKSRLPVEIDVAYLIMGGCSLGLGEATLVVSAVIALPFRSTAPPTYTVNRWTEATQESRKRCAGDIALSSDLLADAFVFLEWLRLRTTGAATATFLEAFLVQEFKFEKIEGLMNHMRDQLMNYAFLDRLDDVDTVNKVAESLRENASTMLMLLSMALSRRAAFIRDAGHINEKDRHASMVFVRTSKQLVVHPFIPSGARWETGGIVIPVILKNSTTILGGMFSLVDTSLFFASLLLLYPQIEYSRPVTTERGRVVYFGVACNWQMKRFVVSIDDATQILDFRENINTAIGCMRALRMLPHPISKTRFAIALKEHDRFFDMERLHRETQRRLHSLAAALNVQEHQGSFETFAKHYTAPKEIIPFNDVAATDVLLLRRFADGTLWDEQRPSPQSAPAIGSSPQKSAVLTPFDTAIPAPYDDDDDDVQIIQNSYFMLHGPLIEDDDDD
Protein: SUF system FeS cluster assembly SufBD core domain-containing protein (Q72DA8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- SUF system FeS assembly ATPase SufC, putative
- Nitrogen fixation protein NifU
Sequence:
MSFKKVDLSRYQFDGAQASSIGDLTQLDAADKQRLLYAGIDVNQQNLAGSFMHMNHSGVHCTSRQEGLEILDIKQALDTYHGLPDYFWKLVDRNKDEYTRAADEHLHGGYFIRARAGAKIEAPVQSCLFIKGNGVGQNVHNVVVVEEGAEMHIITGCATAHDTRSVAHLGISEFYVHKGGKLTFTMIHNWGEEAAVRPRSAGYLEEDAVFLSNYVLLKPVTDLQMYPTITLGGRGSVARFNSVIVAPTGSYVDTGNRILLEAPDTRGEIIARTMTTGGTIINRGHIAGHAVPARGHLECKGLILGGGVIHAIPELEGTQDGVELSHEAAVGKIAQEEIEYLMARGLDEDEATSTIVRGFLNVDIMGLPEELEKAVEEQINQLDAGDAM
Protein: Probable hydrolase nit2 (EC 3.5.-.-) (O94660)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Bis
- Large ribosomal subunit protein eL31
Sequence:
MTLAAVAQLNSSGSILKNLAICKELISQAAAKGAKCIFFPEASDFIAHNSDEAIELTNHPDCSKFIRDVRESATKHSIFVNICVHEPSKVKNKLLNSSLFIEPLHGEIISRYSKAHLFDVEIKNGPTLKESNTTLRGEAILPPCKTPLGKVGSAICFDIRFPEQAIKLRNMGAHIITYPSAFTEKTGAAHWEVLLRARALDSQCYVIAPAQGGKHNEKRASYGHSMIVDPWGTVIAQYSDISSPNGLIFADLDLNLVDHVRTYIPLLRRNDLYPTI
Protein: acid phosphatase (EC 3.1.3.2) (Q8ING6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FAD synthase
- FAD synthase
- Low molecular weight phosphotyrosine protein phosphatase 1
- Low molecular weight phosphotyrosine protein phosphatase 2
- GH19849p
- acid phosphatase
- Putative riboflavin kinase
- Thiamine pyrophosphokinase 1
- IP06402p
Sequence:
MKVLFVCIGNTCRSPMAEAILKHLVVKRNLQDWYVDSAGLRSWNVGLEPQARGQQLLKQHGLKTNHLGRMISAQDFYDFDYIFAMDNSNLLELEHMAASLTPSPTCKIQLLGSYIGRKEDEIIEDPYFIQGMGGFNAAYLQILESCERFLQHYKSDDKELSLGS
Protein: RING finger protein 151 (Q2KHN1)
Organism: Homo sapiens (Human)
Function: May be involved in acrosome formation of spermatids.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9CQ29}. Nucleus {ECO:0000250|UniProtKB:Q9CQ29}.
Interaction partners:
Sequence:
MGGGYDLNLFASPPDSNFVCSVCHGVLKRPARLPCSHIFCKKCILRWLARQKTCPCCRKEVKRKKVVHMNKLRKTIGRLEVKCKNADAGCIVTCPLAHRKGHQDSCPFELTACPNEGCTSQVPRGTLAEHRQHCQQGSQQRCPLGCGATLDPAERARHNCYRELHNAWSVRQERRRPLLLSLLRRVRWLDQATSVVRRELAELSNFLEEDTALLEGAPQEEAEAAPEGNVGAEVVGEPRANIPCK
Protein: ATP synthase subunit delta', mitochondrial (F-ATPase delta' subunit) (Q96252)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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 turnover 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(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit O, mitochondrial
- ATP synthase subunit beta-2, mitochondrial
- ATP synthase subunit beta-3, mitochondrial
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit 9
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit gamma, mitochondrial
Sequence:
MFKQASRLLSRSVAAASSKSVTTRAFSTELPSTLDSTFVEAWKKVAPNMDPPQTPSAFMKPRPSTPSSIPTKLTVNFVLPYTSELTGKEVDMVIIPASTGQMGVLPGHVPTIAELKPGIMSVHEGTDVKKYFLSSGFAFLHANSVADIIAVEAVPLDHIDPSQVQKGLAEFQQKLASATTDLEKAEAQIGVEVHSAINAALSG
Protein: ILK associated serine/threonine phosphatase (Integrin-linked kinase associated phosphatase) (F8SNU7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLFGDLPEPERSPRPAAGKEAQKGPLLFDDLPPASSTDSGSGGPLLFDDLPPASSGDSGDVISVEKTVKRCLLDTFKHTDEEFLKQASSQKPAWKDGSTATCVLAVDNILYIANLGDSRAILCRYNEESQKHAALSLSKEHNPTQYEERMRIQKAGGNVRDGRVLGVLEVSRSIGDGQYKRCGVTSVPDIRRCQLTPNDRFILLACDGLFKVFTPEEAVNFILSCLEDEKIQTREGKSAADARYEAACNRLANKAVQRGSADNVTVMVVRIGH
Protein: Protocadherin alpha-7 (PCDH-alpha-7) (Q9UN72)
Organism: Homo sapiens (Human)
Function: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination. Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q91Y13}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q91Y13}.
Interaction partners:
- Protocadherin alpha-4
- Protocadherin alpha-10
- Protocadherin alpha-6
- Protocadherin alpha-9
- Protocadherin alpha-2
Sequence:
MVCPNGYDPGGRHLLLFIIILAAWEAGRGQLHYSVPEEAKHGNFVGRIAQDLGLELAELVPRLFRAVCKFRGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVERPLQVFHVDVEVKDINDNPPVFPATQRNLFIAESRPLDSRFPLEGASDADIGENALLTYRLSPNEYFFLDVPTSNQQVKPLGLVLRKLLDREETPELHLLLTATDGGKPELTGTVQLLITVLDNNDNAPVFDRTLYTVKLPENVSIGTLVIHPNASDLDEGLNGDIIYSFSSDVSPDIKSKFHMDPLSGAITVIGHMDFEESRAHKIPVEAVDKGFPPLAGHCTVLVEVVDVNDNAPQLTLTSLSLPIPEDAQPGTVITLISVFDRDFGVNGQVTCSLTPRVPFKLVSTFKNYYSLVLDSALDRESVSAYELVVTARDGGSPSLWATASVSVEVADVNDNAPAFAQPEYTVFVKENNPPGCHIFTVSAGDADAQKNALVSYSLVELRVGERALSSYVSVHAESGKVYALQPLDHEELELLQFQVSARDAGVPPLGSNVTLQVFVLDENDNAPALLAPRVGGTGGAVRELVPRSVGAGHVVAKVRAVDADSGYNAWLSYELQPVAAGASIPFRVGLYTGEISTTRALDETDAPRHRLLVLVKDHGEPSLTATATVLVSLVESGQAPKASSRASLGIAGPETELVDVNVYLIIAICAVSSLLVLTLLLYTALRCSAPSSEGACSLVKPTLVCSSAVGSWSFSQQRRQRVCSGEGPPKTDLMAFSPSLPQGPSSTDNPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPTNSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
Protein: Vitamin D3 receptor (VDR) (1,25-dihydroxyvitamin D3 receptor) (Nuclear receptor subfamily 1 group I member 1) (P11473)
Organism: Homo sapiens (Human)
Function: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells. Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3-responsive target genes. Plays a central role in calcium homeostasis (By similarity). Also functions as a receptor for the secondary bile acid lithocholic acid (LCA) and its metabolites.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:16207705, ECO:0000269|PubMed:28698609}. Cytoplasm {ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:16207705, ECO:0000269|PubMed:28698609}. Note=Localizes mainly to the nucleus (PubMed:12145331, PubMed:28698609). Translocated into the nucleus via both ligand-dependent and ligand-independent pathways; ligand-independent nuclear translocation is mediated by IPO4 (PubMed:16207705). {ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:16207705, ECO:0000269|PubMed:28698609}.
Interaction partners:
Sequence:
MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAALIEAIQDRLSNTLQTYIRCRHPPPGSHLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPECSMKLTPLVLEVFGNEIS
Protein: Nuclear transport factor 2 (NTF-2) (A8JUT4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU369002}. Nucleus {ECO:0000256|RuleBase:RU369002}.
Interaction partners:
Sequence:
MSLNPQYEDIGKGFVQQYYAIFDDPANRANVVNFYSATDSFMTFEGHQIQGAPKILEKVQSLSFQKITRVITTVDSQPTFDGGVLINVLGRLQTDEDQPHAYIQTFVLKPVGGSFFVQHDIFRLSLHDV
Protein: Leukocyte tyrosine kinase receptor (EC 2.7.10.1) (P08923)
Organism: Mus musculus (Mouse)
Function: Receptor with a tyrosine-protein kinase activity. Following activation by ALKAL1 or ALKAL2 ligands at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, leading to activation of the mitogen-activated protein kinase (MAPK) pathway (By similarity). Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (By similarity). The exact function of this protein is not known; studies with chimeric proteins demonstrate its ability to promote growth and specifically neurite outgrowth, and cell survival. Involved in regulation of the secretory pathway involving endoplasmic reticulum (ER) export sites (ERESs) and ER to Golgi transport (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:2836739, ECO:0000269|PubMed:8995435}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform A]: Endoplasmic reticulum {ECO:0000305|PubMed:8380920}. Note=Retained in the endoplasmic reticulum. {ECO:0000305|PubMed:8380920}.; SUBCELLULAR LOCATION: [Isoform B]: Endoplasmic reticulum {ECO:0000305|PubMed:8380920}. Note=Retained in the endoplasmic reticulum. {ECO:0000305|PubMed:8380920}.
Interaction partners:
- ALK and LTK ligand 2
Sequence:
MGCSHRLLLWLGAAGTILCSNSEFQTPFLTPSLLPVLVLNSQEQKVTPTPSKLEPASLPNPLGTRGPWVFNTCGASGRSGPTQTQCDGAYTGSSVMVTVGAAGPLKGVQLWRVPDTGQYLISAYGAAGGKGAQNHLSRAHGIFLSAVFFLRRGEPVYILVGQQGQDACPGGSPESQLVCLGESGEHATTYGTERIPGWRRWAGGGGGGGGATSIFRLRAGEPEPLLVAAGGGGRSYRRRPDRGRTQAVPERLETRAAAPGSGGRGGAAGGGSGWTSRAHSPQAGRSPREGAEGGEGCAEAWAALRWAAAGGFGGGGGACAAGGGGGGYRGGDTSESDLLWADGEDGTSFVHPSGELYLQPLAVTEGHGEVEIRKHPNCSHCPFKDCQWQAELWTAECTCPEGTELAVDNVTCMDLPTTASPLILMGAVVAALALSLLMMCAVLILVNQKCQGLWGTRLPGPELELSKLRSSAIRTAPNPYYCQVGLSPAQPWPLPPGLTEVSPANVTLLRALGHGAFGEVYEGLVTGLPGDSSPLPVAIKTLPELCSHQDELDFLMEALIISKFSHQNIVRCVGLSFRSAPRLILLELMSGGDMKSFLRHSRPHPGQLAPLTMQDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCSGASRVAKIGDFGMARDIYQASYYRKGGRTLLPVKWMPPEALLEGLFTSKTDSWSFGVLLWEIFSLGYMPYPGHTNQEVLDFIATGNRMDPPRNCPGPVYRIMTQCWQHQPELRPDFGSILERIQYCTQDPDVLNSPLPVEPGPILEEEEASRLGNRSLEGLRSPKPLELSSQNLKSWGGGLLGSWLPSGLKTLKPRCLQPQNIWNPTYGSWTPRGPQGEDTGIEHCNGSSSSSIPGIQ
Protein: Uncharacterized fimbrial-like protein YbgD (P37909)
Organism: Escherichia coli (strain K12)
Subcellular location: Fimbrium {ECO:0000305}.
Interaction partners:
- Uncharacterized fimbrial chaperone YbgP
- Cell division protein YtfB
Sequence:
MFKGQKTLAALAVSLLFTAPVYAADEGSGEIHFKGEVIEAPCEIHPEDIDKNIDLGQVTTTHINREHHSNKVAVDIRLINCDLPASDNGSGMPVSKVGVTFDSTAKTTGATPLLSNTSAGEATGVGVRLMDKNDGNIVLGSAAPDLDLDASSSEQTLNFFAWMEQIDNAVDVTAGEVTANATYVLDYK
Protein: Testis-specific serine/threonine-protein kinase 2 (TSK-2) (TSK2) (TSSK-2) (Testis-specific kinase 2) (EC 2.7.11.1) (DiGeorge syndrome protein G) (DGS-G) (Serine/threonine-protein kinase 22B) (Q96PF2)
Organism: Homo sapiens (Human)
Function: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates TSKS at 'Ser-288' and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:18495105}. Note=Present in the cytoplasm of elongating spermatids. In spermatozoa, localizes in the equatorial segment, neck, the midpiece and in a specific sperm head compartment (By similarity). In spermatids, concentrates in centrioles during flagellogenesis. {ECO:0000250}.
Interaction partners:
- Testis-specific serine kinase substrate
Sequence:
MDDATVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHGSIIKTYEIFETSDGRIYIIMELGVQGDLLEFIKCQGALHEDVARKMFRQLSSAVKYCHDLDIVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDSNGRIILSKTFCGSAAYAAPEVLQSIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIRKMLRIQKEHRVDFPRSKNLTCECKDLIYRMLQPDVSQRLHIDEILSHSWLQPPKPKATSSASFKREGEGKYRAECKLDTKTGLRPDHRPDHKLGAKTQHRLLVVPENENRMEDRLAETSRAKDHHISGAEVGKAST
Protein: Thiamine-triphosphatase (EC 3.6.1.28) (E9QBE4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTVEVERKFVCDAEIMRKLQDIGAECVGEREFGDQYFDSPDFLLTLKDFWLRCRDGQWELKSPAVSEAPAETLCTRYREITSLPVIQSEVSKIIRESNCSQRKQIGQTEDTPICSTGDTKWLNELGLVCFAEFRTQRCSYVLEREDGAVRVDLDRADFGYCVGEIEVLVPEGGDVNAALQSITSIAEQLGLNSEKKVKGKMDVFLQRNRPDHYNKLLSAHIL
Protein: Phosphate acetyltransferase EutD (EC 2.3.1.8) (Ethanolamine utilization protein EutD) (P77218)
Organism: Escherichia coli (strain K12)
Function: When expressed independently of the eut operon it can restore growth to a double pta-acs deletion mutant.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:21046341}. Note=It is not clear if this enzyme is found in the cytoplasm or the bacterial microcompartment. {ECO:0000305|PubMed:21046341}.
Interaction partners:
- Acetate kinase
- Acetaldehyde dehydrogenase
- PFL-like enzyme TdcE
- Formate acetyltransferase 1
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Acetyl-coenzyme A synthetase
- Acetaldehyde dehydrogenase
- Acetate kinase EutQ
- Corrinoid adenosyltransferase EutT
- Probable pyruvate-flavodoxin oxidoreductase
Sequence:
MIIERCRELALRAPARVVFPDALDQRVLKAAQYLHQQGLATPILVANPFELRQFALSHGVAMDGLQVIDPHGNLAMREEFAHRWLARAGEKTPPDALEKLTDPLMFAAAMVSAGKADVCIAGNLSSTANVLRAGLRIIGLQPGCKTLSSIFLMLPQYSGPALGFADCSVVPQPTAAQLADIALASAETWRAITGEEPRVAMLSFSSNGSARHPCVANVQQATEIVRERAPKLVVDGELQFDAAFVPEVAAQKAPASPLQGKANVMVFPSLEAGNIGYKIAQRLGGYRAVGPLIQGLAAPMHDLSRGCSVQEIIELALVAAVPRQTEVNRESSLQTLVE
Protein: Eukaryotic translation initiation factor 3 subunit J (eIF3j) (Eukaryotic translation initiation factor 3 30 kDa subunit) (eIF-3 30 kDa) (High-copy suppressor of Rpg1 protein 1) (Q05775)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit B
- Translation initiation factor RLI1
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor eIF-1
- Eukaryotic translation initiation factor 1A
- Small ribosomal subunit protein uS3
Sequence:
MSWDDEAINGSMGNDDAVLMDSWDAEIGDDEPVMQSWDAEEEEKKPAPKPKKEQPKKVKKGKESSADRALLDIDTLDEKTRKELIKKAEMESDLNNAADLFAGLGVAEEHPRARALQKEQEEQALKRPAFTKDTPIETHPLFNAETKREYQDLRKALTAAITPMNKKSPLNYSSSLAIDLIRDVAKPMSIESIRQTVATLNVLIKDKEREERQARLARVRGGTATGGAGKKKVKGKTNLGGAFKKDQDFDLDGPDDFEFGDDDFM
Protein: GH20986p (Q961J2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWDISGALSLLNCYVKWLALGHFPQNTSSYTEGSYTWFSKGWKEAFMSGDQEPWVFRGGLIADLQRLMPVDSGNDLFVYKLPEQPTANYYLLRPYCNSDEQQVNDLCTRLYLQWRGELDGGRHIPFPLPANVPNIVADGLIGGYLTLSPQLCIVAYDESNRIIGYSCAALDVNIFRRNLELCWYTELREKYSRDICPLEGGEEVVQLVTSLVESYHDSSGNGALDQCPVEVSGSFPAVLISGTLREAEERDSGITKRMLTVLLAALRANGCFGAHVRVPQQDVAQVNFYSRIGFVDVYREEATKCIYMGRRF
Protein: Homoserine dehydrogenase (HDH) (EC 1.1.1.3) (Q6FK85)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Homoserine kinase
- Aspartokinase
- Aspartate-semialdehyde dehydrogenase
- Threonine synthase
- Candida glabrata strain CBS138 chromosome J complete sequence
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- cystathionine gamma-lyase
- Branched-chain-amino-acid aminotransferase
- Candida glabrata strain CBS138 chromosome H complete sequence
- Cystathionine beta-synthase
Sequence:
MSNKSVNVAIIGTGVVGSSFLDQIVAMKSNITYNIIYVAELSKALISEDYSPLALGSDWAKAVNGANQGPLALEKLVDFLKKSPIPVILVDNTSSAAIASFYPTFVENGISIATPNKKAFSSDLATWDSLFSGKPTNGLVYHEATVGAGLPILGFLREIIQTGDEIEKIEGIFSGTLSYIFNEFSTTTTNDVKFSDVVKVAKQLGYTEPDPRDDLNGLDVARKVTIVARISGVKVESPTSFPVQSLIPKPLESVESVDEFLQKLPEYDDELTQLKKEAAEENKVLRFIGKVDVATGKPSVGIEKYDHSHPFASLKGSDNVISIKTKRYTNPVVIQGAGAGAAVTAAGILGDVIKAAQRLVGA
Protein: Putative divalent cation/proton antiporter TMEM165 (Transmembrane protein 165) (Transmembrane protein PT27) (Transmembrane protein TPARL) (Q9HC07)
Organism: Homo sapiens (Human)
Function: May function as a calcium/proton transporter involved in calcium and in lysosomal pH homeostasis. Therefore, it may play an indirect role in protein glycosylation.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:P52875}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Calcium-transporting ATPase type 2C member 1
Sequence:
MAAAAPGNGRASAPRLLLLFLVPLLWAPAAVRAGPDEDLSHRNKEPPAPAQQLQPQPVAVQGPEPARVEKIFTPAAPVHTNKEDPATQTNLGFIHAFVAAISVIIVSELGDKTFFIAAIMAMRYNRLTVLAGAMLALGLMTCLSVLFGYATTVIPRVYTYYVSTVLFAIFGIRMLREGLKMSPDEGQEELEEVQAELKKKDEEFQRTKLLNGPGDVETGTSITVPQKKWLHFISPIFVQALTLTFLAEWGDRSQLTTIVLAAREDPYGVAVGGTVGHCLCTGLAVIGGRMIAQKISVRTVTIIGGIVFLAFAFSALFISPDSGF
Protein: Arrestin-related trafficking adapter 5 (P53244)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May regulate endocytosis by recruiting RSP5 ubiquitin ligase activity to specific plasma membrane proteins in response to extracellular stimuli.
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
- Arrestin-related trafficking adapter 3
- Arrestin-related trafficking adapter 6
- Protein LDB19
- Protein ECM21
- Arrestin-related trafficking adapter 10
- Transcription factor CSR2
- Ubiquitin ligase-binding protein BUL2
- Ubiquitin ligase-binding protein BUL1
Sequence:
MFSLSSLSSSGGHSEQKERERISYFDIRINSPYKDIILIQGSPLELSSIPLSGNLVISVKNEIVVKKISLRLVGRFKLEFLQVGRYKKNSSSLASLVKEKRKIFECYWDNLLVSSKGDVLVGGENAENQHNSSSGRSTSNQDMDTSGNAIFLSKRSLSSPVFNKIIRRKTHSSHRKILELPENGVTGTPFEGLRENARSRSSSSNTLNNNSHSYSNRDGSGSSYLFLMKRGNYELPFNTMLPPEVCETIEGLQSGSILYSFEAIIDGRQLWDTDLSVHTSPHGPIGSTSTSGNGMRTKNKIIIKKFKYLRILRTLSMDNLAMQEEISVGNTWRDKLQYETSIPSRAVPIGSTTPVKIKIFPFEKNIRLDRIEMALIQYYAMKDSSAQIYDDEIAVMKITHLADFGPLTDKLDVDCPFTIPDNLKQITQDCCLQDNLIRVMHKLQVRILLQRQVDGEYKNLEIKAQLPMLLFISPHLPMKGRLVLFDKHDGKIHFRPGELVPLFLTTYPAQGLTPGVELNSTTTAHLALPQPPPNYHESTNDHLMPALQPLGADSVVLTVPSYEQAQAQASASSYVTGSVPAYCDDD