wanglab/gogpt-training-data huggingface dataset:
Protein: Regulatory protein PHO2 (General regulatory factor 10) (P07269)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulator in phosphate metabolism and acts as a derepressor of another central regulator PHO5. Binds to the upstream activator sequence (UAS) of PHO5. It also binds to the TRP4, HIS4, and CYC1 promoters.
Subcellular location: Nucleus.
Interaction partners:
- Myb-like DNA-binding protein BAS1
- Phosphate system positive regulatory protein PHO4
- Histidine biosynthesis trifunctional protein
- Transcriptional factor SWI5
- PHO85 cyclin PHO80
- Bifunctional purine biosynthetic protein ADE5,7
- Phosphoribosylaminoimidazole carboxylase
- ATP phosphoribosyltransferase
- General control transcription factor GCN4
- Adenylosuccinate lyase
Sequence:
MMEEFSYDHDFNTHFATDLDYLQHDQQQQQQQQHDQQHNQQQQPQPQPIQTQNLEHDHDQHTNDMSASSNASDSGPQRPKRTRAKGEALDVLKRKFEINPTPSLVERKKISDLIGMPEKNVRIWFQNRRAKLRKKQHGSNKDTIPSSQSRDIANDYDRGSTDNNLVTTTSTSSIFHDEDLTFFDRIPLNSNNNYYFFDICSITVGSWNRMKSGALQRRNFQSIKELRNLSPIKINNIMSNATDLMVLISKKNSEINYFFSAMANNTKILFRIFFPLSSVTNCSLTLETDDDIINSNNTSDKNNSNTNNDDDNDDNSNEDNDNSSEDKRNAKDNFGELKLTVTRSPTFAVYFLNNAPDEDPNLNNQWSICDDFSEGRQVNDAFVGGSNIPHTLKGLQKSLRFMNSLILDYKSSNEILPTINTAIPTAAVPQQNIAPPFLNTNSSATDSNPNTNLEDSLFFDHDLLSSSITNTNNGQGSNNGRQASKDDTLNLLDTTVNSNNNHNANNEENHLAQEHLSNDADIVANPNDHLLSLPTDSELPNTPDFLKNTNELTDEHRWI
Protein: Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (Gamma-Glu-GABA hydrolase) (EC 3.5.1.94) (P76038)
Organism: Escherichia coli (strain K12)
Function: Involved in the breakdown of putrescine via hydrolysis of the gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate.
Interaction partners:
- Gamma-glutamylputrescine synthetase PuuA
- HTH-type transcriptional regulator PuuR
- NADP/NAD-dependent aldehyde dehydrogenase PuuC
- Gamma-glutamylputrescine oxidoreductase
- 4-aminobutyrate aminotransferase PuuE
- Gamma-aminobutyraldehyde dehydrogenase
- 4-aminobutyrate aminotransferase GabT
- Glutamine synthetase
- Putrescine importer PuuP
- Glutamate synthase large chain
Sequence:
MENIMNNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLLEQLLPKLDGIYLPGSPSNVQPHLYGENGDEPDADPGRDLLSMAIINAALERRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAPSHEVQVEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEYALSRILFEGFITACQHHIAEKQRL
Protein: Amino acid ABC transporter ATP binding protein (Q9I405)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004417}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004417}.
Interaction partners:
- Amino acid ABC transporter membrane protein
- Glutamate/aspartate import permease protein GltK
- L-glutamate/L-aspartate-binding protein
- Glutathione hydrolase proenzyme
- Glutaminase-asparaginase
- Amino acid ABC transporter membrane protein
- Putative glutamine transport system permease protein GlnP
- Glutamate/aspartate import permease protein GltK
- Glutamate/aspartate import permease protein GltK
- Probable permease of ABC transporter
Sequence:
MISIKNVSKWYGDFQVLTDCSTEVAKGEVVVVCGPSGSGKSTLIKCVNALEPFQKGDIVVDGTSIADPKTNLPKLRSRVGMVFQHFELFPHLSITENLTIAQIKVLGRSKEEATKKGLALLERVGLKEHAHKHPGQLSGGQQQRVAIARALAMDPVVMLFDEPTSALDPEMVNEVLDVMVQLAHEGMTMMCVTHEMGFARKVANRVIFMDRGQIVEDCEKEEFFGDVSARSERAQQFLAKILPH
Protein: Neudesin (Neuron-derived neurotrophic factor) (SCIRP10-related protein) (Spinal cord injury-related protein 10) (Q6IUR5)
Organism: Rattus norvegicus (Rat)
Function: Acts as a neurotrophic factor in postnatal mature neurons enhancing neuronal survival. Promotes cell proliferation and neurogenesis in undifferentiated neural progenitor cells at the embryonic stage and inhibits differentiation of astrocytes (By similarity). Its neurotrophic activity is exerted via MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT pathways (By similarity). Neurotrophic activity is enhanced by binding to heme (By similarity). Acts also as an anorexigenic neurotrophic factor that contributes to energy balance (By similarity).
Subcellular location: Secreted, extracellular space {ECO:0000250|UniProtKB:Q9CQ45}. Mitochondrion {ECO:0000269|PubMed:31536960}. Endoplasmic reticulum {ECO:0000269|PubMed:31536960}. Note=Localized to mitochondria and endoplasmic reticulum by PINK1 and PARK7. {ECO:0000250|UniProtKB:Q9UMX5}.
Interaction partners:
- Cytochrome b5 type B
- Cytochrome b5
Sequence:
MARPAPWWWLRPLAALALALALVRVPSARAGQMPRPAERGPPVRLFTEEELARYSGEEEDQPIYLAVKGVVFDVTSGKEFYGRGAPYNALAGKDSSRGVAKMSLDPADLTHDISGLTAKELEALDDIFSKVYKAKYPIVGYTARRILNEDGSPNLDFKPEDQPHFDIKDEF
Protein: Histidinol dehydrogenase, chloroplastic (HDH) (EC 1.1.1.23) (Protein HISTIDINE BIOSYNTHESIS 8) (Q9C5U8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Imidazoleglycerol-phosphate dehydratase 1, chloroplastic
- Histidine biosynthesis bifunctional protein hisIE, chloroplastic
- Imidazoleglycerol-phosphate dehydratase 2, chloroplastic
- Histidinol-phosphate aminotransferase 1, chloroplastic
- 1-
- ATP phosphoribosyltransferase 2, chloroplastic
- ATP phosphoribosyltransferase 1, chloroplastic
- Bifunctional phosphatase IMPL2, chloroplastic
- Imidazole glycerol phosphate synthase hisHF, chloroplastic
- Histidinol-phosphate aminotransferase 2, chloroplastic
Sequence:
MSLNLSRLSLLSSPRISISTHAPRKGYVCCSMKSYRLSELSSSQVDSLKSRPRIDFSSIFATVNPIIDAVRSNGDNAVKEYTERFDKVQLNKVVEDMSELSVPELDSNVKEAFDVAYDNIYAFHLAQKSTEKSVENMKGVRCKRVSRSIGSVGLYVPGGTAVLPSTALMLAIPAQIAGCKTVVLATPPSKDGSICKEVLYCAKRAGVTHILKAGGAQAIAAMAWGTDSCPKVEKIFGPGNQYVTAAKMILQNSEAMVSIDMPAGPSEVLVIADEHASPVYIAADLLSQAEHGPDSQVVLVVVGDSVDLNAIEEEIAKQCKSLPRGEFASKALSHSFTVFARDMIEAISFSNLYAPEHLIINVKDAEKWEGLIENAGSVFIGPWTPESVGDYASGTNHVLPTYGYARMYSGVSLDSFLKFMTVQSLTEEGLRNLGPYVATMAEIEGLDAHKRAVTLRLKDIEAKQLA
Protein: Dynein regulatory complex subunit 2 (Coiled-coil domain-containing protein 65) (Q6DHI2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes (By similarity). Plays a critical role in the assembly of N-DRC and also stabilizes the assembly of multiple inner dynein arms and radial spokes. Coassembles with DRC1 to form a central scaffold needed for assembly of the N-DRC and its attachment to the outer doublet microtubules.
Subcellular location: Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000250|UniProtKB:A8JB22}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A8JB22}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8JB22}.
Interaction partners:
- Dynein regulatory complex protein 1
- Dynein regulatory complex subunit 4
- Coiled-coil domain-containing protein 40
- Coiled-coil domain-containing protein 39
- Dynein, axonemal, intermediate chain 1, paralog 1.
- Dynein regulatory complex subunit 3.
- Radial spoke head protein 9 homolog
- Dynein axonemal assembly factor 19
- Armadillo repeat containing 4
- Radial spoke head component 4A.
Sequence:
MPKKAGKKAGGKLAGLTEEERLLYMQQKAQAEEEIAKRKEDMLTHFLKDKLQKEEKNTVLNLHKLRQQWRAVLTQTKIAELRNDMSVLSQTFERVLDYKDNIIRSLQVDLSERELQSELKRSSHLHNVDCLLEIHKSRLAQLEFNFKSSLVELSSEYNTEREQILSQHQQECVDLDNVMFSMEKHYSDLDGEAKRDYQSTRNQIKKRNFDDKQAVKEQMDGVVEKLWQDQQQVLNHYNESTRDKIITTDDLMNKDVQSAKEIDSLKKHIQKLQDSISTFRGQLSSGQTDKTAEQLRSERDELAQEVQHFRVQLNAAQAIRKKHITKLTVQSNDATKKLQEIVARGERLLRQCEMCCKLETEHEKVLPFYKSSLSEEEQKQEKAKAMESSNEKLTQLMHDYSPLAKFWQRYNKVELDCLCVKREKLLLLQENERLRLFLKQYLDEVSVSDESFRQQKLLVVSSPALQDTAATDRHQQKRHVVQEAACIVQKQL
Protein: Aggrecan core protein (Cartilage-specific proteoglycan core protein) (CSPCP) (Q61282)
Organism: Mus musculus (Mouse)
Function: This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. May play a regulatory role in the matrix assembly of the cartilage.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Hyaluronan and proteoglycan link protein 1
- Tenascin-R
- Brevican core protein
- Receptor-type tyrosine-protein phosphatase zeta
- Cartilage oligomeric matrix protein
- Fibronectin
- Fibulin-1
- Versican core protein
- Neurocan core protein
- Collagen alpha-1
Sequence:
MTTLLLVFVTLRVIAAVISEEVPDHDNSLSVSIPQPSPLKVLLGSSLTIPCYFIDPMHPVTTAPSTAPLTPRIKWSRVSKEKEVVLLVATEGQVRVNSIYQDKVSLPNYPAIPSDATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRTYGIRDTNETYDVYCFAEEMEGEVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYLHANQTGYPDPSSRYDAICYTGEDFVDIPENFFGVGGEDDITIQTVTWPDLELPLPRNVTEGEALGSVILTAKPIFDLSPTISEPGEALTLAPEVGSTAFPEAEERTGEATRPWGFPAEVTRGPDSATAFASEDLVVRVTISPGAAEVPGQPRLPGGVVFHYRPGSTRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKDSSPGVRTYGVRPSSETYDVYCYVDKLEGEVFFATRLEQFTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRTVYLYPNQTGLPDPLSKHHAFCFRGVSVAPSPGEEGGSTPTSPSDIEDWIVTQVGPGVDAVPLEPKTTEVPYFTTEPRKQTEWEPAYTPVGTSPQPGIPPTWLPTLPAAEEHTESPSASEEPSASAVPSTSEEPYTSSFAVPSMTELPGSGEASGAPDLSGDFTGSGDASGRLDSSGQPSGGIESGLPSGDLDSSGLSPTVSSGLPVESGSASGDGEVPWSHTPTVGRLPSGGESPEGSASASGTGDLSGLPSGGEITETSTSGAEETSGLPSGGDGLETSTSGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSETSTSGIEDISVLPTGGESLETSASGVGDLSGLPSGGESLETSASGAEDVTQLPTERGGLETSASGVEDITVLPTGRESLETSASGVEDVSGLPSGREGLETSASGIEDISVFPTEAEGLDTSASGGYVSGIPSGGDGTETSASGVEDVSGLPSGGEGLETSASGVEDLGPSTRDSLETSASGVDVTGFPSGRGDPETSVSGVGDDFSGLPSGKEGLETSASGAEDLSGLPSGKEDLVGSASGALDFGKLPPGTLGSGQTPEVNGFPSGFSGEYSGADIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATTSSELEGRGTIGISGSGEVSGLPLGELDSSADISGLPSGTELSGQASGSPDSSGETSGFFDVSGQPFGSSGVSEETSGIPEISGQPSGTPDTTATSGVTELNELSSGQPDVSGDGSGILFGSGQSSGITSVSGETSGISDLSGQPSGFPVFSGTATRTPDLASGTISGSGESSGITFVDTSFVEVTPTTFREEEGLGSVELSGFPSGETELSGTSGTVDVSEQSSGAIDSSGLTSPTPEFSGLPSGVAEVSGEFSGVETGSSLPSGAFDGSGLVSGFPTVSLVDRTLVESITQAPTAQEAGEGPSGILEFSGAHSGTPDISGELSGSLDLSTLQSGQMETSTETPSSPYFSGDFSSTTDVSGESIAATTGSGESSGLPEVTLNTSELVEGVTEPTVSQELGHGPSMTYTPRLFEASGDASASGDLGGAVTNFPGSGIEASVPEASSDLSAYPEAGVGVSAAPEASSKLSEFPDLHGITSAFHETDLEMTTPSTEVNSNPWTFQEGTREGSAAPEVSGESSTTSDIDTGTSGVPSATPMASGDRTEISGEWSDHTSEVNVAISSTITESEWAQPTRYPTETLQEIESPNPSYSGEETQTAETTMSLTDAPTLSSSEGSGETESTVADQEQCEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQDYQWIGLNDRTIEGDFRWSDGHSLQFEKWRPNQPDNFFATGEDCVVMIWHERGEWNDVPCNYQLPFTCKKGTVACGDPPVVEHARTLGQKKDRYEISSLVRYQCTEGFVQRHVPTIRCQPSGHWEEPRITCTDPNTYKHRLQKRSMRPTRRSRPSMAH
Protein: 60S ribosomal protein L35, putative (Q38FW8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S acidic ribosomal protein P0
- 40S ribosomal protein S14
- 40S ribosomal protein S23, putative
- 60S ribosomal protein L44
- 60S ribosomal protein L6, putative
- 40S ribosomal protein S17, putative
- 40S ribosomal protein S24
- 60S ribosomal protein L10, putative
- 60S ribosomal protein L37a, putative
- Eukaryotic translation initiation factor 5A
Sequence:
MSHIVKIRDLKEKGKDDLLKQLSEFKKELSQLRVSQQMNVGAARLGRIRTIRKGIARIMTVLNKNERENLRKFYSDKKLRSAKPKTLRAKLTHRRRLALKANEKNRKTRRQLRMAHKFPRRIYAVKV
Protein: Sideroflexin-4 (Q925N1)
Organism: Mus musculus (Mouse)
Function: Mitochondrial amino-acid transporter (By similarity). Does not act as a serine transporter: not able to mediate transport of serine into mitochondria (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6P4A7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEPNLQFWISERQAFFRRFCQWMDLLDPVNMFISIGSIEKSRQLLFTTEDAPKHYLDNQVIKDAWNKSLSTVHPDSSKLIPHLFRPAAFLPVTAPMVFLLMMPDTGIKSIILTQGCLYGYTTAFNITNGNASYSHGPVERTLLGAGVSVSSTFIGLIPHLFQMKYPPNNFWLKRTLPIVFLAQVSGMNVFASRSFENHRGIEVMDKEGHVVGHSRKAGRKAIKDTAKSRAVLFGTSALAPELFIHIFKRTRFYPQTLLSLVILRMSSTFFMMGLMVPVSFSMFPQIGQIQCSQLEEKIQSSTEEKELFYYRGV
Protein: KiSS-1 metastasis suppressor (Kisspeptin) (Metastasis-suppressor KiSS-1 precursor) (A8C5J1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Kisspeptin
- KISS1 receptor b
- KISS1 receptor a
- Progonadoliberin
- Progonadoliberin
- Preprotachykinin 2a
- Lhb protein
- Follicle-stimulating hormone beta subunit
- FMRFamide related peptide 1
- Substance-K receptor
Sequence:
MMLLTVILMLSVARVHTNPSGHFQYYLEDETPEETSLRVLRGTDTRPTDGSPPSKLSALFSMGAGPQKNTWWWSPESPYTKRRQNVAYYNLNSFGLRYGKREQDMLTRLKQKSPVK
Protein: Zinc finger protein 554 (K7EQV8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVTCAHLGRRARLPAAQPSACPGTCFSQEERMAAGYLPRWSQELVTFEDVSMDFSQEEWELLEPAQKNLYREVMLENYRNVVSLEALKNQCTDVGIKEGPLSPAQTSQVTSLSSWTGYLLFQPVASSHLEQREALWIEEKGTPQASCSVSLLLPRLQCSGVISAHCNLHLPGSSDSSASAS
Protein: SD07741p (Q960C4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYNGIGLTTPRGSGTNGHVQRNWACVRPGKKDKDYRAEDDTKKLDAQLNRPPNKEILDHDRKRKIEVKCLELEDILEKQGRTPEEIKSQVDSFRQKLMGQGKTDLAKDEFGRVAARDTHQIAEAQQQKNARLREAFNISEYFVEGSSFDGDRKAKEDLAKSVALQKELDAQRESLAAAAAAAAAGKDKETGKRYALVRTPSRERDRDAGDAAANGDERDHVSKTDKKKRKKRARESSASPERKKKKKSKKHKKESKSKKKKSRKRKHSESGRDSDRDSDEEDDSSEEERRESKNVRKKAKKDKKKRDKKLKKKSRARASSSDSERTNSPSRKENKSDRSRGANASKSDEKAPQQENVMRSRSRERKDTRSSRPLEASIDSRQRKPRERSAATPPRKEPERHRERSKDRQRSKEKHRSRDRLRSRERQRSRERQRSRERQRSKERQRSKERQRSIERQRSKERQRSKERQRSRSKDALRCKEKPQSNEKERSRERRRSKSKDRQRSKEKHRPKDEKQTLDKRRDRSTDRSKENQRSNERQRSKERQRSKERERSKDRQRSRERRRSKERQLSKDRQGLKERQRSNERKRSKERQPSKEKQRSRERQRSREPLQSKDRQRSKERQRSRERPAKEARPTRSPRERSSKSRDDRRHRSPTNASRKQKDDTKLSRNARFKSPAHSPEAPPKKSVPTPAFNPFKAAEDTVNDILGTKSVMVALEQTKRQRAASSSSSDSDSSGSSSTSSRTPSPKPTPRKQKKRSKTPELKEVKKEISPRKESRVSVKREQSNSPQKSKSKSKVDESSPKRTSRRSRSISSELRYSPAERHPERYHDIVQDKKRPSKVREAHSTKPAPVVRLRAQSDDGSDAETGVDGAALEEFQQSRREREEQQELRMLEQLKSGIAAKAKQKIKIMEKDPAKEGSEPLVAALADSSLVDAIVSKVSTATVAAAESAARRSRSRERRSRSKRRTSTSHHRHDSSSESRSRYSSSSSRSGSHSSRSGSHSSRTSCSTNSSSGSSSSGSGSGSSQSGSRSPSIPRRRGSPSFLDRRRITSRRSPRSTRR
Protein: Uncharacterized protein Rv3660c (P9WKX7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May play a role in septum formation.
Interaction partners:
- Possible conserved alanine rich membrane protein
- Putative conjugal transfer protein Rv3659c
- DUF4244 domain-containing protein
- Probable conserved transmembrane protein
- Apoptosis inhibitor Rv3654c
- Uncharacterized protein Rv1708
- SAF domain-containing protein
Sequence:
MLTDPGLRDELDRVAAAVGVRVVHLGGRHPVSRKTWSAAAAVVLDHAAADRCGRLALPRRTHVSVLTGTEAATATWAAAITVGAQHVLRMPEQEGELVRELAEAAESARDDGICGAVVAVIGGRGGAGASLFAVALAQAAADALLVDLDPWAGGIDLLVGGETAPGLRWPDLALQGGRLNWSAVRAALPRPRGISVLSGTRRGYELDAGPVDAVIDAGRRGGVTVVCDLPRRLTDATQAALDAADLVVLVSPCDVRACAAAATMAPVLTAINPNLGLVVRGPSPGGLRAAEVADVAGVPLLASMRAQPRLAEQLEHGGLRLRRRSVLASAARRVLGVLPRAGSGRHGRAA
Protein: S-phase cyclin A associated protein in the ER (H3BPM0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMASFQRSNSHDKVRRIVAEEGRTARNLIAWSVPLESKDDDGKPKCQTGGKSKRTIQGTHKTTKQSTAVDCKITSSTTGDKHFDKSPTKTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDNYVRDFKALIDWIQLQEKLEKTDAQSRPTSLAWEVKKMSPGRHVIPSPSTDRINVTSNARRSLNFGGSTGTVPAPRLAPTGVSWADKVKAHHTGSTASSEITPAQSCPPMTVQKASRKNERKDAEGWETVQRGRPIRSRSTAVMPKVSLATEATRSKDDSDKENVCLLPDESIQKGQFVGDGTSNTIESHPKDSLHSCDHPLAEKTQFTVSTLDDVKNSGSIRDNYVRTSEISAVHIDTECVSVMLQAGTPPLQVNEEKFPAEKARIENEMDPSDISNVSAANLSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGSGSVSFCGMSMDWNDVLADYEARESWRQNTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE
Protein: Enhancer of acetyltransferase chameau (RE10167p) (Q9VUK1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQSIAFALLIFAGILAYGNAAPQMNLGWLQAVLAEAGQRNTTVKFGNNTVIITGVSNSVANSNQGNTTPSSPRNQWNNNWYPYYNNGYYRIMPTINGQIVEGPQSSAEESHEISQEFSHEISQSDEESGEDQYHQEDQTEEDEDDNETDLSEDQLDDLEEDQLDKEKELEDGHDQSEEDNENEDELIDPEEDAIDQVLDDIEKEIAARENE
Protein: Core gene UL38 family protein (ORF 62) (ORF62) (Q76RF6)
Organism: Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Interaction partners:
Sequence:
MKVQAENAARLGRQVLGLLPPPTHRVSLTRGPEFARGVRDLLSKYAASTRPTVGSLHEALRQAPFRQPTYGDFLVYSQTFSPQEPLGTFLFSFKQEDNGSSMDMLLTPTSLFMLSGMEAAKAPQTHKVAGVWYGSGSGLADFIPNLSELMDTGEFHTLLTPVGPMVQSVHSTFVTKVTSAMKGVGLARDEPRAHVGLTLPCDMLVDLDESCPMVQRREPAGLNVTIYASLVYLRVNQRPSMALTFFQSGKGFAEVVAMIKDHFTDVIRTKYIQLRHELYINRLVFGAVCTLGTVPFDSHPVHQSLNVKGTSLPVLVFANFEAACGPWTVFL
Protein: Keratin-associated protein 24-1 (Q3LI83)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 8-1
- Keratin-associated protein 27-1
- Keratin-associated protein 20-1
- Keratin-associated protein 15-1
- Keratin-associated protein 25-1
- Keratin-associated protein 13-3
- Keratin-associated protein 11-1
- Keratin-associated protein 7-1
- Keratin-associated protein 22-1
- Keratin-associated protein 20-2
Sequence:
MPAGSMSTTGYPGVCSTTSYRTHCYIPVTSSVTLSSSDLSPTFGHCLPSSYQGNLWLLDYCQESYGEAPTCKSPSCEPKTCSTTGCDPSNSSVPCNSPSAGQVFSVCETTNVSPSPSCSPSTQTNGYVCNCHIPTRNASKACQTLRNGSNCFGQLNCLSKSFQTLNHCRLSTLGYKSYQNPCFIPSYVSPLCYISNSCQPQSYLVRNYHYSSYRPTSCRPLSYLSRSFRSLSYIPSTFPPLRYLCSGSRPLKCY
Protein: Branched-chain-amino-acid aminotransferase (BCAT) (EC 2.6.1.42) (Transaminase B) (P0AB80)
Organism: Escherichia coli (strain K12)
Function: Acts on leucine, isoleucine and valine.
Interaction partners:
- Dihydroxy-acid dehydratase
- 2-isopropylmalate synthase
- L-threonine dehydratase biosynthetic IlvA
- Acetolactate synthase isozyme 2 small subunit
- Valine--pyruvate aminotransferase
- L-threonine dehydratase catabolic TdcB
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Ketol-acid reductoisomerase
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- Cystathionine gamma-synthase
Sequence:
MTTKKADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYDSHKGPVVFRHREHMQRLHDSAKIYRFPVSQSIDELMEACRDVIRKNNLTSAYIRPLIFVGDVGMGVNPPAGYSTDVIIAAFPWGAYLGAEALEQGIDAMVSSWNRAAPNTIPTAAKAGGNYLSSLLVGSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTPPFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLADEVFMSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFGLFTGETEDKWGWLDQVNQ
Protein: Elongation factor 1-alpha (EF-1-alpha) (50 kDa actin-binding protein) (ABP-50) (P0CT32)
Organism: Dictyostelium discoideum (Social amoeba)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. It is also an abundant actin filament bundling protein.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase domain-containing protein
- Elongation factor 1-beta
- Small ribosomal subunit protein eS30
- Eukaryotic peptide chain release factor subunit 1
- Sulfate adenylyltransferase
- Heat shock factor-type DNA-binding domain-containing protein
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS10
Sequence:
MGKEKTHINIVVIGHVDAGKSTTTGHLIYKCGGIDKRVIEKYEKEASEMGKQSFKYAWVMDKLKAERERGITIDIALWKFETSKYYFTIIDAPGHRDFIKNMITGTSQADCAVLVIASPTGEFEAGIAKNGQTREHALLAYTLGVKQMIVAINKMDEKSTNYSQARYDEIVKEVSSFIKKIGYNPEKVAFVPISGWNGDNMLERSDKMEWYKGPTLLEALDAIVEPKRPHDKPLRIPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPAGLSTEVKSVEMHHEQLPEARPGDNVGFNVKNVSVKEIKRGMVAGDSKNDPPQETEKFVAQVIVLNHPGQIHAGYSPVLDCHTAHIACKFTEIVDKVDRRTGAVVAKEGTAAVVLKNGDAAMVELTPSRPMCVESFTEYPPLGRFAVRDMRQTVAVGVIKSTVKKAPGKAGDKKGAAAPSKKK
Protein: CTO1 family protein C17G9.12c (Q9UUE0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C17G9.13c
Sequence:
MLYIVDFDETITTYDTIHLLAEAVNKPEEWSVISDKYWQEYLAWREALPHSTTLTSYLPLLGGSRYLEEASIKRIEKSQYFSGLSEGALDNIVQLITLRAGFVEFINALVPDLRVSKTIFHVLSVNWSARVIEQTLLHHTDLTADLLCVHANDFDFDTSTNTTNGRILARNASSLLMNSTDKVREFRRIVQTDAVSSPLNVVYIGDSPTDFGCLQISPISILMRSNQKYYDILSRFEDVQLVDISEFPVQKAVPGKKIIYTCSDWCAIQKAFLA
Protein: Myosin X (E9PEW5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLRESLEQKLEKRREEEVSHAAMVIRAHVLGFLARKQYRKVLYCVVIIQKNYRAFLLRRRFLHLKKAAIVFQKQLRGQIARRVYRQLLAEKREQEEKKKQEEEEKKKREEEERERERERREAELRAQQEEETRKQQELEALQKSQKEAELTRELEKQKENKQVEEILRLEKEIEDLQRMKEQQELSLTEASLQKLQERRDQELRRLEEEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEFSSELAESACEEKPNFNFSQPYPEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNDTVVPTSPSADSTVLLAPSVQDSGSLHNSSSGESTYCMPQNAGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRCSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRTAKEIIDNTTKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHASTDQEIQEMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGSEMEKYALFTYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTVVADVLAKFEKLAATSEVGDLPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHHPAPEENLQVLAALRLQYLQGDYTLHAAIPPLEEVYSLQRLKARISQSTKTFTPCERLEKRRTSFLEGTLRRSFRTGSVVRQKVEEEQMLDMWIKEEVSSARASIIDKWRKFQGMNQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSASSQGSSR
Protein: Erythrocyte membrane protein band 4.1 like 2 (E9PIG0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTEVGSVSEVKKDSSQLGTDATKEKPKEVAENQQNQSSDPEEEKGSQPPPAAESQSSLRRQKREKETSESRGISRFIPPWLKKQKSYTLVVAKDGGDKKEPTQAVVEEQVLDKEEPLPEEQRQAKGDAEEMAQKKQEIKVEVKEEKPSVSKEEKPSVSKVE
Protein: O-acetyl-ADP-ribose deacetylase (EC 3.1.1.106) (Regulator of RNase III activity) (P0A8D6)
Organism: Escherichia coli (strain K12)
Function: Deacetylates O-acetyl-ADP ribose to yield ADP-ribose and free acetate. Down-regulates ribonuclease 3 (RNase III) activity. Acts by interacting directly with the region of the ribonuclease that is required for dimerization/activation. Overexpression inhibits biofilm formation via an RNase III-independent pathway. This inhibition is RpoS-dependent. Overexpression also results in increased susceptibility to apramycin.
Interaction partners:
- Cardiolipin synthase C
- Replication-associated recombination protein A
- Uncharacterized protein YmdA
Sequence:
MKTRIHVVQGDITKLAVDVIVNAANPSLMGGGGVDGAIHRAAGPALLDACLKVRQQQGDCPTGHAVITLAGDLPAKAVVHTVGPVWRGGEQNEDQLLQDAYLNSLRLVAANSYTSVAFPAISTGVYGYPRAAAAEIAVKTVSEFITRHALPEQVYFVCYDEENAHLYERLLTQQGDE
Protein: UDP-N-acetylglucosamine transferase subunit ALG14 (Asparagine-linked glycosylation 14 homolog) (Q96F25)
Organism: Homo sapiens (Human)
Function: Involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16100110}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-N-acetylglucosamine transferase subunit ALG13
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- GDP-Man:Man
- Dol-P-Man:Man
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dol-P-Man:Man
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Glutamine--fructose-6-phosphate aminotransferase 1
Sequence:
MVCVLVLAAAAGAVAVFLILRIWVVLRSMDVTPRESLSILVVAGSGGHTTEILRLLGSLSNAYSPRHYVIADTDEMSANKINSFELDRADRDPSNMYTKYYIHRIPRSREVQQSWPSTVFTTLHSMWLSFPLIHRVKPDLVLCNGPGTCVPICVSALLLGILGIKKVIIVYVESICRVETLSMSGKILFHLSDYFIVQWPALKEKYPKSVYLGRIV