wanglab/gogpt-training-data huggingface dataset:
Protein: PAB1-binding protein 1 (Poly(A)-binding protein-binding protein) (P53297)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-mRNA polyadenylation. May act to repress the ability of PAB1 to negatively regulate polyadenylation. Negative regulator of poly(A) nuclease (PAN) activity. Promotes mating-type switching in mother cells by positively regulating HO mRNA translation. Localizes MKT1 to polysomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15082763}. Nucleus {ECO:0000269|PubMed:14562095}. Mitochondrion {ECO:0000269|PubMed:14576278}. Note=Localizes to polysomes. {ECO:0000269|PubMed:15082763}.
Interaction partners:
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Protein LSM12
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein-associated protein B
- Protein NAM8
- Protein PBP4
- ATP-dependent RNA helicase DHH1
- Post-transcriptional regulator MKT1
- Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1
- Negative growth regulatory protein NGR1
Sequence:
MKGNFRKRDSSTNSRKGGNSDSNYTNGGVPNQNNSSMFYENPEITRNFDDRQDYLLANSIGSDVTVTVTSGVKYTGLLVSCNLESTNGIDVVLRFPRVADSGVSDSVDDLAKTLGETLLIHGEDVAELELKNIDLSLDEKWENSKAQETTPARTNIEKERVNGESNEVTKFRTDVDISGSGREIKERKLEKWTPEEGAEHFDINKGKALEDDSASWDQFAVNEKKFGVKSTFDEHLYTTKINKDDPNYSKRLQEAERIAKEIESQGTSGNIHIAEDRGIIIDDSGLDEEDLYSGVDRRGDELLAALKSNSKPNSNKGNRYVPPTLRQQPHHMDPAIISSSNSNKNENAVSTDTSTPAAAGAPEGKPPQKTSKNKKSLSSKEAQIEELKKFSEKFKVPYDIPKDMLEVLKRSSSTLKSNSSLPPKPISKTPSAKTVSPTTQISAGKSESRRSGSNISQGQSSTGHTTRSSTSLRRRNHGSFFGAKNPHTNDAKRVLFGKSFNMFIKSKEAHDEKKKGDDASENMEPFFIEKPYFTAPTWLNTIEESYKTFFPDEDTAIQEAQTRFQQRQLNSMGNAVPGMNPAMGMNMGGMMGFPMGGPSASPNPMMNGFAAGSMGMYMPFQPQPMFYHPSMPQMMPVMGSNGAEEGGGNISPHVPAGFMAAGPGAPMGAFGYPGGIPFQGMMGSGPSGMPANGSAMHSHGHSRNYHQTSHHGHHNSSTSGHK
Protein: Protein PXR1 (G-patch nucleolar protein) (PinX1-related protein 1) (P53335)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in rRNA-processing at A0, A1 and A2 sites through its action in U18 and U24 snoRNA 3'-end final trimming. Negative regulator of telomerase through competition for binding to EST2 with TLC1.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12107183, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43
- U3 small nucleolar RNA-associated protein 7
- Protein SQS1
- rRNA 2'-O-methyltransferase fibrillarin
- Essential nuclear protein 1
- 13 kDa ribonucleoprotein-associated protein
- ATP-dependent RNA helicase FAL1
- Probable ATP-dependent RNA helicase DHR2
- Nuclear localization sequence-binding protein
- Suppressor of glycerol defect protein 1
Sequence:
MGLAATRTKQRFGLDPRNTAWSNDTSRFGHQFLEKFGWKPGMGLGLSPMNSNTSHIKVSIKDDNVGLGAKLKRKDKKDEFDNGECAGLDVFQRILGRLNGKESKISEELDTQRKQKIIDGKWGIHFVKGEVLASTWDPKTHKLRNYSNAKKRKREGDDSEDEDDDDKEDKDSDKKKHKKHKKHKKDKKKDKKDKKEHKKHKKEEKRLKKEKRAEKTKETKKTSKLKSSESASNIPDAVNTRLSVRSKWIKQKRAALMDSKALNEIFMITND
Protein: M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B) (P48966)
Organism: Rattus norvegicus (Rat)
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 (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P30305}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P30305}.
Interaction partners:
- Cyclin-dependent kinase 1
- 14-3-3 protein beta/alpha
- 14-3-3 protein epsilon
- Serine/threonine-protein kinase PLK1
- CHK2 checkpoint homolog
- 14-3-3 protein zeta/delta
- G2/mitotic-specific cyclin-B1
- 14-3-3 protein theta
- 14-3-3 protein gamma
- Cyclin-A2
Sequence:
MEVPPQKSAPGSALSTARVLGGIQRPRHLSGFGFGSDGLLGSPERAASSSPVTTLTQTMYNLAGLGSETPKTQVGSLSFQNRLTDLSLSRRTSECSLSSESSESSDAGLCMDSPSPMDPQTAERTFEQAIQAASRVIQKMQFTIKASVFASEAAGHSPVLQNITNSQALDSWEKDEAGYRAASSPGEDKENDGYIFKMPQKLPHSSSARALAEWASRREAFTQRPSSAPDLMCLTTDGKMDVEEASPVAQSSSLTPVERACEEDDGFVDILESDLKDDDMVPAGMENLISAPLVKKLDKEEEQDLIMFSKCQRLFRSPSMPCSVIRPILKRLERPHDRDVPVLSKRRKSGTPLEEQQLEEPKARVFRSKSLCHEIESILDSDHRGLIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVEKFVIVDCRYPYEYEGGHIKNAVNLPLEPDAETFLLKHPITPCNLDKRIILIFHCEFSSERGPRMCRFIRERDRAANDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHAAFRDELRNFRLKTRSWAGERSTTQLCSRLQDQ
Protein: Uncharacterized protein (Q387N4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- 30S ribosomal protein S8, putative
- Uncharacterized protein
- tRNA pseudouridine synthase A-like protein
- Kinteoplast poly
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Small ribosomal subunit protein mS41
- Uncharacterized protein
Sequence:
MRWTAVLCKVSKVPTRSVIPADALRYHPRYSVPRKMVLSNTFNVVGENNRYTSLKLILEKLSGHVGRRQYKMLCNLEKHYDKLKDEGIDWHELKWLSREELIVLFDKVLHLTRTERAALLPAIEAKVCGVLRQTDSRHSTVVCMNRGNANHGWRCGRNGHTNDVYFEGKAKANTAALQLCRRSSVRSVERSGVLVEVRSEPDFSVVGRFDHSLSPRVWSTPENPTFQVTTIGYEFRVHREDPRVIPQIVEAAEEWELHANITKQVIWEMLEMYAVERDRQPLDLKPGEMGDPDIPSRHATAFNVQVVPPSSAGDEAIQVVEQRIVRADGSEVPWFQEPPPQLFSGGIPVILPFAPSIIVKSTFRQVTRSSAQDVTRQLLQPVVDVTCFLHPNVCFWWNAEDEQRCLGHIVDYAKRIPFALPFNLYFRVNLSKDLRGVQNYTEELGKRMSMKAHYFNLRSYGVR
Protein: F-BAR domain only protein 2 (Q3UQN2)
Organism: Mus musculus (Mouse)
Function: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor.
Subcellular location: Membrane, clathrin-coated pit {ECO:0000305|PubMed:20448150, ECO:0000305|PubMed:21762413}; Peripheral membrane protein {ECO:0000305|PubMed:20448150, ECO:0000305|PubMed:21762413}; Cytoplasmic side {ECO:0000305|PubMed:20448150, ECO:0000305|PubMed:21762413}. Note=Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2.
Interaction partners:
- Intersectin-2
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- Intersectin-1
- Epidermal growth factor receptor substrate 15
- AP-2 complex subunit beta
- AP-2 complex subunit alpha-2
- Disabled homolog 2
- Amphiphysin
- Formin-binding protein 1
Sequence:
MVMAHFVENFWGEKNNGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPMWDVFKTSTEKLANCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQAIQNITQALQKSKENYTAKCVEQERLKKEGATQREIEKAAVKSKKATDTYKLYVEKYALTKADFEQKMTETAQKFQDIEETHLIHIKEIIGSLSNAVKEIHLQIGQVHEEFINNMANTTIESLIQKFAESKGTGKERPGLIEFEECDPASAVEGIKPRKRKTFALPGIIKKEKDAESVECPDADSLNIPDVDEEGFSIKPEANQNDTKENHFYSSSDSDSEDEEPKRYRIEIKPAHPNNLHHTMASLDELKVSIGNITLSPAVSRHSPVQMNRNSSNEELTKSKPSSLPTEKGTNDLLAWDPLFGSSLESSSAPLTSSSSARPTTPLSLGTLVPPPRPASRPKLASGKLSGINEIPRPFSPPVTSNTSPPPTAPLARAESSSSISSSASLSAANTPTVGVSRGPSPVSLGNQDTLPVAIALTESVNAYFKGADPTKCIVKITGDVTISFPSGIIKVFTSNPSPAVLCFRVKNISRLEQILPNSQLVFSDPSQCDSNTKDFWMNMQAVTIYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVLSNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSGISEKSDSGGSGSLRAKFDLSEGPSKPTTLAVQFLSEGNTLSGVDIELVGTGYRLSLVKKRFATGRYLADC
Protein: RHOMBOID-like protein 15 (F4J5V3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTYGISSSQKIIQSLRSREESFTVGEKRELFAGVQTRVGQWWNAIPFLTSSVVVVCGVIYLICLLTGYDTFYEVCFLPSAIISRFQVYRFYTAIIFHGSLLHVLFNMMALVPMGSELERIMGSVRLLYLTVLLATTNAVLHLLIASLAGYNPFYQYDHLMNECAIGFSGILFSMIVIETSLSGVTSRSVFGLFNVPAKLYPWILLIVFQLLMTNVSLLGHLCGILSGFSYSYGLFNFLMPGSSFFTTIESASWMSSFIRRPKFIMCTGGNPSSYIPTYSAQNTTSSGFSTGNAWRSLSSWLPQREASNQSSEDSRFPGRGRTLSTARDPTAPAGETDPNLHARLLEDSSSPDRLSDATVNTVADSRQAPIANAAVLPQSQGRVAASEEQIQKLVAMGFDRTQVEVALAAADDDLTVAVEILMSQQA
Protein: Nucleoprotein (NP) (Nucleocapsid protein) (Protein N) (P03521)
Organism: Vesicular stomatitis Indiana virus (strain San Juan) (VSIV)
Function: Encapsidates the genome in a ratio of one N per nine ribonucleotides, protecting it from nucleases. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Nucleocapsid assembly is concommitant with replication, therefore viral replication depends on the intracellular concentration of free N, termed N(0). All replicative products are resistant to nucleases.
Subcellular location: Virion {ECO:0000269|PubMed:1850035, ECO:0000269|PubMed:20133572, ECO:0000269|PubMed:21177817, ECO:0000269|PubMed:35476516, ECO:0000269|PubMed:35970826, ECO:0000269|PubMed:36216930}. Host cytoplasm. Note=The nucleocapsid is synthesized in the cytoplasm, and is subsequently transported via microtubules to the cell periphery. About 1240 copies of N are present in the virion (PubMed:35476516). {ECO:0000269|PubMed:35476516}.
Interaction partners:
Sequence:
MSVTVKRIIDNTVIVPKLPANEDPVEYPADYFRKSKEIPLYINTTKSLSDLRGYVYQGLKSGNVSIIHVNSYLYGALKDIRGKLDKDWSSFGINIGKAGDTIGIFDLVSLKALDGVLPDGVSDASRTSADDKWLPLYLLGLYRVGRTQMPEYRKKLMDGLTNQCKMINEQFEPLVPEGRDIFDVWGNDSNYTKIVAAVDMFFHMFKKHECASFRYGTIVSRFKDCAALATFGHLCKITGMSTEDVTTWILNREVADEMVQMMLPGQEIDKADSYMPYLIDFGLSSKSPYSSVKNPAFHFWGQLTALLLRSTRARNARQPDDIEYTSLTTAGLLYAYAVGSSADLAQQFCVGDNKYTPDDSTGGLTTNAPPQGRDVVEWLGWFEDQNRKPTPDMMQYAKRAVMSLQGLREKTIGKYAKSEFDK
Protein: Zinc finger C3HC-type protein 1 (Nuclear-interacting partner of ALK) (mNIPA) (Nuclear-interacting partner of anaplastic lymphoma kinase) (Q80YV2)
Organism: Mus musculus (Mouse)
Function: Essential component of a SCF-type E3 ligase complex, SCF(NIPA), a complex that controls mitotic entry by mediating ubiquitination and subsequent degradation of cyclin B1 (CCNB1). Its cell-cycle-dependent phosphorylation regulates the assembly of the SCF(NIPA) complex, restricting CCNB1 ubiquitination activity to interphase. Its inactivation results in nuclear accumulation of CCNB1 in interphase and premature mitotic entry (By similarity). Overexpression may be able to protect from apoptosis induced by IL-3 withdrawal.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q86WB0}. Nucleus envelope {ECO:0000250|UniProtKB:Q86WB0}. Note=Resident of the nuclear basket (NB). Occurs at the nuclear envelopes (NE) of all TPR-containing cell types, including proliferating and non-dividing, terminally differentiated cells of different morphogenetic origin. {ECO:0000250|UniProtKB:Q86WB0}.
Interaction partners:
- GPN-loop GTPase 1
Sequence:
MAATSEGPLFAASIEKTWGSVVRSPEGTPQKVRELIDEGIVPEEGGTEPKDTAATFQSVDGSPQAEQSPLESTSKEAFFHRVETFSSLKWAGKPPELSPLICAKYGWVTVECDMLKCSSCQAFLCASLQPTFDFGRYKERCAELKKSLCSAHEKFCFWPDSPSPDRFGMLPLGEPAVLISEFLDRFQSLCHLDLQLPSLRPEDLKTMCLTEDAVSALLHLLEDELDFHADDRKTTSKLGSDVQVQATACVLSLCGWACSSLEPTQLSLITCYQCMRKVGLWGFQQIESSMTDLEASFGLTSSPIPGVEGRPEHFPLVPESPRRMMTRSQDATVSPGSEQSEKSPGPIVSRTRSWESSSPVDRPELEAASPTTRSRPVTRSMGTGDSAGVEVPSSPLRRTKRARLCSSSSSDTSPRSFFDPTSQHRDWCPWVNITLVKETKENGETEVDACTPAEPGWKAVLTILLAHKRSNQPAETDSMSLSEKSRKVFRIFRQWESSSSS
Protein: Uncharacterized protein (Q9VEL5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Odorant binding protein b
- Aquarius
- IP02289p
- AT20289p
- Uncharacterized protein
- Accessory gland protein Acp29AB
- Uncharacterized protein, isoform A
- Lectin-29Ca
Sequence:
MEGNRSLVVLGLILILIQLTTPTSTPAPTPQPAGAEEAPGNSTAEASKSSTASKCKSTEILSENGCVDRENFLNKIVMRSWRDEGFEKAKARAGLVDGVECRDGELRTAFGCSKPLYPPHVDVNRVPVHHSRLNGERIVHDKGIYKLYHHVEDVEQKPIRKPRVVGPPITGNKRPRKYVFLPGRSIGKGHTCRANEVLGRRNRCIHRKRLAGQRQNQTIENEQSQ
Protein: Vacuolar protein sorting-associated protein 8 homolog (Vacuolar protein sorting 8) (Q9VRX2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes probably as part of the class C core vacuole/endosome tethering (CORVET) complex. Specifically required for endocytic trafficking in a subset of cells, such as hemocytes and nephrocytes, which are highly active in endocytosis.
Subcellular location: Early endosome {ECO:0000269|PubMed:27253064}. Note=Localization to the early endosome is dependent on Rab5 and class C core vacuole/endosome tethering (CORVET) complex subunits dor/Vps18, car/Vps33A and Vps16A. {ECO:0000269|PubMed:27253064}.
Interaction partners:
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 39 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting 33B
- Vacuolar protein sorting-associated protein 33A
- Vacuolar protein sorting-associated protein 41 homolog
- Ras-related protein Rab5
- Vacuolar protein sorting-associated protein 16B
- Vacuolar protein sorting-associated protein 45
Sequence:
MSELKAPSLQSLLESERGSTDSLLAESLQLDFEDLDDAEFAIPPTDVLPTLEAVLSEFEADSDVASEFGMPVPHATPTPSIGEDSTIRTDGRGGGGSIMRYTLLHGISAQLSSAAERVNAGAASSCAVAAFIAIGTSHGHILNFDVTQTLRWAHQDKHGQGAVASLAFNADSTRLLAGFSRGLVAMLDTHTGDVLRELFDVITPNTGVLHVKWTSRSSLALCADAGGSVWSLSFTRKLGIRGCQSRCLFSGARGEVCAVEPLIMDSQGRHELDQYCIVALATLSKYFIVTVRPRLRVIKYHVLQGPPDCLPLLAWHLVLIQAADTSRSVDPVIVVGRGNQLFFHQLFVSNGRITLLYLRHVQLQGSLLSAHWLGPKCVASLDTAEILHLVDVRSSKELECMDMANAGLVYGSAQFKGLATGGNVSPAFALAGSNACYNSVVSRGTQLYVLGARSLHIIGVRTWSERISFLVKHHRWQEACQLALDGYIASVDRPRKRAQAKERIIMLFKEYIANSARAPEYCLGAIVNCLITVGELDLLWTQLWEKLHNSSTELFLQHISEHIEKETIHSVNPVISQALVDYWLEHSPAKLEQLILKLDWMCLDLNQVLKAVKKHRLFRAQIYLNTQALNDYTAALTELLPLVTPDETDLGNCLLVYVSSCLAGREYPSGEIPVELVHQVKHDVLRCLTSQHSKENAGDELPYPYLRALLKFDTRETLNVISLAFQEREFSNELGISHRKRIINLLLEIMSPENATWAEIGCLLNFIAQQISMQCLPRDRQLLERVLSHLAQEEIANESSRQHSERENAWHELLSSNCLAEISSDEEQLRLAEKAKCYCVVEYLLEKLERYDTILDSYIRNEARHETMFAYMERHVASPKRSIFRQLKRNLRELLTINAKETTRLLSLHYPEKINELLDNLRREENLLYLFLKCLNDRKSELEASQMELLLELYCKMESSSTVEEFLRSNSGYRLENAIAIAESHHLNRSVIYLYEKQESYAKAFELSMELLKSAAGEEAAKEAQTISALLARSVETLPAQELERCWFALLQYILPHQELQSITKSLLHEASQHIDLHNLVQLIMNTHNVSTSFGDIKDLLMGMLDSSRHKTEALRASAGALCQDLHLKFVKRYQHAHRGLWVTTTKCSMCRQRLYDHSQVLIFGGCGHGIHEQCMEESETQFEECPRCFTAIPDQSIGLPRPNKNLISISSSLEMGALQLKAPPRRFI
Protein: GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (EC 2.4.1.131) (Alpha-1,2-mannosyltransferase alg11) (Asparagine-linked glycosylation protein 11) (Galactomannan deficiency protein 3) (Glycolipid 2-alpha-mannosyltransferase) (O74878)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:11015724}; Single-pass membrane protein {ECO:0000250|UniProtKB:P53954}.
Interaction partners:
- Dol-P-Man:Man
- UDP-N-acetylglucosamine transferase subunit alg13
- UDP-N-acetylglucosamine transferase subunit alg14
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Alpha-1,3/1,6-mannosyltransferase alg2
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Probable Dol-P-Man:Man
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3
Sequence:
MITTLAIALFIAVVAIHSHIRRKICKEIGIRLIKKIAPVKASLYKQVGVEPKLARTVGFFHPYCNAGGGGERVLWTAVKSVQTEFPNVISVVYTGDNVSKAEILRRVKNTFEIDLDSSKIVFVYLKLRFLVSATTWHRFTLLGQSLGSMILGFEAIYRFAPDIFIDTMGYAFTFCVVKSFQNIPVGAYVHYPTISTDMLKSLKQVSLLAKVKMAYWRWFAQLYSDAGSHADYVMTNSSWTRNHIASLWGKDIQLSVVFPPCNTSELEKIDINRKREPTLLYLAQYRPEKNHENVLRSFALYFEQHPDSPAKLLLVGSVRGEEDMCFVNHLKTLATELNLQSKVKFVVDAPWPKVVEYLGTCSIGVNYMWNEHFGIGVVEYMAAGLIPVVNNSGGPKFDIVIPWIGKPTGFHASTISEYAEAYHKALTLSPQEQLEMRINARSACARFGEHVFMRDFGNVFAKLLREDYSRT
Protein: BM-40 (MIP10412p1) (Secreted protein, acidic, cysteine-rich, isoform A) (Secreted protein, acidic, cysteine-rich, isoform B) (O97365)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Viking, isoform A
- Collagen alpha-1
- Glutactin
- Nidogen
Sequence:
MRSLWLLLGLGLLAVSHVQASTEFSEDLLDEDLDLSDIDENEEEFLRLLEEKNKIKDIERENEIATKLAEVQHNLLNPVVEVDLCETMSCGAGRICQMHDEKPKCVCIPECPEEVDTRRLVCTNTNETWPSDCSVYQQRCWCDSGEPGCTNPDNAHMHIDYYGACHEPRSCEGEDLKDFPRRMRDWLFNVMRDLAERDELTEHYMQMELEAETNNSRRWSNAAVWKWCDLDGDTDRSVSRHELFPIRAPLVSLEHCIAPFLESCDSNKDHRITLVEWGACLELDPEDLKERCDDVQRAQPHLLG
Protein: SH3 domain-containing protein (Q54IA6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- SH3 domain-containing protein
- Clathrin heavy chain
Sequence:
MSKEKTSWGSIKTNFARTKHKVLASFGAAETTVDSKIVAEKEKLFTLFKLMKRLNKNVDKYEATLKEINILQNEISHDLLALNENDPAIKAYQEVSTSLEQERIRIEEILENYYHDPLRVYLSQFRDIRSRLEELDLRRLDMDRYYRDYNIKANKGKDASSLQKTENKHTKTKEAYQELSDEIMKDMYALFDDRKLAFDPSFACFINRNNEYFARAAAEYQGALASVQHINEFEATTHPQAITPVESSSMSRNVRSSSVFTSPKEFSSNGSTPTQRPRASTIATPSPSSSSSYDSSPYSTTTTTTTTTNNSVNLSKPSYGVPSPQQQHYPPQQYQSSPQQQDEVPYSSPHVQPQPSINLHKPTVNTSPVNGGSGRPLPTPATNSGVILNKPRSTTMASGRPLPTPAPAPTTKRVQALYDFQGQDSTELSFKKGDMITVFKQNGEWYDAELNGVKGLVPCNHTSG
Protein: Probable conserved Mce associated transmembrane protein (O07420)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Probable conserved Mce associated protein
- Probable conserved Mce associated membrane protein
- Mce-family protein Mce1F
- Probable conserved Mce associated membrane protein
- Mce-family protein Mce1D
- Mce-family protein Mce1C
- Conserved integral membrane protein YrbE1B
- Mce-family protein Mce1B
- Mce-family protein Mce1A
- Possible Mce-family lipoprotein LprK
Sequence:
MTVVVEKTPTTLPQATPNGAAPWHVRAGAFAIDVLPGLAVAATMALTALTVPPGSAWRWLCACLLGLTILLLAVNRLLLPTITGWSLGRALTGIRVVRRDGSAIGPWRLLVRDLAHLVDTLSLFVGWLWPLWDSRRRTFADLLLRTEVRRVEPVQRPAVIRRLTAAVALAAAGACASATAVGAAVVYVNEWQTDHTRAQLATRGPKLVVDVLSYDPETVQRDFERARSLATDRYRPQLSIQQDSVRESGPVRNQYWVTDSAVLSATPAQATMLLFMQGERGTPPNQRYIQSTVRAIFQKSRGQWRLDDLAVVMKPRQPTGEK
Protein: Uncharacterized protein (Q38C35)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLWIQICTFVVLSTCLLVPEVVNAWSYGELLPVSFHLRLKRTAAATDIPRGADDMIEVKETKNNQWLITRPLPPDNSPRFAINTRAHQPSTRLFEYATNATKQEGGSISDVAVRFQIERGLAKSTAWYPLMKTIIKKITTEKRKSKVEHSKEEHYLAGLNFHFGYQSGTFHKITSFRVEPTYSKVKNNDLELHYQWTEHRTYNPHIALCICSLVAVIAASSTLSLIFTKKTHLTKAFSKKEVRVKNHKQ
Protein: Ornithine aminotransferase, mitochondrial (EC 2.6.1.13) (Ornithine--oxo-acid aminotransferase) (Q9VW26)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Arginase
- Delta-1-pyrroline-5-carboxylate synthase
- Ornithine decarboxylase 1
- Argininosuccinate synthase
- Argininosuccinate lyase, isoform B
- Ornithine decarboxylase 2
- GH20963p
- Multifunctional fusion protein
- Pyrroline-5-carboxylate reductase
- Pyrroline-5-carboxylate reductase
Sequence:
MFAKLSARGIATRMSFLAQKTASQETTAAAGSRSELVYARENKYGAHNYHPLPVALTKGEGVFVWDVEGKRYFDYLSAYSAVNQGHCHPKIVAALTAQASKLALTSRAFYSDVLGEYEEYVTKLFGFDKVLPMNTGVEGGETACKLARKWGYLEKKIPANQAKIIFARNNFWGRTLSAVSASNDPSSYEGFGPFMPGFELIEYDNVSALEESLKDPNVCAFMVEPIQGEAGVVVPSDGYLKKVRELCTKYNVLWIADEVQTGLARTGKLLAVDYEQVQPDILILGKALSGGMYPVSAVLCNDQVMLCIKPGEHGSTYGGNPLGCRVAMAALEVLQEEKLAENAFKMGDLLRNELSTLPKDVVSVVRGKGLLNAIVINQKFDAWEVCLRLKENGLLAKPTHGDIIRFAPPLVINETQMRESIDIIRKTILSM
Protein: Zinc transporter 4 (ZRT/IRT-like protein 4) (OsZIP4) (Q6ZJ91)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Zinc transporter that mediates zinc uptake from the rhizosphere and may be responsible for the translocation of zinc within the plant.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16263903}; Multi-pass membrane protein {ECO:0000269|PubMed:16263903}.
Interaction partners:
Sequence:
MDAMRQSTPRAMLLLCAVLMLAVAPPGAATAAAVAGCECGNAAAAAVAGEDARGALRLKLVAIASILAAGAAGVLVPVLGRSFAALRPDGDVFFAVKAFAAGVILATGMVHILPAAFDALASPCGGGRGGGGGFPFAGLVAMAAAMATMMIDSVAAGYYRRSHFKKPRPVDDPADAARAAGVEEGGAEHAGHVHVHTHATHGHAHGHVHSHGHGHGHSHGSAPAAATSPEDASVAETIRHRVVSQVLELGILVHSVIIGVSLGASLRPSSIRPLVGALSFHQFFEGIGLGGCIVQANFKAKATVIMATFFSLTAPVGIALGIAISSSYSKHSSTALVVEGVFNSAAAGILIYMSLVDLLAADFNNPKLQTNTKLQLAVYLALFLGAGMMSLLAIWA
Protein: Zinc finger protein 711 (Zinc finger protein 6) (Q9Y462)
Organism: Homo sapiens (Human)
Function: Transcription regulator required for brain development. Probably acts as a transcription factor that binds to the promoter of target genes and recruits PHF8 histone demethylase, leading to activated expression of genes involved in neuron development, such as KDM5C. May compete with transcription factor ARX for activation of expression of KDM5C.
Subcellular location: Nucleus {ECO:0000305|PubMed:20346720}.
Interaction partners:
- Histone lysine demethylase PHF8
Sequence:
MDSGGGSLGLHTPDSRMAHTMIMQDFVAGMAGTAHIDGDHIVVSVPEAVLVSDVVTDDGITLDHGLAAEVVHGPDIITETDVVTEGVIVPEAVLEADVAIEEDLEEDDGDHILTSELITETVRVPEQVFVADLVTGPNGHLEHVVQDCVSGVDSPTMVSEEVLVTNSDTETVIQAAGGVPGSTVTIKTEDDDDDDVKSTSEDYLMISLDDVGEKLEHMGNTPLKIGSDGSQEDAKEDGFGSEVIKVYIFKAEAEDDVEIGGTEIVTESEYTSGHSVAGVLDQSRMQREKMVYMAVKDSSQEEDDIRDERRVSRRYEDCQASGNTLDSALESRSSTAAQYLQICDGINTNKVLKQKAKKRRRGETRQWQTAVIIGPDGQPLTVYPCHICTKKFKSRGFLKRHMKNHPDHLMRKKYQCTDCDFTTNKKVSFHNHLESHKLINKVDKTHEFTEYTRRYREASPLSSNKLILRDKEPKMHKCKYCDYETAEQGLLNRHLLAVHSKNFPHVCVECGKGFRHPSELKKHMRTHTGEKPYQCQYCIFRCADQSNLKTHIKSKHGNNLPYKCEHCPQAFGDERELQRHLDLFQGHKTHQCPHCDHKSTNSSDLKRHIISVHTKDFPHKCEVCDKGFHRPSELKKHSDIHKGRKIHQCRHCDFKTSDPFILSGHILSVHTKDQPLKCKRCKRGFRQQNELKKHMKTHTGRKIYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEFCKKGFRRPSEKNQHIMRHHKEALM
Protein: guanylate kinase (EC 2.7.4.8) (Q8I2M1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- GMP synthase
- Hypoxanthine phosphoribosyltransferase
- Ribonucleoside-diphosphate reductase
- DNA-directed RNA polymerases I, II, and III subunit RPABC2, putative
- nucleoside-diphosphate kinase
- Nucleoside diphosphate kinase
- Inosine triphosphate pyrophosphatase
- Ribonucleoside-diphosphate reductase small chain, putative
- Ribonucleoside-diphosphate reductase small chain, putative
- Pyruvate kinase
Sequence:
MNNIYPLVICGPSGVGKGTLIKKLLNEFPNYFYFSVSCTTRKKREKEKEGVDYYFIDKTIFEDKLKNEDFLEYDNYANNFYGTLKSEYDKAKEQNKICLFEMNINGVKQLKKSTHIKNALYIFIKPPSTDVLLSRLLTRNTENQEQIQKRMEQLNIELHEANLLNFNLSIINDDLTLTYQQLKNYLLNSYIHLNNHTRN
Protein: Zinc finger PHD-type domain-containing protein (Q389Y3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRIVIDVDAVLPIRYADDENNVDSNCKPFNIIEDNSQSDNDEESITKRGTEKKPAAPVVRKRSRPPSSHSSSALYSALQPRKNWAKNMFRGDTPYSLLKREDLFERCNYIMDHDDFVWCSENNVPHTLFADAVTQLERRYATCLLETVKNRTAAGGASSEENVSNWSEQTMGLGDGRGYGLAGGIACGVCSQKERSERAGDRFLRCRRCGVQAHLSCWYLNQLPLDVEDWSCPACHVARREKGLGHCCVCRRKGGVMLPYMSGVEWRRYEQLASHEIPKEDSPAAAFCHVVCALAFSELLIDEQRRVVHPAKRAKRVGVIALCVFCRSNSGEGLTMCHHKRCFTSMHPACAQIAGTIECYRAESVPAGSAWGGCNVYCSDHFREALSVAAHSEVTSVNAESAALKHVTPSGLVTLENDNHVEGSNLAGVVSNSAVAPSLDAVKLRWVEKRAQRLRESAQMVEEIRKGKRDILSVLFRPEVVKVSATEVQLSRFVFLIPELQQHINSAVEGILPVVDDEYEDVQRYRKVQSRTRHAGNTVQLYQKMQQVVSHVDVFCELSNVIRKRAALRREWVETELKILHQRCGIADDN
Protein: Uncharacterized protein At4g15545 (Q93W28)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Phosphoglycerate mutase-like protein 1
- TSA1-like protein
- ACT domain-containing protein ACR11
- ACT domain-containing protein ACR12
- Histidine-containing phosphotransfer protein 2
- LIM domain-containing protein WLIM1
- ACT domain-containing protein ACR6
- Small ribosomal subunit protein mS29
- ACT domain-containing protein ACR10
- Methylthioribose kinase
Sequence:
MSEIEEEEEEGSASAITGSRSFDLPDELLQVLPSDPFEQLDVARKITSIALSTRVSALESESSDLRELLAEKEKEFEELQSHVESLEASLSDAFHKLSLADGEKENLIRENASLSNTVKRLQRDVSKLEGFRKTLMMSLQDDDQNAGTTQIIAKPTPNDDDTPFQPSRHSSIQSQQASEAIEPAATDNENDAPKPSLSASLPLVSQTTTPRLTPPGSPPILSASGTPKTTSRPISPRRHSVSFATTRGMFDDTRSSISISEPGSQTARTRVDGKEFFRQVRSRLSYEQFGAFLGNVKDLNAHKQTREETLRKAEEIFGGDNRDLYVIFEGLITRNAH