wanglab/gogpt-training-data huggingface dataset:
Protein: Transcriptional adapter 3 (ADA3 homolog) (mADA3) (Transcriptional adapter 3-like) (ADA3-like protein) (Q8R0L9)
Organism: Mus musculus (Mouse)
Function: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex. Also known as a coactivator for p53/TP53-dependent transcriptional activation (By similarity). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcriptional adapter 2-alpha
- SAGA-associated factor 29
- Transcription initiation factor TFIID subunit 12
- SPT3, SAGA and STAGA complex component
- Histone acetyltransferase KAT2A
- Transcription initiation factor TFIID subunit 10
- Transcriptional adapter
- Transformation/transcription domain-associated protein
- Transcription initiation factor TFIID subunit 6
- Transcription factor SPT20 homolog
Sequence:
MSELKDCPLQFHDFKSVDHLKVCPRYTAVLARSEDDGIGIEELDTLQLELETLLSSASRRLRVLEAETQILTDWQDKKGDRRFLKLGRDHELGAPPKHGKPKKQKLEGKTGHGPGPGPGRPKSKNVQPKIQEYEFTDDPIDVPRIPKNDAPNRFWASVEPYCADITSEEVRTLEELLKPPEDEAEHYKIPPLGKHYSQRWAQEDLLEEQKDGARAAAVADKKKGLIGPLTELDTKDVDALLKKSEAQHEQPEDGCPFGALTQRLLQALVEENIISPMEDSPIPDMSGKESGADGASTSPRNQNKPFSVPHTKSLESRIKEELIAQGLLESEDRPAEDSEDEVLAELRKRQAELKALSAHNRTKKHDLLRLAKEEVSRQELRQRVRMADNEVMDAFRKIMAARQKKRTPTKKEKDQAWKTLKERESILKLLDG
Protein: Proline and serine-rich protein 3 (Q2NL68)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:26638075}.
Interaction partners:
- IQ domain-containing protein C
- Uncharacterized protein C19orf44
Sequence:
MDRSLPVFSIQDSPFGDAPLGRSHYWPSQSQTWCPKTLSPSRSQRSRLPQAPKALATGPNSPELFEESWPSSSGTPSLPSTTEGQMWASPAPTLIDSGDSVVAKYINRFRQAQPTSREERQPAGPTPADFWWLQSDSPDPSSQSAAAGANKPEGRPHTAVPTAVNVTSASHAVAPLQEIKQNLHTWNSSLLDLETLSLQSRAARLLKRSKASISSSSSLSPSDASTSSFPTSSDGLSPFSETFIPDSSKGLGPRAPASPAPAQAQTPTPAPAPASSQAPLRPEDDILYQWRQRRKLEQAQGSKGDRAWVPPLTPALRTLAESLKAKALPPAAGSVIRKSEATPSPGACLQPEVPLSPAEQATTVKASPPAFQVGSPEALAPPPPAADHAPSEALLAQAALLLQAAEDSDGSEFQDDPVLQVLRAHRAELSRQKREADARLSFLLDQAEDLGSWSPPAGSPPRSPRRLLRREGDSLEARRL
Protein: Claudin-10 (Oligodendrocyte-specific protein-like) (OSP-like) (P78369)
Organism: Homo sapiens (Human)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in the regulation of paracellular epithelia permeability to ions in multiple organs. It acts as a paracellular ion channel probably forming permselective pores; isoform 1 appears to create pores preferentially permeable to cations and isoform 2 for anions. In sweat glands and in the thick ascending limb (TAL) of Henle's loop in kidney, it controls paracellular sodium permeability which is essential for proper sweat production and renal function.
Subcellular location: [Isoform 1]: Cell junction, tight junction {ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:35650657}. Cell membrane {ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:28686597, ECO:0000269|PubMed:28771254, ECO:0000269|PubMed:35650657}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell junction, tight junction {ECO:0000269|PubMed:19383724}. Cell membrane {ECO:0000269|PubMed:19383724}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Occludin
- Tight junction protein 1
- Claudin-16
- Claudin-23
- Claudin-8
- Tight junction protein ZO-3
- Claudin-9
- Claudin-18
- Claudin-12
- Claudin-11
Sequence:
MASTASEIIAFMVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYWANLWKACVTDSTGVSNCKDFPSMLALDGYIQACRGLMIAAVSLGFFGSIFALFGMKCTKVGGSDKAKAKIACLAGIVFILSGLCSMTGCSLYANKITTEFFDPLFVEQKYELGAALFIGWAGASLCIIGGVIFCFSISDNNKTPRYTYNGATSVMSSRTKYHGGEDFKTTNPSKQFDKNAYV
Protein: Serpin 100A (Q9VA48)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serpin 43Aa
- 20-hydroxyecdysone protein
- Male accessory gland protein
Sequence:
MKAVLCAIFVTLLAAIGQGLPTQLEDENHGSFAGQVSQLIALQLLKFNKDIDANQVHSPLGVASILAMLAEASEGDTYSEFEQVFGYPKDRTKLRDAYKRILGSYQNRDAAVALPSFQTWLYIYRNNSAREEFKDLLEKHYYVDVKDISRQEYDWNEPNTSLQLSEEKDNTDSTEGSTEQSNSKDVIGFETLKRIKLDDEDIPAIPSDGYGQEIIDKEASKFDRDVDDKQYVEKPVAQAEAELLQKEQKQQATTESELESQPEETTTLSVEKQEKPDMAAEENPAEKQQNKRSDQEESQIKNLEENETVQEEEKLAKIMAAPALTAGEPEKVRLPLQKLENAVKTAAKDGADEIMLALESHLPSVSRVNGARSLFQQDDITSALSANSITGRSAGSKSKMLLFNGLYYRGSWANPFYQLRDGSDEFFFMTNEDAVKAPMMHARGKFQVADLPQVKARVLSLPYETSRYALCIVLPDETEGLSDVISQLQTSDFLLAKKQFQMKELHISMPKFQVEETSRSEAMLKQMGLKKVFSRTEAQLSLLSEDPDVHVDEIVQFVNVRVDEGGSSANSLSAATMQARTPSVESTVLPVPEPEPELPGVERFEVNRPFAYFIVDCQEQFVLASGKIYTPEFKEDLPSVSIEVELEQS
Protein: Proline iminopeptidase (PIP) (EC 3.4.11.5) (Prolyl aminopeptidase) (PAP) (P93732)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specifically catalyzes the removal of N-terminal proline residues from peptides.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Aminotransferase ALD1, chloroplastic
- Protein SAR DEFICIENT 4
- Probable flavin-containing monooxygenase 1
- Probable prolyl 4-hydroxylase 9
- Pyrroline-5-carboxylate reductase
- Probable prolyl 4-hydroxylase 10
- Prolyl 4-hydroxylase 13
- Probable prolyl 4-hydroxylase 12
- Prolyl 4-hydroxylase 1
- Probable prolyl 4-hydroxylase 7
Sequence:
MNLILASFSLAPCFCVRFFPSNHNNLNLLFPGQRKIQVSCGGKSEVLKSDTMEPHEAETFVNKRTLYAPIEPYSSGNLKVSDVHTLYWEQSGKPDGHPVVFLHGGPGGGTAPSNRRFFDPEFYRIVLFDQRGAGKSTPHACLEENTTWDLVNDIEKLREHLKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVLRGIFLLRKKEIDWFYEGGAAAIYPDAWEEFRDLIPENERGSSLVDAYHKRLNSDDLEIQYAAARAWTKWEMMTAYLRPNLENVQKAEDDKFSLAFARIENHYFVNKGFFPSDSHLLDNVDKIRHIKTTIVQGRYDVCCPMMSAWDLHKAWPEAELKIVYDAGHSANEPGISAELVVANEKMKALMG
Protein: DNA/RNA-binding protein ALBA1 (PfAlba1) (Q8IAX8)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000269|PubMed:22167473}. Chromosome, telomere {ECO:0000269|PubMed:22167473}. Cytoplasm {ECO:0000269|PubMed:22167473, ECO:0000269|PubMed:26415947}. Note=Localizes to the nucleus in the ring stages and expands to punctate loci in the cytoplasm during the trophozoite and schizont stages. {ECO:0000269|PubMed:22167473, ECO:0000269|PubMed:26415947}.
Interaction partners:
- Ribonuclease P/MRP protein subunit RPP1, putative
- Ribonuclease P protein subunit RPR2, putative
- Ribonuclease P protein subunit p29, putative
- H/ACA ribonucleoprotein complex subunit 2
Sequence:
MKKDREPIDEDEMRITSTGRMTNYVNYGAKILGDEDKKSIKIKATGNAIGKAVTLAEIIKRRFKGLHQITRCGSTVITDQYVSGQDNSEHVVQEKTVSFIEILLSREQLDMKDAGYQPPLDEKYVKEMTPEEIVNSRPFRRGGFRPRFYRGFRGGRGGFLRRGGYRGFGDRVYEPRSSFRGGRGSGYGGNFGRGGYRSGGGMGGGFRGGFRGGFRGGRDGGYRGGNRGGSRSGFRGGRGGFRGGRALS
Protein: Deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) (DNA photolyase) (OsCPDII) (Photoreactivating enzyme) (Q6F6A2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutylpyrimidine dimers (CPDs), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. Required for plant survival in the presence of UV-B light. Not involved in the repair of (6-4) photoproducts.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Os05g0210500 protein
- 
Sequence:
MPPTSVSPPRTAPGPANPSPAHPSRVRVIHPGGGKPGGPVVYWMLRDQRLADNWALLHAAGLAAASASPLAVAFALFPRPFLLSARRRQLGFLLRGLRRLAADAAARHLPFFLFTGGPAEIPALVRRLGASTLVADFSPLRPVREALDAVVGDLRREAPGVAVHQVDAHNVVPVWTASAKMEYSAKTFRGKVSKVMDEYLVEFPELPAVVPWDREQPEGVDWDALIARVCSEAENVPEIDWCEPGEEAAIEALLGSKDGFLTKRIKSYETDRNDPTKPRALSGLSPYLHFGHISAQRCALEAKKCRHLSPKSVDAFLEELVVRRELADNFCYYQPQYDSLSGAWEWARKTLMDHAADKREHIYTREQLENAKTHDPLWNASQLEMVHHGKMHGFMRMYWAKKILEWTSGPEEALSTAIYLNDKYEIDGRDPSGYVGCMWSICGLHDQGWKERPVFGKIRYMNYAGCKRKFDVDAYISYVKRLAGQSKKRNAEESPNPVVKLSKSQH
Protein: Eukaryotic translation initiation factor 3 subunit K (cDNA FLJ55131, highly similar to Eukaryotic translation initiation factor 3 subunit 12) (B4DQ48)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIDQAHQEERPIRQILYLGDLLETCHFQAFWQALDENMDLLEGITGFEDSVRKFICHVVGITYQHIDRWLLAEMLGDLSDSQLKVWMSKYGWSADESGQIFICSQEESIKPKNIVEKIDFDSEW
Protein: SRP-independent targeting protein 2 homolog (Meiotically up-regulated gene 69 protein) (O14193)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May function in a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum (By similarity). Has a role in meiosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Autophagy-related protein 9
- Mitochondrial import inner membrane translocase subunit tim10
Sequence:
MANAAQKKLAAQNKHILTFMLAADLIVNVLFWILRFFVRSGLSKFSKFVYAFASISSGFLHYQLHRAAAPKYDARGSLLYVGQDLLQEGVTSYMVDYMYFSWILIFLAALTSVKVFAFYLLVPIFVVYKAAPLLKMLLQQLKNFKNQALNQPPQQQQQQQQQQHQQHATPSEPVLSKRQQKLRKKAAKYSRP
Protein: Glucosamine 6-phosphate N-acetyltransferase (EC 2.3.1.4) (A0A8I6AKF3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKPDETPMFDPSLLKEVDWSQNTAIFSPAISPMHPGEGLVLRPLCTADLNKGFFKVLGQLTETGVVSPEQFMKSFEHMKKSGDYYVTVVEDVTLGQIVATATLIIEHKFIHSCAKRGRVEDVVVSDELCTCNHGNWKLNCYKITLECLPQNVGFYKKFDYTVSEENYMCRRFLK
Protein: 4-hydroxyphenylpyruvate 3-dimethylallyltransferase (EC 2.5.1.111) (4HPP 3-dimethylallyltransferase) (Aromatic prenyltransferase NovQ) (Dimethylallyl diphosphate:4-hydroxyphenylpyruvate dimethylallyl transferase) (Novobiocin biosynthesis protein Q) (Q9L9F1)
Organism: Streptomyces niveus (Streptomyces spheroides)
Function: Magnesium-independent aromatic prenyltransferase that catalyzes the irreversible transfer of a dimethylallyl group to 4-hydroxyphenylpyruvate to produce the ring A structure in the novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases. It is able to prenylate many different compounds, including the phenylpropanoids 4-coumarate and caffeate, the plant polyketide resveratrol, the (iso)flavonoid naringenin, apigenin, daidzein and genistein, and the dihydroxynaphthalenes 1,6-DHN and 2,7-DHN.
Subcellular location: Cytoplasm {ECO:0000269|Ref.3}.
Interaction partners:
Sequence:
MPALPMNQEFDRERFRVDLRATAAAIGAPVTPRVTDTVLETFRDNFAQGATLWKTTSQPGDQLSYRFFSRLKMDTVGRAVDAGLLDGTHPTVPIVEDWSDLYGGTPVQSADFDAGRGMAKTWLYFGGLRPAEDILSVPALPAPVQARLKDFLGLGLAHVRFAAVDWRHRSANVYFRGQGPLDTAQFARVHALSGGTPPAADVVAEVLAYVPEDYCVAITLDLHTGAIDRVCFYALKVPKDARPRVPARIATFLEVAPSHDPEECNVIGWSFGRSGDYVKAERSYTGNMTEILSGWNCFFHGEEGRDHDLRALQDTGSITGGAR
Protein: 23.6 kDa heat shock protein, mitochondrial (OsHsp23.6) (B7EZJ7)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- 16.9 kDa class I heat shock protein 3
- 18.1 kDa class I heat shock protein
- Chaperone protein ClpB1
- 23.2 kDa heat shock protein
Sequence:
MALARQCLSKRLAAGCALARPLHAASPVAAAAANSHGPLNFRALFSSAGADAAATTGGCAPAKGDGHSREVAVVDRSRRRWPWRDLRDFVPLRLVDGIGSALSQVAETLTRPLTGKVREDEERYRLRFEVPGLGKDDVRVYVDDGVLAIHGEKRDVVEEDRGRDGDGECWAAATYHAGLLLPEDAVAEGITAEVRDGVLHVTVPRSPERKRSVTEVKVR
Protein: Membrane dipeptidase (Q9HTG8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- 4-vinyl reductase 4VR domain-containing protein
- DgcA, Dimethylglycine catabolism
- Sarcosine oxidase gamma subunit
- Electron transfer flavoprotein alpha/beta-subunit N-terminal domain-containing protein
- Sarcosine oxidase delta subunit
- DgcB, Dimethylglycine catabolism
- Sarcosine oxidase subunit beta subunit beta)
- Glycine betaine monooxygenase oxygenase subunit
- Glycine betaine monooxygenase reductase subunit
- Glutathione-independent formaldehyde dehydrogenase
Sequence:
MSPAELHADSIVIDGLIIAKWNRELFEDMRKGGLTAANCTVSVWEGFQATVNNIAASNKLIRDNSDLVIPVRSTADIRKAKEQGKTGILYGFQNAHAFEDQIGYVEVFKQLGVGIVQMCYNTQNLVGTGCYERDGGLSGFGREIVAEMNRVGIMCDLSHVGSKTSEEVILESKKPVCYSHCLPSGLKEHPRNKSDEELKFIADHGGFVGVTMFAPFLKKGIDSTIDDYAEAIEYVMNIVGEDAIGIGTDFTQGHGHDFFEWLTHDKGYARRLTNFGKIVNPLGIRTVGEFPNLTETLLERGMPERVVRKVMGENWVRVLRDVWGE
Protein: HTH-type transcriptional repressor KstR2 (A0R4Z6)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Controls the expression of a small regulon that may play a role in the utilization of cholesterol.
Interaction partners:
- HTH-type transcriptional repressor KstR
- Acetyl-CoA acetyltransferase
- Enoyl-CoA hydratase
- Short chain dehydrogenase
- 3-ketosteroid-9-alpha-monooxygenase, oxygenase component
- Acyl-CoA dehydrogenase IpdE1
- Short chain dehydrogenase
- Coenzyme A transferase, subunit A
- Steroid C26-monooxygenase-3-oxocholest-4-en-26-oate forming])
- 3-oxosteroid 1-dehydrogenase
Sequence:
MAPDTPSQPASRRDELLQLAATMFADRGLKATTVRDIADSAGILSGSLYHHFKSKEQMVEEVLRDFLDWLFGRYQQILDTATSPLEKLTGLFMASFEAIEHRHAQVVIYQDEAKRLSDLPQFDFVETRNKEQRKMWVDILQEGVADGSFRPDLDVDLVYRFIRDTTWVSVRWYKPGGPLSAEQVGQQYLAIVLGGITQSQGDKHA
Protein: Large ribosomal subunit protein eL6 (60S ribosomal protein L6) (TAX-responsive enhancer element-binding protein 107) (TAXREB107) (P47911)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q02878}. Cytoplasm {ECO:0000269|PubMed:36517592}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q2YGT9}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q02878, ECO:0000250|UniProtKB:Q2YGT9}.
Interaction partners:
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein eL37
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein eL24
Sequence:
MAGEKAPDTKEKKPAAKKAGSDAAASRPRAAKVAKKVHPKGKKPKKAKPHCSRNPVLVRGIGRYSRSAMYSRKALYKRKYSAAKTKVEKKKKKEKVLATVTKTVGGDKNGGTRVVKLRKMPRYYPTEDVPRKLLSHGKKPFSQHVRRLRSSITPGTVLIILTGRHRGKRVVFLKQLDSGLLLVTGPLVINRVPLRRTHQKFVIATSTKVDISDVKIPKHLTDAYFKKKQLRKPRHQEGEIFDTEKEKYEITEQRKADQKAVDLQILPKIKAVPQLQGYLRSQFSLTNGMYPHKLVF
Protein: CCR4-NOT transcription complex subunit 7 (EC 3.1.13.4) (BTG1-binding factor 1) (CCR4-associated factor 1) (CAF-1) (Caf1a) (Q9UIV1)
Organism: Homo sapiens (Human)
Function: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT8. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:9820826}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q60809}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:31439799}. Note=NANOS2 promotes its localization to P-body (By similarity). Recruited to cytoplasmic ribonucleoprotein membraneless compartments by CAPRIN1, promoting deadenylation of mRNAs (PubMed:31439799). {ECO:0000250|UniProtKB:Q60809, ECO:0000269|PubMed:31439799}.
Interaction partners:
- CCR4-NOT transcription complex subunit 6-like
- CCR4-NOT transcription complex subunit 9
- Protein Tob1
- CCR4-NOT transcription complex subunit 3
- CCR4-NOT transcription complex subunit 6
- CCR4-NOT transcription complex subunit 2
- CCR4-NOT transcription complex subunit 1
- CCR4-NOT transcription complex subunit 10
- CCR4-NOT transcription complex subunit 4
- Protein PAT1 homolog 1
Sequence:
MPAATVDHSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQLGLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFHSGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMAFFKMREMFFEDHIDDAKYCGHLYGLGSGSSYVQNGTGNAYEEEANKQS
Protein: Rho guanine nucleotide exchange factor scd1 (P40995)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for mating and morphogenesis. May contain a cryptic binding site for cdc42 that is enhanced by binding Ras. Interacts directly with scd2. Promotes the exchange of cdc42-bound GDP by GTP. Involved in septation and stimulates the elongation of conjugation tubes.
Subcellular location: Nucleus. Cytoplasm. Note=Located at the growing cell ends and tips of conjugation tubes.
Interaction partners:
- Cell division control protein 42 homolog
- Protein scd2/ral3
- Ras-like protein 1
- Serine/threonine-protein kinase shk1/pak1
- Probable Rho-type GTPase-activating protein 4
- Rho guanine nucleotide exchange factor gef1
- Guanine nucleotide-binding protein subunit beta
- Protein kinase byr2
- Protein MON2 homolog
- Formin-3
Sequence:
MAYFQDRKTSSRSLPSYINHSTQNLVGPRKDETNLSEYMKLRLLQSPSQVIYNLENTVSLYRRCLNLRKRLMDISELAAFFDSIHREALNSSFKILEFKDIEFDDPVTEIWLFCRLGYPLCALFNCLPVKQKLEVNSSVSLENTNVCKASLYRFMLMCKNELGLTDAALFSISEIYKPSTAPLVRALQTIELLLKKYEVSNTTKSSSTPSPSTDDNVPTGTLNSLIASGRRVTAELYETELKYIQDLEYLSNYMVILQQKQILSQDTILSIFTNLNEILDFQRRFLVGLEMNLSLPVEEQRLGALFIALEEGFSVYQVFCTNFPNAQQLIIDNQNQLLKVANLLEPSYELPALLIKPIQRICKYPLLLNQLLKGTPSGYQYEEELKQGMACVVRVANQVNETRRIHENRNAIIELEQRVIDWKGYSLQYFGQLLVWDVVNVCKADIEREYHVYLFEKILLCCKEMSTLKRQARSISMNKKTKRLDSLQLKGRILTSNITTVVPNHHMGSYAIQIFWRGDPQHESFILKLRNEESHKLWMSVLNRLLWKNEHGSPKDIRSAASTPANPVYNRSSSQTSKGYNSSDYDLLRTHSLDENVNSPTSISSPSSKSSPFTKTTSKDTKSATTTDERPSDFIRLNSEESVGTSSLRTSQTTSTIVSNDSSSTASIPSQISRISQVNSLLNDYNYNRQSHITRVYSGTDDGSSVSIFEDTSSSTKQKIFDQPTTNDCDVMRPRQYSYSAGMKSDGSLLPSTKHTSLSSSSTSTSLSVRNTTNVKIRLRLHEVSLVLVVAHDITFDELLAKVEHKIKLCGILKQAVPFRVRLKYVDEDGDFITITSDEDVLMAFETCTFELMDPVHNKGMDTVSLHVVVYF
Protein: Ribosomal protein S1 (Q2F910)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MFLVDAGLGTPKICMQDELTGLPIKRATRFENKVGSKNVVAGESLIKKRIEERFFIDLVAGESLIKERAAARFNDFVGSLDVAAGEPLLLPQRFRQNRAWIELKKIWQTKKKVKGFRIKKIKGGYSVAIAGFITFLPFAKKKKRIANDRFTIDSFNPKRRDIVIIAADQTRT
Protein: Bet1-like protein At4g14600 (Q8VXX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE associated with ER-derived vesicles (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- VAMP-like protein YKT62
- Golgi SNAP receptor complex member 1-1
- Golgi SNAP receptor complex member 1-2
- Syntaxin-31
- Syntaxin-32
- VAMP-like protein YKT61
- Bet1-like protein At1g29060
- At3g55600
- Vesicle transport v-SNARE family protein
- SNARE-like superfamily protein
Sequence:
MASNPHRSGAGGSLYGGAAPYRSREGLSTRNAAGSEEIQLRIDPMHSDLDDEITGLHGQVRQLKNIAQEIGSEAKFQRDFLDELQMTLIRAQAGVKNNIRKLNMSIIRSGNNHIMHVVLFALLVFFVLYIWSKMFKR
Protein: Fibroblast growth factor (FGF) (A0A8J8XTJ6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGSPRSALSCLEQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPRGHHTTEQSLRFEFLNYPPFTRSLRGSQRTWAPEPR
Protein: Metacaspase (Q386I9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSEKVAGYVQCVVGIIFGVVTGGASIYVTIAMELLQVAVPYVLVTLGLQRRPPKGGVDKAMAEAESVEAEVMKKPSKQQRSFRALFIGIDYKGTPAELRGCQADAVMMAGTMEKIGIPITERCVLMDTDDPRFNAIKPTRANILQHMAWLVKDAKPGDALFLHYSGYGAQVRAEEDKEEEFDQCIVPCDYEENGCILDNELHEIISTLPRGVRLTAVFDCSHAGTLLDLPFSLICSSNDCSAVGEMKRIRTGGDVNAHVLMFSACGDDEAAADLPNAGDFVEGASGSGGAATQCFISMLLNKTPGTIYSLLSTTRDKLREKGFKQSPQMSASRCLSLTEKFTLTELFSVAEPCPNILTGEPRWKTTPLGGK
Protein: DASH complex subunit dam1 (Outer kinetochore protein dam1) (Q9HDZ6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore.
Subcellular location: Nucleus {ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:16079915, ECO:0000269|PubMed:18256284, ECO:0000269|PubMed:20624975}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:16079915, ECO:0000269|PubMed:20624975}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:16079915, ECO:0000269|PubMed:18256284, ECO:0000269|PubMed:20624975}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18256284, ECO:0000269|PubMed:20624975}. Note=Associates with the mitotic spindle and the kinetochore. Kinetochore association occurs only during mitosis (PubMed:16079914). During metaphase, localizes to the plus-ends of intranuclear microtubules (INMs) (PubMed:18256284). In the cytoskeleton, localizes to cortical microtubules (PubMed:20624975). {ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:18256284, ECO:0000269|PubMed:20624975}.
Interaction partners:
- DASH complex subunit dad1
- DASH complex subunit spc19
- DASH complex subunit dad2
- DASH complex subunit dad3
- DASH complex subunit ask1
- DASH complex subunit duo1
- DASH complex subunit dad4
- Kinetochore protein ndc80
- DASH complex subunit spc34
- Spindle pole body component alp14
Sequence:
MEKYQKATQNPLENVDNVKIESENAIPSNLQAFTKSLAVLDDNVSEFRKRMNHLSATKQILDNFNESFSSFLYGLQINAFCVDYENAPLSESFLLQAKKDQFKATLMTRTGHSISDPPYDGGVISHDPNFATADETFATNDTSFIERPETYSASR
Protein: Putative maltooligosyl trehalose synthase (EC 5.4.99.15) ((1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase) (P9WQ21)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl alpha-D-glucoside) by intramolecular transglycosylation.
Interaction partners:
- Glycogen operon protein GlgX homolog
- Malto-oligosyltrehalose trehalohydrolase
- Trehalose synthase/amylase TreS
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- 4-alpha-glucanotransferase
- Trehalose-6-phosphate synthase
- Maltokinase
- Trehalose-phosphate phosphatase
- 1,4-alpha-glucan branching enzyme GlgB
- Uncharacterized glycosyl hydrolase Rv2006
Sequence:
MAFPVISTYRVQMRGRSNGFGFTFADAENLLDYLDDLGVSHLYLSPILTAVGGSTHGYDVTDPTTVSPELGGSDGLARLSAAARSRGMGLIVDIVPSHVGVGKPEQNAWWWDVLKFGRSSAYAEFFDIDWELGDGRIILPLLGSDSDVANLRVDGDLLRLGDLALPVAPGSGDGTGPAVHDRQHYRLVGWRHGLCGYRRFFSITSLAGLRQEDRAVFDASHAEVARWFTEGLVDGVRVDHLDGLSDPSGYLAQLRELLGPNAWIVVEKILAVDEALEPTLPVDGSTGYDVLREIGGVLVDPQGESPLTALVESAGVDYQEMPAMLADLKVHAAVHTLASELRRLRRCIAAAAGADHPLLPAAVAALLRHIGRYRCDYPGQAAVLPCALAETHSTTPQLAPGLQLIAAAVARGGEPAVRLQQLCGAVSAKAVEDCMFYRDARLVSLNEVGGEPRRFGVGAAEFHHRAATRARLWPRSMTTLSTHDTKRGEDVRARIGVLSQVPWLWAKFIGHAQAIAPAPDAVTGQFLWQNVFGVWPVSGEVSAALRGRLHTYAEKAIREAAWHTSWHNPNRAFEDDVHGWLDLVLDGPLASELTGLVAHLNSHAESDALAAKLLALTVPGVPDVYQGSELWDDSLVDPDNRRPVDYGTRRVALKALQHPKIRVLAAALRLRRTHPESFLGGAYHPVFAAGPAADHVVAFRRGDDILVAVTRWTVRLQQTGWDHTVLPLPDGSWTDALTGFTASGHTPAVELFADLPVVLLVRDNA