wanglab/gogpt-training-data huggingface dataset:
Protein: UBX domain-containing protein (Q57W23)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYVCENVDAALAYVNKWRAPLLILVNSADSAAAAATCSLNCDDIPEFYASGRVHGKKVINPNFRFSSEAIQHSGPLQRRALEVFLKESRLDSVVVVHLIVAGSAAHELFVAAVPEAKDVAPCLFVFSPKQSGMERVALHGPNLTPANISNVLRTSFQALQVPESTGARSTFLTQVGDMNAAQQRLLLSQPQDAGAPRFGALSTVAVTPAARAAPAGDTTRTHPAVPSQMGEKRAGDKDEGGVAKGDSDEAPHSKRSVVECRDGEGCRVKYRGGGSDERLETETVSGPEEGKQTEHPPCGSSTVNDEGDKTAVATADSQSASNGIDLRCGLPNGETYTVRGLDSSTATLAANVREQVATLLEHNEFVFARPYPPHRFTVEEETRTLETIGMRNSSVVRVIPTGAPSYGAATSQVKSGATEVFGMVSSWFGRASGFGNSSTAPQASGTSATRAARPPNSRVRTMAQMLAENEEEENRRALRNSAMEGGQGSRANRYYGGASTEYVGRDDGEDSEDEEVRRRS
Protein: Cytochrome P450 regulator dap1 (O13995)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for sterol biosynthesis. Functions as a positive regulator of cytochrome P450 enzymes erg5 and erg11. Function requires bound heme.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MASTQVVFIVTLFLYLLITRWRRKNEKSFIASEEPKQPEWRDYTPAELKEYNGSKNSLVFLAIKGTVYNVTMGSKFYGPQGPYSAFAGHDASRGLAKNSFDDEFIPDSDAEELDDCSDLNDEERQALNDWKAFFDQKYQAVGRLISPREARAAATISETEEKVAHN
Protein: Fibrous sheath CABYR-binding protein (PKA-phosphorylated calcium and CABYR-binding protein) (A1EGX6)
Organism: Mus musculus (Mouse)
Function: May be involved in the later stages of fibrous sheath biogenesis and spermatozoa capacitation. Inhibits ROPN1 and ROPN1L SUMOylation. Binds calcium.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:17855365}. Note=Localizes to cortex of the fibrous sheath including the surface of the longitudinal columns and ribs of the principal piece of sperm flagella. {ECO:0000269|PubMed:17855365}.
Interaction partners:
- Calcium-binding tyrosine phosphorylation-regulated protein
- Transmembrane protein 190
Sequence:
MEECEEPEEPISLGRQEYRRRRRPSQPMVDKSQQTEITEKRKAMASVQPPAPKATHSIGNIPGSKDNYSRKEYESLRLSSQLQKTLMKRKHVQDMTDKSLQTEPIVEEKVEVIFIDKTLKLEENTAGVGEIAPELPQSIPEVEIPTSRPTSHLIDRSQQTSCTGDWSLIYICPKEKVDKEQQTYFSELEIIIRSIPGSSMTKSKEETIPIAQEDPLVEINGSLEIEVLSPEELPDVMMSFTEGEISGELQALSNGEATVKGELFLTEEIPIQAPSPAEETSAAETATTTAKDVVDIQAPPADKLSSVEAPADISPTLVQGALSDKPSDQQYPQGTEMAPSELPVEDLDPFSEEVLEKVQALTTDSMLEDLGIAESTIAEETSGKVQHPLSEETSKEVPAEVHFPIAADFEESAILINEKFATDEVFEEYKPPIIEEVSADKATAEVQPPSAEDASEEVASSEVLPPSTEQGTVEDLTAEVLSTPTEEGPTEVPPQPTEEGPAEVPPPLSEEGPAEVPPAPAEEAPAEVLPPPAEEAPAEVPPPLTEEGPAEVPPPLTEEGPAEVPLAPAEEVPAEFLPPPAEEVPAEVPPPLTEEGPAEVPPPLTEEGPEEVPPLPAEEAPTKVPPSPAEKGSAEVSPPQTEEGPAEVPPPPAEEFPTEVPSSSAEEGSSEVPLPPTAERPEEAPPPATEEAPVEVLPPATEEAPVEVLPPATEEAPVEVQSPAAEEGLAEVPPPPTEESPTHDVPTEVQVPQAKESPGQVLPLSGESTAEEASAQVQPPSFEKAPLESLPLEEVEKIHLDNLPFEVQPLPTEDIAIGVPAESQALPADENPAREDTVETQPSSFEGAPIAENPIEAPLPASEADTGREDSAVHPSSLGPTDEAPAEIQILQTDDIPTEMSPVENQPLPAEEGFPEVVSEEEATAAEVRFPLSEGAPAQEATVEAQLTSVEESPKRASVDVQPLSPETPVEESPGVDLPLKTNEVTMQEFRVEKMPAEDSLPPSEQTPADQVLLKEHRLSQVADISEKELESTTLTSDKMSEGIDSVPEDVSGTKDDQISTFKIEGTIKIELKN
Protein: EF hand (Q57TS8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSFMLATNCPDELCCALCLDSWKKPVELQPCGHIFCQECIGAPRVCPVCRAPVNCTKQPHRSLVNLAQNLPVRCSSCGWTGRREGSDSHTCPTASWSGSTEAPSTTNAQSTCQGSRQQSVADTPWLRYGLTQEEYDSIVALFVFFDSDESGHLCREEMGRLARWLNFARTDDDIDRMFREMDEDGTGTLCLEEFLSWLSKNRPDPSVLYGMSQQQYNCVMMQFRLYDRDRDGFLDADDFSKLAVRIGDVPDIESGMQLFRSITTGHCEKIGLHQFLLYCVGRMFR
Protein: 26S proteasome non-ATPase regulatory subunit 7 homolog B (26S proteasome regulatory subunit RPN8b) (AtRPN8b) (Protein MATERNAL EFFECT EMBRYO ARREST 34) (Q9C774)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome non-ATPase regulatory subunit 1 homolog B
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome regulatory subunit 6A homolog B
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome regulatory subunit 4 homolog B
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 3 homolog B
- 26S proteasome non-ATPase regulatory subunit 1 homolog A
Sequence:
MDVIKTQQISARTIEKVIVHPLVLLSIVDHYNRVAKDTSKRVVGVLLGSSSRGTVDVTNSYAVPFEEDDKDTSIWFLDHNYHESMFHMFKRINAKEHIVGWYSTGPKLRENDLDVHALFNGYVPNPVLVIIDVQPKELGIPTKAYYAVEEVKENATQKSQQVFVHVPTEIAAHEVEEIGVEHLLRDVKDTTISTLATEVTAKLTALKGLDARLREIRTYLDLVIEGKLPLNHEILYHLQDVFNLLPNLNVNELVKAFAVKTNDMMLVIYLSSLIRSVIALHSLINNKLLNKEHEKAEDSKPVDIPLITES
Protein: Collagen type IV alpha 1 chain (F1MA59)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
- Collagen type IV alpha 2 chain
- CD44 antigen
- Glycoprotein VI
- Integrin beta-1
- Collagen type IV alpha 6 chain
- Laminin subunit beta-1
- Integrin subunit alpha 5
- Integrin alpha-1
- Collagen type XVIII alpha 1 chain
- Integrin subunit alpha 3
Sequence:
MGPRLSVWLLLPLAALLLHEERSRAAAKGDCGGSGCGKCDCHGVKGQKGERGFPGLQGVIGFPGMQGPEGPHGPPGQKGDAGEPGLPGTKGTRGPPGAAGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFSGNPGPPGLPGMKGDPGEILGHVPGTLLKGERGFPGIPGAPGSPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGSSFQGPKGDKGEQGVSGPPGVPGQAQVKEKGDFAPTGEKGQKGEPGFQGTPGYGEKGEPGKPGPRGKPGKDGEKGEKGSPGFPGESGYPGLPGRQGPQGEKGEPGLPGPPGTVVGTRPLGEKGERGYPGSPGLRGEPGPKGYPGSPGQPGPPGFAVPGQTGAPGFPGERGEKGERGSPGVSLPGPSGRDGAPGPPGPPGPPGQPGHTNGIVECQPGPPGDQGPPGIPGQPGLTGEVGQKGQKGESCLACDTEGLRGPPGPQGPPGEIGFPGQPGAKGDRGLPGRDGLEGLPGPQGSPGLIGQPGAKGEPGEIFFDMRLKGDKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPGSIGLKGERGPPGGVGFPGSRGDIGPPGPPGVGPIGPIGEKGQAGLPGGPGSPGLPGPKGEAGKVVPLPGPPGAAGLPGSPGFPGPQGDRGFPGTPGRPGNPGEKGAVGQPGIGFPGLPGPKGVDGLPGEIGRPGSPGRPGFNGLPGNPGPQGQKGEPGIGLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPGVQGPAGPPGVPGIGPPGAMGPPGGQGPPGSSGPPGVKGEKGFPGFPGLDMPGPKGDKGSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPAGAPGLPGEKGDHGFPGSSGPRGDPGFKGDKGDVGLPGMPGSMEHVDMGSMKGQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGIPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGSQGVPGSPGEKGAKGEKGQSGLPGIGIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGLPGRGFPGFPGTKGDKGSKGEVGFPGLAGSPGIPGAKGEQGFMGPPGPQGQPGLPGTPGHPVEGPKGDRGPQGQPGLPGHPGPMGPPGFPGIDGPKGDKGNPGWPGAPGAPGPKGDPGFQGMPGIGGSPGITGSKGDMGPPGVPGFQGQKGLPGLQGVKGDQGDQGIPGPKGLQGPPGPPGPYDVIKGEPGLPGPEGPPGLKGLQGPPGPKGQQGVTGSVGLPGPPGVPGFDGAPGQKGETGPFGPPGPRGFPGPPGPDGLPGSMGPPGTPSVDHGFLVTRHSQTTDDPLCPPGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLSTPEPMPMSMAPISGDNIRPFISRCAVCEAPAMVMAVHSQTIQIPQCPNGWSSLWIGYSFVMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRRT
Protein: Oligodendrocyte transcription factor 1 (Oligo1) (Class B basic helix-loop-helix protein 6) (bHLHb6) (Class E basic helix-loop-helix protein 21) (bHLHe21) (Q8TAK6)
Organism: Homo sapiens (Human)
Function: Promotes formation and maturation of oligodendrocytes, especially within the brain. Cooperates with OLIG2 to establish the pMN domain of the embryonic neural tube (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- DNA-binding protein inhibitor ID-4
- Oligodendrocyte transcription factor 2
- DNA-binding protein inhibitor ID-2
- Transcription factor SOX-10
- Homeobox protein Nkx-2.2
- Chondroitin sulfate proteoglycan 4
- Myelin proteolipid protein
- Achaete-scute homolog 1
- Glial fibrillary acidic protein
- Myelin basic protein
Sequence:
MYYAVSQARVNAVPGTMLRPQRPGDLQLGASLYELVGYRQPPSSSSSSTSSTSSTSSSSTTAPLLPKAAREKPEAPAEPPGPGPGSGAHPGGSARPDAKEEQQQQLRRKINSRERKRMQDLNLAMDALREVILPYSAAHCQGAPGRKLSKIATLLLARNYILLLGSSLQELRRALGEGAGPAAPRLLLAGLPLLAAAPGSVLLAPGAVGPPDALRPAKYLSLALDEPPCGQFALPGGGAGGPGLCTCAVCKFPHLVPASLGLAAVQAQFSK
Protein: Large ribosomal subunit protein uL2 (60S ribosomal protein L8) (P62919)
Organism: Rattus norvegicus (Rat)
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 {ECO:0000250|UniProtKB:P62917}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS7
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein eL32
Sequence:
MGRVIRGQRKGAGSVFRAHVKHRKGAARLRAVDFAERHGYIKGIVKDIIHDPGRGAPLAKVVFRDPYRFKKRTELFIAAEGIHTGQFVYCGKKAQLNIGNVLPVGTMPEGTIVCCLEEKPGDRGKLARASGNYATVISHNPETKKTRVKLPSGSKKVISSANRAVVGVVAGGGRIDKPILKAGRAYHKYKAKRNCWPRVRGVAMNPVEHPFGGGNHQHIGKPSTIRRDAPAGRKVGLIAARRTGRLRGTKTVQEKEN
Protein: Ankyrin repeat and SOCS box protein 9 (ASB-9) (Q91ZT8)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes at least two forms of creatine kinase, CKB and CKMT1A (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96DX5}.
Interaction partners:
- Elongin-C
- Creatine kinase B-type
- Elongin-B
- Cullin-5
- Creatine kinase U-type, mitochondrial
- Elongin-B
- Creatine kinase M-type
- Ankyrin repeat and SOCS box protein 6
Sequence:
MDGEQRGRSDRPGGSPHLPFLSNPLMGDVVSDWSPLHDAAIHGCLLTLRNLISQGWPVNIITADHVSPLHEACLRGHLSCASVLLSHGAQVNGMTIDWRTPLFNACVSGSQDCVNLLLQHGATPHPETELASPIHEAAKRGYVKCIESLAAHGANIDYNISHLGTPLYVACKNQQVACAKKLLESGVSVNQGKGLDSPLHVVARMSSVELVHLLMDFGANAQAKNADGKRPVDLVPLESPLIQIFLQNEGPQSLRQLCRLRIRKCFGIRQHHKISELLLPEDLKRFLLHL
Protein: NADPH-dependent 1-acyldihydroxyacetone phosphate reductase (ADR) (EC 1.1.1.101) (1-acyl DHAP reductase) (Acyl/alkyl DHAP reductase) (Acylglycerone-phosphate reductase) (Triacylglycerol lipase ayr1) (TAG lipase) (EC 3.1.1.3) (Q09851)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Can convert acyl and alkyl dihydroxyacetone-phosphate (DHAP) into glycerolipids and ether lipids, respectively. Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA). Also has triacylglycerol (TAG) lipase activity. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs. Lipolysis of TAG by AYR1 is essential for starvation-induced autophagy. Forms an NADPH-regulated cation-selective channel in the mitochondrial outer membrane.
Subcellular location: Lipid droplet {ECO:0000250|UniProtKB:P40471}. Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P40471}.
Interaction partners:
- Lysophospholipid acyltransferase
- Uncharacterized acyltransferase C1718.04
- Triacylglycerol lipase ptl3
- Uncharacterized acyltransferase C1851.02
- Putative lysophosphatidic acid:oleoyl-CoA acyltransferase
- Probable sterol O-acyltransferase 2
- Double-strand break repair protein rad32
- Diacylglycerol O-acyltransferase 1
- Phospholipid:diacylglycerol acyltransferase
- Succinate--CoA ligase subunit beta, mitochondrial
Sequence:
MEAEKFVLITGCSEGGIGNALALKFHQEGFQVLATARQVERMDNLTKAGLQTLKLDVTDEDSVREVEQEVRKFTNGSLHYLINNAGAPCSAPAIDLDIEDVSKVMDVNFYGVIRMNKAFQHQLIRAKGTIVNVNSLVSYVPFAFNAAYNASKAALLAYSNTLRIELAPFGVQVTSIMTGGVQTKIQSKPLGTMTEAAIPENSIYYPYRKLILENRNPVEKFVTIEEFADAAYPQLVGRGRWYQLFKPGVRPAQIWAGYMSSAGRVGSMLPVEVFSMSVRLIVKLPSTAVWRDHTVD
Protein: PAI-1 mRNA-binding protein variant (cDNA, FLJ92551, Homo sapiens PAI-1 mRNA-binding protein (PAI-RBP1), mRNA) (Q5VU21)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKNPLPPSVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGEGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDRPIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSGLKHEDKRGGSGSHNWGTVKDELTDLDQSNVTEETPEGEEHHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKKGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDPEAFPALA
Protein: Rifin (Q8IJ09)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHCYNILLFSFTLIILLLSSSQVNNQMNHYNRAHMKNIEPTKSYRSLCECELYTSMYDDDPEMKEIMHDFDRQTSQRFEEYNERMNKNRQKCKEQCNRDIKNIILKDKIEKELKQQLATLETDISTDDIPTCVCNKSVADKVEKTCLKCGGVLGGAVPELGLLCGYGAYELVKVAIGAAEKAAIAEGAKAGIAEGIRVAIKGIKGAFNIEFLDGKTLAEVITGKTFNNSTFFVEKFVQEYNTVCLSSTTYQDTLFCDYGSMFGGKVDNITAISLNAKNTAIKAGQAAAKMTTETTKALTAEKTGEVTSTSAIFSNPMVISFIVVVIIVIILLIIYLILRYRRKKKMKRKLQYIKLLE
Protein: Isoamylase 1, chloroplastic (AtISA1) (EC 3.2.1.68) (Protein REDUCED GRAVITROPIC 3) (O04196)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the trimming of pre-amylopectin chains. Accelerates the crystallization of nascent amylopectin molecules during starch synthesis. ISA1 and ISA2 work exclusively together as a multimeric holoenzyme. ISA1-ISA2 removes preferentially branches that are very close to other branches. Promotes negative gravitropic responses in shoots by facilitating starch granules (statoliths) formation in hypocotyls.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18431481}.
Interaction partners:
- Alpha-glucan phosphorylase 1
- Alpha-glucan phosphorylase 2, cytosolic
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- Alpha-amylase 3, chloroplastic
- Probable alpha-amylase 2
- Alpha-amylase 1
- 1,4-alpha-glucan-branching enzyme 2-2, chloroplastic/amyloplastic
- Isoamylase 2, chloroplastic
- 1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic
Sequence:
MDAIKCSSSFLHHTKLNTLFSNHTFPKISAPNFKPLFRPISISAKDRRSNEAENIAVVEKPLKSDRFFISDGLPSPFGPTVRDDGVNFSVYSTNSVSATICLISLSDLRQNKVTEEIQLDPSRNRTGHVWHVFLRGDFKDMLYGYRFDGKFSPEEGHYYDSSNILLDPYAKAIISRDEFGVLGPDDNCWPQMACMVPTREEEFDWEGDMHLKLPQKDLVIYEMHVRGFTRHESSKIEFPGTYQGVAEKLDHLKELGINCIELMPCHEFNELEYYSYNTILGDHRVNFWGYSTIGFFSPMIRYASASSNNFAGRAINEFKILVKEAHKRGIEVIMDVVLNHTAEGNEKGPIFSFRGVDNSVYYMLAPKGEFYNYSGCGNTFNCNHPVVRQFILDCLRYWVTEMHVDGFRFDLGSIMSRSSSLWDAANVYGADVEGDLLTTGTPISCPPVIDMISNDPILRGVKLIAEAWDAGGLYQVGMFPHWGIWSEWNGKFRDVVRQFIKGTDGFSGAFAECLCGSPNLYQGGRKPWHSINFICAHDGFTLADLVTYNNKNNLANGEENNDGENHNYSWNCGEEGDFASISVKRLRKRQMRNFFVSLMVSQGVPMIYMGDEYGHTKGGNNNTYCHDNYMNYFRWDKKEEAHSDFFRFCRILIKFRDECESLGLNDFPTAKRLQWHGLAPEIPNWSETSRFVAFSLVDSVKKEIYVAFNTSHLATLVSLPNRPGYRWEPFVDTSKPSPYDCITPDLPERETAMKQYRHFLDANVYPMLSYSSIILLLSPIKDP
Protein: Pre-mRNA-splicing factor SYF2 (CCNDBP1-interactor) (p29) (O95926)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as component of the spliceosome.
Subcellular location: Nucleus {ECO:0000269|PubMed:11118353, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
Interaction partners:
- Pre-mRNA-processing factor 19
- Pleiotropic regulator 1
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-processing factor 17
- Crooked neck-like protein 1
- U2 small nuclear ribonucleoprotein A'
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor RBM22
- Pre-mRNA-splicing factor SYF1
- SNW domain-containing protein 1
Sequence:
MAAIAASEVLVDSAEEGSLAAAAELAAQKREQRLRKFRELHLMRNEARKLNHQEVVEEDKRLKLPANWEAKKARLEWELKEEEKKKECAARGEDYEKVKLLEISAEDAERWERKKKRKNPDLGFSDYAAAQLRQYHRLTKQIKPDMETYERLREKHGEEFFPTSNSLLHGTHVPSTEEIDRMVIDLEKQIEKRDKYSRRRPYNDDADIDYINERNAKFNKKAERFYGKYTAEIKQNLERGTAV
Protein: Wee1-like protein kinase 2 (EC 2.7.10.2) (Wee1-like protein kinase 1B) (Wee1B kinase) (pWee1B) (pigWee1B) (A4PES0)
Organism: Sus scrofa (Pig)
Function: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:21123961}.
Interaction partners:
- Cell division cycle 2
- Serine/threonine-protein kinase CHK1
- Wee1-like protein kinase
- M-phase inducer phosphatase
- Double-strand-break repair protein rad21 homolog
- Serine/threonine-protein kinase Chk2
Sequence:
MGDNGDNKELKQKLNFSYSEEEQEDEGQKEAQESKKVQYHTPERCGHQDSEAKFTPPRTPLNHVCELSTPQVKDRASPDQGLRTPVSRPHTRPETPAPPDKSKPPPHCESPFTPRGHSSQSVISTGKLPSRGSKHLRLTPGPLTDEMTSLALVNINPFTPESYRRQFLKSNGKRKTRRDLEEAGPEEGKVEKGLPAKRCVLRETNMACRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSTKPVSGLSDENLAMHEVYAHSVLGHHPHVVRYYSSWAEDDHMMIQNEYCNGGSLQAAISENAKSGNHFQEPKLKDILLQISLGLKYIHNYGMVHMDIKPSNIFICHKIPSDSPVVPEEAENEADWFLSANVTYKIGDLGHVTSISEPQVEEGDSRFLAKEILQENYQHLPKADIFALGLTIAVAAGAEALPTNGTSWHHIREGQLPNIPQDLSKEFYNLLKDMIDPDPVARPSAAALTRSRVLCPSLGRTEELQQQLNLEKFKTATLERELKEVQRAQSSKEGQSSPGVTGTHTGSRSTRRLVGGKSAKSSSFTWGQSSP
Protein: Opacity protein opA55 (Q04878)
Organism: Neisseria gonorrhoeae
Function: Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation.
Subcellular location: Cell outer membrane.
Interaction partners:
Sequence:
AGEDHGRGPYVQADLAYAYEHITHDYPEQTGTKKDKISTVSDYFRNIRTHSIHPRVSVGYDFGGWRIAADYARYRKWNDNKYSVDIKELENKNQNKRDLKTENQENGTFHAVSSLGLSAVYDFKLNDKFKPYIGARVAYGHVRHSIDSTKKTTKFLTSSYGGLNPTVYTEENTQNAHHQSNSIRRVGLGVIAGVGFDITPKLTLDTGYRYHYWGRLENTRFKTHEASLGVRYRF
Protein: LP23332p (Rho guanine nucleotide exchange factor 3, isoform H) (Q9W0S0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKMSITGADSGRASATELEESAVATMQLREPTTPPPPISGEDVFASRVSHTTWYLPVEDSSSPPASSTNEARGASPDAEPREGDAAGDSSMSTSDEMPKPGSNEMGTTSDCAASLSQQIKAVSSPTLSEPCLEEQPQKGTESTDVANTGSSAGSGGLGVLQKFKRTLNNFNNKNQLHISPLSPAAVGNNAPKTKTSPTTTTASIAPMITTTTASDPGSEAGDTSSGKYRFGPLIWRSSKERRKTKYNRRDKCNSGDSGIQIELEQDEQYSRATMAVSRQDEPRAFALTNGSCGVALSKMRAIRRTNSAKASSILGPFIVKTKIAKHLNIGESDKAERKAPESLPTRSLSQPNGLESYGMGRPDLEDSDSDSVASNEEAISFYPTTYAEVLYNFTAGGPQELGLERGMLIEILRKEVGPWWFGRIKKEETNLVEDILGPELGWFPKEFVRIIHCPETDNFFIAHRAAADEAAAEEATARAEEGSVPVPVAAFAEDTDVTVTTDQSNVTLIVIESPPTPSAPSVDFVAQPDHSTIIRRSAVRELLDTEVNYVKLLAAICDGYLPAMSKRIDIFSPNSIRLIFSNITAIYKFQRKFLEALRRGIEQNQVAKVFLKMHKGFLCYSTYCNAYPRALIELETYDRVKDARTILENCRESQNLAELPLSAHLLAPVQRICRYPLHLNEIIKSALEKGAKEGNDTDGAKSAGKTTDYEQLDVTELDIPDSQDTVNLALEAMRGITEAVNEGKRHSETIARHQASFQNFKGPPLHLHSARFFLQVDATRQKQNLWNSSYTLFLFDNQLVYCKRDIIKRSHFIYKGRIFLDRCRVVNVRDGKMFGHTIKNSLRIYSESRDKWYDFSFRSANRKHRFLSTLALERQFGGKALYVSEMTGFEYNYEERPGDYSDQSDYDAQDFELATGVTSGESSLPESPAKSTSRLCETLPKKSQSRDGISSAENSQIVTTTSTGSLGRRHFGNWFRKPKSANCTPSQSPTHKPSFDADATLTEARVAAMELAEAAAALVPTDSSSA
Protein: Large ribosomal subunit protein uL23m (Q387G3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribosomal protein L30 ferredoxin-like fold domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Large ribosomal subunit protein mL46
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Large ribosomal subunit protein mL43
- LIM zinc-binding domain-containing protein
- 39S ribosomal protein L28
Sequence:
MVVSLRRFHSYANSSRGGATTCLITGGGKGHFALTVSTRGRFYRPLVDDGINLWRRRMGRIHKGWRTWEYQHTRPDPRPFPDPPVNDYFGRSRIWNPIACKLGYVRKKADEWGWPNKPPPPTGLRHSQEFFPFFFERYFPDAEVRLLLDSVLNNETKRPVFQIPCSMSKVELVNYLKNIYGIDNVVRVEVRNRRGRRYKNEVGEIKMMDDYKVAVVELDTPVSVELKQIKGTEDTSDNRPQERITQ
Protein: ATP synthase subunit 5, mitochondrial (ATP synthase chain 5) (Oligomycin sensitivity conferral protein) (OSCP) (P09457)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 synthesis 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(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit a
- ATP synthase subunit 4
- ATP synthase subunit g, mitochondrial
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit H
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit epsilon, mitochondrial
Sequence:
MFNRVFTRSFASSLRAAASKAAAPPPVRLFGVEGTYATALYQAAAKNSSIDAAFQSLQKVESTVKKNPKLGHLLLNPALSLKDRNSVIDAIVETHKNLDGYVVNLLKVLSENNRLGCFEKIASDFGVLNDAHNGLLKGTVTSAEPLDPKSFKRIEKALSASKLVGQGKSLKLENVVKPEIKGGLIVELGDKTVDLSISTKIQKLNKVLEDSI
Protein: DNA replication licensing factor MCM3 (EC 3.6.4.12) (X2JAI4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368061}.
Interaction partners:
Sequence:
MAHEGEQFIKDIQREYVDFLDDEEDQGIYAGHVKDMIAEKSKRLIVNVNDLKRKNPQRALGLLSNAADEQLAFGRALKEYASTVDPGYAKMHEDLFVGFEGCFGNRHVTPRSLTSIYLGNMVCVEGIVTKVSLIRPKVVRSVHYCPNTRKVMERKYTDLTSFEAVPSGAAYPTKDEDGNLLETEYGLSVYKDHQTLTIQEMPEKAPAGQLPRSVDIVCDDDLVDRCKPGDRVQIVGSYRCLPGKRGGYTSGTFRTVLLANNISLLSKESNLDISREDIMLCKKLAKNNDIFELLSKSLAPSIHGHAYVKQAILCLLLGGVEKILPNGTRLRGDINVLLIGDPSVAKSQLLRYVLNTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDIDRTAIHEVMEQGRVTISKAGIHASLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFVMLDVIDSDVDQMISDHVVRMHRYRNPKEADGEPLSMGSSYADSLSFVSSSEEKDTEVYEKYDALLHGKSRQRHEKILSVEFMRKYIHIAKCMKPKLGEQACEAIANEYSRLRSQEAVETDVARTQPITARTLETLIRLSTAHARARMSKSVTIDDAHAAIELVQFAYFKKVLDKDRPSKRRRNSGSDAEDDNGEASSQRSPSRRSKRTRTATVGADSDEEDIEPPQPDAGDLTRRETRRSLPARSVAMLMASPSSEEQSVATSTTEPAIISDARLGEFKNNLQRLFREAREQSLALARITTAINVGSQEPFTAGEIEAAVHRMTEDNQIMVADDIVFLI
Protein: Basic leucine zipper 8 (AtbZIP8) (bZIP protein 8) (Q9CA46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Floral homeotic protein APETALA 2
- Transcription factor HY5
- Basic leucine zipper 1
- B3 domain-containing transcription factor ABI3
- At5g04840
- Protein ABSCISIC ACID-INSENSITIVE 5
- ABSCISIC ACID-INSENSITIVE 5-like protein 7
- ABSCISIC ACID-INSENSITIVE 5-like protein 5
- ABSCISIC ACID-INSENSITIVE 5-like protein 6
- bZIP transcription factor 60
Sequence:
MAGSVYNLPSQNPNPQSLFQIFVDRVPLSNLPATSDDSSRTAEDNERKRRRKVSNRESARRSRMRKQRHMEELWSMLVQLINKNKSLVDELSQARECYEKVIEENMKLREENSKSRKMIGEIGLNRFLSVEADQIWTF
Protein: Polar localization protein TipN (A0A0H3C899)
Organism: Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus)
Interaction partners:
Sequence:
MKPKKRQPLDFSATPTEIPPEEPKTAPELPESASFVAPDAEPSFAEPLTLSDAAPDDLAVPTPTSVRSRRRREAETARFAEPDMKVANSLAATPQPPAPILEPSAPSAPPARSETREAALDLRGSVSASAASLEAEVVPRRMSGVLFWTLATAVAALWALAPIAFALGYARGVPAFKIEGFALMVFAGLAIGPALLTLLGAYMLRQANGISDELRRNRTLTDRLVTPAALAAAGATNAVDAMRQGVDEAAAAAERAREHIISLRKALAEETARLAEAAAESARMANQLAQGLSHERSAMETLSQSLDARSTAVVDAIGSQARMVAEASDLAETQLREAEAALAARAADLAAAAAEASDAARVGAEDLSRQIARLETAGVGVGDQVASVEKTLAAQRAALVEISQALRSEQEDFAAEAETRTAQLTEFVAYTRVGATELSDTAAMGAEILRGLISAAADQFREMADGAKSQRDTLAEEAKKTLETIGDVAENQRTLLEEELKAAMEAMAEAALKAGESVEARVEAARSRVDQLNEIAFAAGQKADAVFESRMEEARDIIEHSAQMVEQAGARTSQKLQDSVQTARSTLDELEVMLAEIGRRTADLPAEALQKAGEVRIAIEQGVEHLMNAVRRTAEETAAIDQAFQERVRRNYEMLSEAAGAVTASGISTVAARATPAAPPPSRSRAAPPPSALPTVEFDDEDEPPSDRRRLRLTPTATDQEFRSVFEQASARKQTGTPPTEAEADGNWSWRGLLSGIESSSPGDAGLGEKLAAEITAMGIDPHALLPRGRIDEIAAALQTRDGEGAREVVKRLAPAAIRRLVRRLFSDATLKGNTERFLKRYAGMIDEAAGQDREGFLLAALLSSDAGRAYLLLDAASGDLA