wanglab/gogpt-training-data huggingface dataset:
Protein: Myosin-4 (Myosin heavy chain 2b) (MyHC-2b) (Myosin heavy chain 4) (Myosin heavy chain IIb) (MyHC-IIb) (Myosin heavy chain, skeletal muscle, fetal) (Q9Y623)
Organism: Homo sapiens (Human)
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin-3
- Myosin regulatory light chain 11
- Myosin light chain 3
- Myosin-8
- Myosin-1
- Myosin-7
- Myosin regulatory light polypeptide 9
- Myosin light chain 6B
- Myosin-13
Sequence:
MSSDSEMAIFGEAAPFLRKSEKERIEAQNKPFDAKTSVFVVDPKESYVKAIVQSREGGKVTAKTEAGATVTVKEDQVFSMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEPASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKSLCYPRVKVGNEFVTKGQTVQQVYNAVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLAFLFSGAQTAEAEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIEIDHTQYKFGHTKVFFKAGLLGTLEEMRDEKLAQLITRTQAICRGFLMRVEFRKMMERRESIFCIQYNIRAFMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADALADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQMEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLCMDLERAKRKLEGDLKLAQESTMDTENDKQQLNEKLKKKEFEMSNLQGKIEDEQALAIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEESTLQHEATAAALRKKHADSVAELGEQIDSLQRVKQKLEKEKSELKMEINDLASNMETVSKAKANFEKMCRTLEDQLSEIKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEETKAKSTLAHALQSARHDCDLLREQYEEEQEAKAELQRGMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACIALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKVKKQLDHEKSELQTSLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEELDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEALRNLRNTQGILKDTQLHLDDAIRGQDDLKEQLAMVERRANLMQAEVEELRASLERTERGRKMAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELESEVESEQKHNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKLQHELEEAKERADIAESQVNKLRVKSREVHTKVISEE
Protein: Spindlin-2B (Q5JZB8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKTPNAQEAEGQQTRAAAGRATGSANMTKKKVSQKKQRGRPSSQPRRNIVGCRISHGWKEGDEPITQWKGTVLDQVPINPSLYLVKYDGIDCVYGLELHRDERVLSLKILSDRVASSHISDANLANTIIGKAVEHMFEGEHGSKDEWRGMVLAQAPIMKAWFYITYEKDPVLYMYQLLDDYKEGDLRIMPESSESPPTEREPGGVVDGLIGKHVEYTKEDGSKRIGMVIHQVEAKPSVYFIKFDDDF
Protein: ABC transporter G family member 33 (ABC transporter ABCG.33) (AtABCG33) (Pleiotropic drug resistance protein 5) (Q9ZUT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a general defense protein.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Auxin efflux carrier component 3
- Auxin efflux carrier component 2
- Auxin efflux carrier component 7
Sequence:
MGSSFRSSSSRNEHEDGGDEAEHALQWAEIQRLPTFKRLRSSLVDKYGEGTEKGKKVVDVTKLGAMERHLMIEKLIKHIENDNLKLLKKIRRRMERVGVEFPSIEVRYEHLGVEAACEVVEGKALPTLWNSLKHVFLDLLKLSGVRTNEANIKILTDVSGIISPGRLTLLLGPPGCGKTTLLKALSGNLENNLKCYGEISYNGHGLNEVVPQKTSAYISQHDLHIAEMTTRETIDFSARCQGVGSRTDIMMEVSKREKDGGIIPDPEIDAYMKAISVKGLKRSLQTDYILKILGLDICAETLVGNAMKRGISGGQKKRLTTAEMIVGPTKALFMDEITNGLDSSTAFQIIKSLQQVAHITNATVFVSLLQPAPESYDLFDDIVLMAEGKIVYHGPRDDVLKFFEECGFQCPERKGVADFLQEVISKKDQGQYWLHQNLPHSFVSVDTLSKRFKDLEIGRKIEEALSKPYDISKTHKDALSFNVYSLPKWELFRACISREFLLMKRNYFVYLFKTFQLVLAAIITMTVFIRTRMDIDIIHGNSYMSCLFFATVVLLVDGIPELSMTVQRLSVFYKQKQLCFYPAWAYAIPATVLKIPLSFFESLVWTCLTYYVIGYTPEPYRFFRQFMILFAVHFTSISMFRCIAAIFQTGVAAMTAGSFVMLITFVFAGFAIPYTDMPGWLKWGFWVNPISYAEIGLSVNEFLAPRWQKMQPTNVTLGRTILESRGLNYDDYMYWVSLSALLGLTIIFNTIFTLALSFLKSPTSSRPMISQDKLSELQGTKDSSVKKNKPLDSSIKTNEDPGKMILPFKPLTITFQDLNYYVDVPVEMKGQGYNEKKLQLLSEITGAFRPGVLTALMGISGAGKTTLLDVLAGRKTSGYIEGEIRISGFLKVQETFARVSGYCEQTDIHSPSITVEESLIYSAWLRLVPEINPQTKIRFVKQVLETIELEEIKDALVGVAGVSGLSTEQRKRLTVAVELVANPSIIFMDEPTTGLDARAAAIVMRAVKNVAETGRTIVCTIHQPSIHIFEAFDELVLLKRGGRMIYSGPLGQHSSCVIEYFQNIPGVAKIRDKYNPATWMLEVTSESVETELDMDFAKIYNESDLYKNNSELVKELSKPDHGSSDLHFKRTFAQNWWEQFKSCLWKMSLSYWRSPSYNLMRIGHTFISSFIFGLLFWNQGKKIDTQQNLFTVLGAIYGLVLFVGINNCTSALQYFETERNVMYRERFAGMYSAFAYALAQVVTEIPYIFIQSAEFVIVIYPMIGFYASFSKVFWSLYAMFCNLLCFNYLAMFLISITPNFMVAAILQSLFFTTFNIFAGFLIPKPQIPKWWVWFYYITPTSWTLNLFFSSQYGDIHQKINAFGETKTVASFLEDYFGFHHDRLMITAIILIAFPIALATMYAFFVAKLNFQKR
Protein: Phytoene synthase 3, chloroplastic (ZmPSY3) (EC 2.5.1.32) (B0KZ40)
Organism: Zea mays (Maize)
Function: Catalyzes the conversion of geranylgeranyl diphosphate to phytoene. Mediates the first committed step in carotenoid biosynthesis. May play a role in regulating carotenoid flux in response to abiotic stress in roots. May control flux to carotenoid precursors that are required for abiotic stress-induced abscisic acid (ABA) formation in roots.
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:23023170}.
Interaction partners:
- Phytoene dehydrogenase
- Geranylgeranyl pyrophosphate synthase1
- Geranylgeranyl pyrophosphate synthase2
- Geranylgeranyl pyrophosphate synthase3
- prolycopene isomerase
- Geranylgeranyl pyrophosphate synthase4
- Heterodimeric geranylgeranyl pyrophosphate synthase small subunit chloroplastic
- all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]
- all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]
- Solanesyl diphosphate synthase 2 chloroplastic
Sequence:
MMSTSRAVKSPACAARRRQWSADAPNRTATFLACRHGRRLGGGGGAPCSVRAEGSNTIGCLEAEAWGGAPALPGLRVAAPSPGDAFVVPSEQRVHEVVLRQAALAAAAPRTARIEPVPLDGGLKAAFHRCGEVCREYAKTFYLATQLMTPERRMAIWAIYVWCRRTDELVDGPNASHISALALDRWESRLEDIFAGRPYDMLDAALSDTVARFPVDIQPFRDMIEGMRMDLKKSRYRSFDELYLYCYYVAGTVGLMSVPVMGISPASRAATETVYKGALALGLANQLTNILRDVGEDARRGRIYLPQDELEMAGLSDADVLDGRVTDEWRGFMRGQIARARAFFRQAEEGATELNQESRWPVWSSLLLYRQILDEIEANDYDNFTRRAYVPKTKKLMALPKAYLRSLVVPSSSSQAESRRRYSTLT
Protein: Basal cell adhesion molecule (B-CAM cell surface glycoprotein) (Lutheran antigen) (CD antigen CD239) (Q9R069)
Organism: Mus musculus (Mouse)
Function: Laminin alpha-5 receptor. May mediate intracellular signaling (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P50895}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P50895}.
Interaction partners:
- Laminin subunit alpha-5
Sequence:
MEPPDARAGLLWLTFLLSGYSGAQAELHVSVPPRVEVMRGEQVALDCTPREHPEHYVLEWFLVDGTGARHRLASVEPQGSEFLGTVHSLGRVPPYEVDSRGRLVIAKVQVGDGRDYVCVVKAGAAGTSEATSSVRVFATPEDTEVSPNKGTLSVMDQFAQEIATCSSNNGNPVPRITWYRNGQRLEVPMEVNQKGYITIRTVREASGLYSLTSTLYLRLHKDDRDANFHCAAHYDLPSGQHGRLDSHTFRLTLHYPTEHVEFWVGSPSTTEGWVREGDAVQLLCQGDGSPSPEYSFFRQQGTQEEQLNVNLKGNLTLERVHRNQSGIYGCRVEDYDADEEVQLVKKLKLHVAYLDPLELSVPEELFVFLNSSSTVVNCSARGLPTPTVRWTKDSVTLADGPMLSLQSVTFDSAGTYTCEASTPTVPLLSRTQSFQLIVQGAPELKPNEIMPKSGNSWTEGDEVMLTCSARGFPEPKLTWSQRGDTPAEPPFEGRGWKSSSLMVKVTSALSREGVSCEASNIHGKKGHVFHFGSVAPQTAQAGVAVMAVAVSVGLLLLVVAAFYCMRRKGRPGCCRRAEKGAPPAREPELSHSGSERPEHTGLLMGGPSGGGRGGSGGFGDEC
Protein: Olfactomedin 1a (A2AWU3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MQPANKLLSLTLLVLMGTELTQVLPANPEESWQVYSSAQDSEGRCVCTVVAPQQTMCSRDARTKQLRQLLEKVQNMTQSIQNLDQRTQKDLQYVQRMEVQLRGLETKFKQVEESHKQNIAKQYKAIKAKMEELRPMIPVLEEYKADAKLVMQFKEEVKNLTSVLSELQEEIGAFDYEELHNRVSNLEERLRACMQKLACGKLTGISDAITIKTSGSRYGSWMTDPLAPDGDTRVWYMDGYHNNRFVREYKSMADFMYSDNFTSHRLPHPWSGTGQVVYNGSIYFNKFQSNTIIKFDFKTATISKSGQLDYAGFNNRYHYSWGGHSDIDLMVDEGGLWAIYATNQNAGNIVISKLNPATLQIVKSYTTNHPKRSAGEAFMICGTLYVTNGYSGGTKVYYAFHTNSSTYEYIDIPLQNKYSHISMLDYNPRDRALYAWNNGHQVLYNVTLFHVIRSEEL
Protein: NAD-dependent protein deacetylase hst1 (EC 2.3.1.286) (Homologous to SIR2 protein 1) (Regulatory protein SIR2 homolog 1) (C8V3W5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: NAD-dependent histone deacetylase, which could function in telomeric silencing, cell cycle progression and chromosome stability.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Ribosomal RNA-processing protein 8
- HSF-type DNA-binding domain-containing protein
- Transcriptional co-activator
- Tyrosine-protein phosphatase cdcA
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- Histone H4.2
- Histone H4.1
- histone deacetylase
- Histone H3
Sequence:
MDLASAPRGESPPLKAPLVEIEAAEVERSLPQENAAPEEKGSNSQSEYESDSDALDDEWETQSLYEDAIQMIRDDQLRDGTIPGACTLEEAIEFRKRLHEVGKAQFVEETIARDTVTAKKLCTAFGILPPSFLEGAPDEAYHPLLAIAISREFARRQKLPQYNSVDDAVKLLKESKNIIVLTGAGISTSLGIPDFRSKDTGLYSKLENLGLNDPQEVFDIRIFREDPGIFYSIAKDILPTEKKFSPTHGFIRLLQDKGKLLTNYTQNIDNIEANAGVFPENIVQCHGSFATATCVKCQYKVAGDEIYDDIKKGLIPECAQCRKRIAEDSQKPQGQKRKRNSTSAHKDRSKSGEDSSDGEDYEIPTPGVMKPDITFFGEDLPDEFGRRLLHHDRDKVDLVIVIGTSLKVAPVAEVPGVLPPHIPQIYISRTPVAHTNFDIDLLGDCDVVVSELCRRAGWELKHEMISPDEKVDVTPVFGYGSRHVFKVSG
Protein: Aminoglycoside N(6')-acetyltransferase type 1 (EC 2.3.1.82) (AAC(6')-Ih) (Aminoglycoside resistance protein) (Q43899)
Organism: Acinetobacter baumannii
Function: Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin, kanamycin, tobramycin and netilmicin.
Interaction partners:
Sequence:
MNIMPISESQLSDWLALRCLLWPDHEDVHLQEMRQLITQAHRLQLLAYTDTQQAIAMLEASIRYEYVNGTQTSPVAFLEGIFVLPEYRRSGIATGLVQQVEIWAKQFACTEFASDAALDNQISHAMHQALGFHETERVVYFKKNIG
Protein: Stomatin like 3 (D4A100)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDIHRKRERDTNTHIQIRLGVCGWILFFLSFLLMLITFPVSIWMCLKIIKEYERAVVFRLGRIQADKAKGPGTAETMGTTTTTTTTTTTTTTTTTISTTTTTRGIY
Protein: Aquaporin-10b (Q1L8T0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Aquaporin 1a
- Aqp8a protein
- Aquaporin-8bb
- Aquaporin-0a
- Aquaporin
- Aquaporin 1a
- HCLS1-associated protein X-1
- Aquaporin
- Uncharacterized protein.
- Aquaporin 9b
Sequence:
MFGGVFWSLCFNTVRVWISGSGHHLSEYQGRVPVNQPGLRTGNHIWHLHCKRSVRFSWTRLPFYVCSQLFGAFLAAATVALQYYDAIMDFTGGHLTVSGATATAGIFSTYPADYLSLWGGVVDQIIGTAALLVCVLALGDAHNTPAPAGLEPVLVGAAVLVIGISMGSNSGYAINPARDFGPRLFSYIAGWGDEVFRAGHGWWWVPIIVTCVGALLGSLLYELLIGVHHPDSEAVDHEDPTAALQQTVEMEGAQSFDTIKENKKSGIFSITSADVG
Protein: Proline dehydrogenase (EC 1.5.5.2) (E7EQL6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKMTFYGHFVAGEDQESIQPLLRHYRAFGVSAILDYGVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQYQAHWAFGDRRNGVISARTYFYANEAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGRPQFLLQFSEVLAKWRCFFHQMAVEQGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDWFTAETLGVSGTMDLLDWSSLIDSRTKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRMLQRMDVLAKKATEMGVRLMVDAEQTYFQPAISRLTLEMQRKFNVEKPLIFNTYQCYLKDAYDNVTLDVELARREGWCFGAKLVRGAYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDYVLEELKHNAKAKVMVASHNEDTVRFALRRMEELGLHPADHRVYFGQLLGMCDQISFPLGQAGYPVYKYVPYGPVMEVLPYLSRRALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA
Protein: D-aspartate oxidase (DASOX) (DASPO) (DDO) (EC 1.4.3.1) (Q922Z0)
Organism: Mus musculus (Mouse)
Function: Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.
Subcellular location: Peroxisome matrix {ECO:0000250|UniProtKB:Q99489}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99489}. Note=Active in the peroxisomal matrix. {ECO:0000250|UniProtKB:Q99489}.
Interaction partners:
- Putative aspartate aminotransferase, cytoplasmic 2
- Aspartate aminotransferase, cytoplasmic
- Omega-amidase NIT2
- L-amino-acid oxidase
- Aspartate aminotransferase, mitochondrial
- Amine oxidase
- Amine oxidase
- Citrate synthase, mitochondrial
- Citrate synthase
- Pyruvate carboxylase, mitochondrial
Sequence:
MDTVCIAVVGAGVIGLSTAACISQLVPGCTVTVISDRFTPDTTSNVAAGMLIPHTCADTPVPTQKRWFRETFEHLSEIAKSAEAADAGVHLVSGWQIFRSVPAEEVPFWADVVLGFRKMTEAELKRFPQYVFGQAFTTLKCETSAYLPWLERRIKGSGGLLLTRRIEDLWELQPSFDIVVNCSGLGSRRLVGDPMISPVRGQVLQARAPWVKHFIRDGGGLTYVYPGMSYVTLGGTRQKGDWNRSPDAELSREIFSRCCTLEPSLHRAYDIKEKVGLRPSRPGVRLQKEILVRGQQTLPVVHNYGHGSGGISVHWGSALEATRLVMECIHTLRTPASLSKL
Protein: UDP-glucose:(Heptosyl) LPS alpha 1,3-glucosyltransferase WaaG (Q9HUF6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Lipopolysaccharide core heptose
- Lipopolysaccharide heptosyltransferase 1
- lipopolysaccharide heptosyltransferase II
- Heptose kinase
- Lipopolysaccharide kinase
- Serine/threonine protein kinase
- 3-deoxy-D-manno-octulosonic acid transferase
- Probable carbamoyl transferase
- Probable glycosyl transferase
- InaA protein
Sequence:
MTLAFILYKYFPFGGLQRDFMRIALECQRRGHDIRVYTLIWEGDVPDGFEVLVAPVRSIFNHRRNEKFTAWVRADLDRRPVQRVIGFNKMPGLDVYYAADACFEEKAQTLRNPLYRQWGRYRHFAGYERAVFDPASKTEILMISEVQQPLFVKHYGTQAERFHLLPPGISQDRRAPANAADVRAEFRREFGLEEDDLLLVQIGSGFKTKGLDRSLKALSALPKALRRRTRLIAIGQDDPKPFLLQIAALGLNDQVQILKGRSDIPRFLLGADLLIHPAYNENTGTVLLEALVSGLPVLVTDVCGYAHYIAEADAGRVLPSPFEQDSLNRLLAEMLEDAPARAAWSRNGLAYADHADLYSMPQRAADLILGEAS
Protein: Portal protein (Capsid protein pb7) (Q6QGD5)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Forms the portal vertex of the capsid and plays a role in governing correct capsid geometry. This portal plays critical roles in capsid assembly, genome packaging, head completion protein attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (By similarity). Binds to the terminase subunits to form the packaging machine (By similarity).
Subcellular location: Virion {ECO:0000269|PubMed:24198424}. Note=Forms the portal complex located at one vertex of the capsid. {ECO:0000269|PubMed:24198424}.
Interaction partners:
Sequence:
MGFKSWITEKLNPGQRIIRDMEPVSHRTNRKPFTTGQAYSKIEILNRTANMVIDSAAECSYTVGDKYNIVTYANGVKTKTLDTLLNVRPNPFMDISTFRRLVVTDLLFEGCAYIYWDGTSLYHVPAALMQVEADANKFIKKFIFNNQINYRVDEIIFIKDNSYVCGTNSQISGQSRVATVIDSLEKRSKMLNFKEKFLDNGTVIGLILETDEILNKKLRERKQEELQLDYNPSTGQSSVLILDGGMKAKPYSQISSFKDLDFKEDIEGFNKSICLAFGVPQVLLDGGNNANIRPNIELFYYMTIIPMLNKLTSSLTFFFGYKITPNTKEVAALTPDKEAEAKHLTSLVNNGIITGNEARSELNLEPLDDEQMNKIRIPANVAGSATGVSGQEGGRPKGSTEGD
Protein: HCG2044777 (PMF1-BGLAP readthrough) (U3KQ54)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAEASSANLGSGCEEKRHEGSSSESVPPGTTISRVKLLDTMVDTFLQKLVAAGSYQRFTDCYKCFYQLQPAMTQQIYDKFIAQLQTSIREEISDIKEEGNLEAVLNALDKIVEEGKVRKEPAWRPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLADAVLAGRRQVEELQLQVQAQQQAWQVRSPAVQSPAKVQPLCPSRRAAR
Protein: Uncharacterized fimbrial-like protein YehD (P33343)
Organism: Escherichia coli (strain K12)
Function: Part of the yehABCD fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches.
Interaction partners:
- Probable fimbrial chaperone YehC
- Outer membrane usher protein YehB
- Uncharacterized fimbrial-like protein YehA
- Uncharacterized fimbrial-like protein YdeS
Sequence:
MKRSIIAAAVFSSFFMSAGVFAADVDTGTLTIKGNIAESPCKFEAGGDSVSINMPTVPTSVFEGKAKYSTYDDAVGVTSSMLKISCPKEVAGVKLSLITNDKITGNDKAIASSNDTVGYYLYLGDNSDVLDVSAPFNIESYKTAEGQYAIPFKAKYLKLTDNSVQSGDVLSSLVMRVAQD
Protein: Cullin-5 (CUL-5) (Q9D5V5)
Organism: Mus musculus (Mouse)
Function: Core component of multiple SCF-like ECS (Elongin-Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. ECS(SOCS1) seems to direct ubiquitination of JAK2. ECS(KLHDC1) complex is part of the DesCEND (destruction via C-end degrons) pathway and mediates ubiquitination and degradation of truncated SELENOS selenoprotein produced by failed UGA/Sec decoding, which ends with a glycine. As part of a multisubunit complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A. May form a cell surface vasopressin receptor (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q93034}. Note=Localizes to sites of DNA damage in a UBAP2 and UBAP2L-dependent manner. {ECO:0000250|UniProtKB:Q93034}.
Interaction partners:
- E3 ubiquitin-protein ligase RBX1
- Elongin-C
- RING-box protein 2
- Elongin-B
- Core-binding factor subunit beta
- Cytokine-inducible SH2-containing protein
- E3 ubiquitin-protein ligase ARIH2
- Ubiquitin-like protein NEDD8
- Suppressor of cytokine signaling 2
- Suppressor of cytokine signaling 1
Sequence:
MATSNLLKNKGSLQFEDKWDFMHPIVLKLLRQESVTKQQWFDLFSDVHAVCLWDDKGSSKIHQALKEDILEFIKQAQARVLSHQDDTALLKAYIVEWRKFFTQCDILPKPFCQLEVTLLGKQSSNKKSNMEDSIVRKLMLDTWNESIFSNIKNRLQDSAMKLVHAERLGEAFDSQLVIGVRESYVNLCSNPEDKLQIYRDNFEKAYLDSTERFYRTQAPSYLQQNGVQNYMKYADAKLKEEEKRALRYLETRRECNSVEALMECCVNALVTSFKETILAECQGMIKRNETEKLHLMFSLMDKVPNGIEPMLKDLEEHIISAGLADMVAAAETITTDSEKYVEQLLTLFNRFSKLVKEAFQDDPRFLTARDKAYKAVVNDATIFKLELPLKQKGVGLKTQPESKCPELLANYCDMLLRKTPLSKKLTSEEIEAKLKEVLLVLKYVQNKDVFMRYHKAHLTRRLILDISADSEIEENMVEWLREVGMPADYVNKLARMFQDIKVSEDLNQAFKEMHKNNKLALPADSVNIKILNAGAWSRSSEKVFVSLPTELEDLIPEVEEFYKKNHSGRKLHWHHLMSNGIITFKNEVGQYDLEVTTFQLAVLFAWNQRPREKISFENLKLATELPDAELRRTLWSLVAFPKLKRQVLLYDPQVNSPKDFTEGTLFSVNQDFSLIKNAKVQKRGKINLIGRLQLTTERMREEENEGIVQLRILRTQEAIIQIMKMRKKISNAQLQTELVEILKNMFLPQKKMIKEQMEWLIEHRYIRRDEADINTFIYMA
Protein: Ovocleidin-17 (V5NUE7)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MAPTWALLGCVLLLPSLRGDPDGCGPGWVPTPGGCLGFFSRELSWSRAESFCRRWGPGSHLAAVRSAAELRLLAELLNASRGGDGSGEGADGRVWIGLHRPAGSRSWRWSDGTAPRFASWHRTAKARRGGRCAALRDEEAFTSWAARPCTERNAFVCKAAA
Protein: SPOC domain-containing protein 1 (B1ASB6)
Organism: Mus musculus (Mouse)
Function: Essential excecutor of PIWIL4-piRNA pathway directed transposon DNA methylation and silencing in the male embryonic germ cells. Associates with the de novo DNA methylation machinery and repressive chromatin remodeling complexes. Tethering of PIWIL4 to a nascent transposable element transcript recruits repressive chromatin remodeling activities and the de novo methylation apparatus through SPOCD1. Not required for piRNA biosynthesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:32674113}. Chromosome {ECO:0000269|PubMed:32674113, ECO:0000269|PubMed:39294378}.
Interaction partners:
- DNA
- Zinc finger with KRAB and SCAN domains 2
Sequence:
MPVDKFLARAGGQRTLSRFQDSLCDFLATGSSRSLCGTSLDFPDRVLVCTEGPAGMEEASSPSFRQATTVEGMVSPEDPTLSKEGLSAKGPPPSPVLPPFRRKCRKCGICPQEEEKSGFSLRFGQRPDGDPPECASPEAFAGPPRLLSSKDTEPGEPGGSWVECAVETEVENMLFSKDGVAPDSLDHLFEFPGLFGGEPLSLVTQEPLQSPALYPEVLTEDSTDQQEVQPAFVVGSPGTPPDPVGPEDKAQSGSRMELEQGLSAPANSCASSPEPLGGLDGAPLEQRRPTHVKKRPWTSPDDSSQDHAEGASKKDFPRLEARVPRGVKTVYYVYTGSGIRLVGAASSSQPGQIEPLEELDTNSARRKRRPTTAHPTPCQSDPSETENAEPHQQRAEDPGEQGMTPLDAGVRSTVVRAMQEVLWTRAQELPDLALREDEVEAIAEGIEEALFHLTQDTNLRYKNKYRSLLFNLRDPRNVDLFLKVAHCDVTPNNLVQMSSIQLAPKELSRWRDQEERKGLDIIEQQQKELYRLPASKLTHKGEVEIPRDLDQMLTLEDLMEPIVPRECSLQPLSTPLEDTTNWHQHHQCDSNCQICTGGEEGRKADDGSQPELQVDISYNVDRKSSTKLPAFSGVIMNREENAIQKAPGPAPASSPEVLKVGETPPKEPQDRLQMPAGLKNAPPSPPPWEGSLDMFSIKHFRAKAQLISGHSCQLVQALPDVIRSAGRLPPSHVWDLLDSMGPSKAKDICVIRLCPHGSRDIQNYRLLYSYLNNKQCHCLATVQQVKMVLLPLPAFEPLPARLRPLGGPGLEITHTSLLLAVLFPKDALPDTATSIPVSNKVPKTVSFSKRVERILYSPEDRRSEATSSPLEEDPKQSLARGSLAPRSVCAPQSFPRGRGRQGPGWGQWSPEAAWCYSQHPSSAGPVFPGIGQGQHLHRASCFHHDLLQHLKVLVTMSHQFQASLWPQSQDSLPPSTVVSAVPDPPGPSLGPMDGGGSNCPPPEGSDPLEPPEHEC
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (Q7KVM5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- FI19335p1
- LD24014p
- WD repeat-containing protein 82
- Cleavage and polyadenylation specificity factor 73
- Cleavage and polyadenylation specificity factor subunit 1
- Probable cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 4
- Factor interacting with poly
- EF-hand domain-containing protein
Sequence:
MMKKLLSNGSNKNKTLKFDEGINLDQIIAKLKLIGEIGSVVQISVREIEAVCSRAREVLLKQPTLLEIPAPINLLGDIHGQYLNLLRYFESNGYPPDSVYLLLGDYVDRGKQSIETLTLLLALKARYPTKFYLLRGNHECSSINHFYGFYDECKRRYTVKLWRTFVDCYNCLPLAAIIEENIFCCHGGLSPHLFSMQQIREIRRPIEIPESGLICDILWSDPDLRIMGWGPNERGVSHTFGSDVVSAFLHRFKLNLICRGHQVVEDGYEFFAKRQLITIFSAPNYCGEFDNAGAMMCINQDLLCTFRVQRPILSEQRRLSDISV
Protein: CREB regulated transcription coactivator 1 (M0QXN6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLPFQTPFQSSGLDTSRTTRHHGLVDRVYRERGRLGSPHRRPLSVDKHGRQADSCPYGTMYLSPPADTSWRRTNSDSALHQSTMTPTQPESFSSGSQDVHQKRVLLLTVPGMEETTSEADKNLSKQAWDTKKTGSRPKSCEVPGINIFPSADQENTTALIPATHNTGGSLPDLTNIHFPSPLPTPLDPEEPTFPALSSSSSTGNLAANLTHLGIGGAGQGMSTPGSSPQHRPAGVSPLSLSTEARRQQASPTLSPLSPITQLEQFNMMENAISSSSLYSPGSTLNYSQAAMMGLTGSHGSLPDSQQLGYASHSGIPNIILTVTGESPPSLSKELTSSLAGVGDVSFDSDSQFPLDELKIDPLTLDGLHMLNDPDMVLADPATEDTFRMDRL
Protein: Histone H3-like centromeric protein cpar-1 (CENP-A-related protein 1) (Centromeric protein A related) (P34440)
Organism: Caenorhabditis elegans
Function: Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Not required for chromosome segregation during meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16273096}. Chromosome {ECO:0000269|PubMed:16273096, ECO:0000269|PubMed:25919583}. Note=Localizes to chromosomes during meiotic prometaphase I and metaphase I (PubMed:16273096, PubMed:25919583). Upon cleavage at the onset of anaphase I, the C-terminus remains localized to chromosomes (PubMed:25919583). The cleaved form transiently associates with chromosome but not centromeres during embryonic mitosis (PubMed:25919583). {ECO:0000269|PubMed:16273096, ECO:0000269|PubMed:25919583}.
Interaction partners:
- Separin homolog sep-1
- JmjC domain-containing protein
- Nucleosome-remodeling factor subunit NURF301-like
- separase
- Histone H2A/H2B/H3 domain-containing protein
- AT hook Transcription Factor family
- Exonuclease domain-containing protein
Sequence:
MADDGPIIEEIAEKNGRVARIMQRLQHDTQRVTSVPGFNTSATGYADLIALLDQYKNDLEAVGFNDLEQARRRAPSVDITVGSNSTNLVDYSHGRHDMPSHRRHDSSDEEITAANSHHQSPINVGNRNDTDGTNGRNGSRAGSSSSDRVRMIAGRNRISKTRRYRPGQKALEEIRKYQESEDLLIPKAPFARLVREIMQTSTPFSSDLRIRSDAINALQEASEALLVQMFDGSSLISAHSKRATLTTTDVQLYRRLCLPNL
Protein: Meiotic recombination protein SPO11 (EC 5.6.2.2) (Q9WTK8)
Organism: Mus musculus (Mouse)
Function: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with TOP6BL, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles. Essential for the phosphorylation of SMC3, HORMAD1 and HORMAD2.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Type 2 DNA topoisomerase 6 subunit B-like
- Meiotic recombination protein DMC1/LIM15 homolog
- HORMA domain-containing protein 1
- MutS protein homolog 4
- Meiotic recombination protein REC8 homolog
- Structure-specific endonuclease subunit MUS81
- Histone-lysine N-methyltransferase PRDM9
- Superkiller complex protein 8
- Meiotic recombination protein REC114
- HORMA domain-containing protein 2
Sequence:
MAFAPMGPEASFFDALDRHRASLLAMVKRGAGETPAGATRVASSSEVLTAIENIIQDIIKSLARNEVPAFTIDNRSSWENIMFDDSVGLRMIPQCTTRKIRSDSPKSVKKFALILKVLSMIYKLIQSDTYATKRDIYYTDSQLFGNQAAVDSAIDDISCMLKVPRRSLHVLSTSKGLIAGNLRYMEEDGTRVQCTCSATATAVPTNIQGMQHLITDAKFLLIVEKDATFQRLLDDNFCSRMSPCIMVTGKGVPDLNTRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQRLNIPKDSLIPLTKHDQMKLDSILKRPYITYQPLWKKELEMMADSKMKAEIQALTLLSSDYLSRVYLPNKLRFGGWI