wanglab/gogpt-training-data huggingface dataset:
Protein: Sperm-associated antigen 8 (HSD-1) (Sperm membrane protein 1) (SMP-1) (Sperm membrane protein BS-84) (Q99932)
Organism: Homo sapiens (Human)
Function: Plays a role in spermatogenesis by enhancing the binding of CREM isoform tau to its coactivator FHL5 and increasing the FHL5-regulated transcriptional activation of CREM isoform tau (By similarity). Involved in the acrosome reaction and in binding of sperm to the zona pellucida (By similarity). Plays a role in regulation of the cell cycle by controlling progression through the G2/M phase, possibly by delaying the activation of CDK1 which is required for entry into mitosis. May play a role in fertility and microtubule formation through interaction with RANBP9.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q3V0Q6}. Nucleus {ECO:0000250|UniProtKB:Q3V0Q6}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15014887, ECO:0000269|PubMed:17187156, ECO:0000269|PubMed:8788182}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:19548270}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19548270}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q3V0Q6}. Note=In mature sperm cells, detected in the acrosomal region of the head and in the middle piece of the tail (By similarity). Localized to the nucleus and cytoplasm of spermatocytes and round spermatids while, in elongating spermatids, expressed in the cytoplasm but not in the nucleus (By similarity). During the cell cycle, localized on the microtubule-organizing center (MTOC) during prophase. In metaphase, extends along spindle microtubules. In anaphase, detected on the astral microtubules and mid-zone. In telophase, remains at the mid-zone. After cytokinesis, returns to the MTOC (PubMed:19548270). Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme (By similarity). {ECO:0000250|UniProtKB:E1BNS6, ECO:0000250|UniProtKB:Q3V0Q6, ECO:0000269|PubMed:19548270}.
Interaction partners:
- Tektin-3
- Protein Flattop
- Cilia- and flagella-associated protein 53
- Cilia- and flagella-associated protein 52
- Parkin coregulated gene protein
- EF-hand domain-containing family member C2
- Tektin-2
- EF-hand domain-containing protein 1
- Tektin-1
- Tektin-4
Sequence:
METNESTEGSRSRSRSLDIQPSSEGLGPTSEPFPSSDDSPRSALAAATAAAAAAASAAAATAAFTTAKAAALSTKTPAPCSEFMEPSSDPSLLGEPCAGPGFTHNIAHGSLGFEPVYVSCIAQDTCTTTDHSSNPGPVPGSSSGPVLGSSSGAGHGSGSGSGPGCGSVPGSGSGPGPGSGPGSGPGHGSGSHPGPASGPGPDTGPDSELSPCIPPGFRNLVADRVPNYTSWSQHCPWEPQKQPPWEFLQVLEPGARGLWKPPDIKGKLMVCYETLPRGQCLLYNWEEERATNHLDQVPSMQDGSESFFFRHGHRGLLTMQLKSPMPSSTTQKDSYQPPGNVYWPLRGKREAMLEMLLQHQICKEVQAEQEPTRKLFEVESVTHHDYRMELAQAGTPAPTKPHDYRQEQPETFWIQRAPQLPGVSNIRTLDTPFRKNCSFSTPVPLSLGKLLPYEPENYPYQLGEISSLPCPGGRLGGGGGRMTPF
Protein: PHD-type domain-containing protein (Q18605)
Organism: Caenorhabditis elegans
Interaction partners:
- Paired amphipathic helix protein sin-3
- Chromo domain-containing protein
- Mortality factor related protein 1
- C2H2-type domain-containing protein
- Bromo domain-containing protein
- Probable histone-binding protein rba-1
- Probable histone-binding protein lin-53
- DEK_C domain-containing protein
- Histone deacetylase
- Putative histone deacetylase 2
Sequence:
MQKKEKEGRRKLKYDSNDGLLPEIRRVCGFPHHISEELSARGSGKKKKQVEEEWKWPEAQICGICSSGGNILCCEQCPASFHLACIGYESSDLPDDNFYCNRCRNLPENVRLFPPEKCSPSVNPVLRVENENHRNWEAIEYHCNRLRDEEQAEKMKKDVAYGPKSEFAEIQDCFRDKNLLKALGMANPMDYTIPPEFQADRDCFSGDAMEDKRPTIMGEVCAECNLKDDWTRMLKCDFCDLIWHQKCVTPPLIHVRAYFYWMCPRHPETVIDSVLIGDEISREDRRRLYDKYADVEPSYEIFEEFCIKTEQFRMKSEVFDSEEMYYDPEEASTSFMQTVIKPRQTSRKTTGRSASKKKSNGRFFASSWDFPGLSSRETSPSRKNSRKSPDSVATERKDRVLDKIDKKRSIKLTEEEIIMSIMPVEESSRAEYLTQKMLGTDIEQSTNFFNRHSAMIDRIRAFYGNLPEKELIKLMREDLDPVETIRGGGTQSIISQNEKPYRKKLKADVEVLIQHVGLGTDSTERHFNSIGTEAFYRRCAPPVTARNVLNQKTLREVVLNSQKEAHEGAGVYEYHAEPEQLENLVLLAYEPSFESPEDRDTYFVPSMTIWSKEPICALTRKWAASGASKQAPPSSSSSEAPSVEAEVKEEVVEEEDEENEARMRRESTATSSIVYNNDTGPLEFIEENMPPPAATITEKSDPFDFSSLEMPEIHEKAETVYEAEGYYGESDDLPLDLRRTKSESDLVDRIIWPLVRSALQNFIRREDCHQMHLEHNYSSLYQTHDSDEENQPVVEVEKLITYEEYQENLYSAEFASPQTPPPIPPPPAVYYDNFSDAPRKRGRPVGSRNRKEGDTTIPKQQRKRNPQPVGRGRGRGGGRPRGSRSSRGSMDDGGGSRRHSTASDANESAELLNQPVTKQLRDEIKEIKLKYTKMMMDRGFEQAKDEYFRNRDAALSKWTPEQWKEHNEQCVAARLSSLIPYDQRYFLPTQRVLARLDLEDGDLRLPAVHLPIAIQRCVTKLGTAHDCHVRCDKLTGDAWCSVLADYHCDIVRDYYSDNFYISTLGTEAVFVDGRAVRRPRLTPFEAAEKLRTRGSSTIIPPHIKCRCQKHSDLQISRQESTGELVRCGILKLEHGARIQIGCVAFIFSRI
Protein: Carboxylic ester hydrolase (EC 3.1.1.-) (Q2UH24)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
Sequence:
MLSGFFWSALAMFYSRIRSVASTAAVTSLFTATVAQAGNCSSSVIPHPSIPGGQVLDLSAVPVSNYAYDESTLDFCNVTVTYTHPGKNDTIHATVWLPFTNWNHRLQGSGGGGFAMRSEDAVLAAAVAQNYTVLATDGGHDLNSQSSASWSLDASGNVNMALLEDFAYVALGDAATIGKQIATSFYGLAPRYSYWNGCSTGGRQGLMLAQRYPTAYDGIMAAAPAINWASFLVAEFWPQFVMNQLNAFPPTCVSDAITAAAIKACDDIDGVLDGVISAPDLCDFDPFTTVDTRVNCSGVSVRISKKDAEVANSAWEGFRSSEGSFLWYGLDKGTPLSMGASSLASTVCSTPFNCTGSPFAISSDWIRRFVLQDPSFDLTTLDHKALDRVFSLSKERYNDIISTDNPDLSAFKQAGGKMITWHGLSDTLIFPKGTEQYYKRVEEKDPSVRDFYRFFKAPGVHHCSGGVGPVPVDPLSQVVDWVENGVVPETVDALAADGRRRNLCQYPLVSVYKGGDVKDAASYRCEEGH
Protein: Coiled-coil domain-containing protein 141 (Coiled-coil protein associated with myosin II and DISC1) (E9Q8Q6)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20956536}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20956536, ECO:0000269|PubMed:34298015}. Note=Co-localized with DISC1 at/around the centrosome. Localizes to the centrosome, at least in part, in a DISC1-dependent manner (PubMed:20956536). Accumulates and oscillates at the dilation in cortical neurons during migration (PubMed:34298015). CAMDI protein level is stabilized at the G1 phase and destabilized at the G2 /M phase (PubMed:34298015). {ECO:0000269|PubMed:20956536, ECO:0000269|PubMed:34298015}.
Interaction partners:
- Disrupted in schizophrenia 1 homolog
Sequence:
MSCKESPHVGASTTTVSSVAVHAGDSKIVIAVVKCGKWVRLQLAESQPNLLEIGSSQDETKKLLHDHELLLAKLKALEDRVWELLREADRTAEANKAQSQVYDAMAQTLGEAWATLVSMLERRRELLGLTSEFFQSALEFAIKIDQAEAFLQNPHEFESTEALQSLLLLHDRHAKELLERSLDLLNKSQQLTDFIEKFKCEGSTMNSELIQGAQSSCLKIDSLLELLQDRRRQLDKYLQQQRQELSQVLQLCLWDQQENQVSSWFQKAIRDLQEQSLGASLSDNRELICKHEDLIVKAKEWDSAVEKLKSQALGILLSKDLAGKEHLQLSNQKLNRLQEEFGRLMVERKAWLSMANDFFTSANKSFDVLGKVEAYLKLLKSEGLSLPVLAAKHEELHREIKDSTATALQKGRTLISQVDSCRSRVTGIHEMMGYIQNRVDCLTEQCTAHEEFARKRQQLATSVDDYLRKVEMSIQEIRPILATTLDVASSPSESEKILNKYLELDIQVKETAHALEAAAKIMTEKNELELNEVALLPLKVKWLEEELSTLGRSISCRSRILQTYVAFRKSSEEAEEQLQSLKEFYLTEIPWKDEDDAVVKCQSNSAERKWQLFLKKSFLTQDLSLEFLNLINMAKENEILNVKNEMHIMENIMEKQTNGREELSHLRVAWYLKAIEGKPAREQWEMFKEKLTKTTHSVKLLHEVLMPVSALDLGGSLQSTSDLRRRWIAMKPQLQQLHEDVQQITKEWEVLSSQGAPLKEKAEQLKDLVHLHRRQRERIQEYEEILYKTVQFHQVKEELVHLIKPRELELLAQPMELASSEEVQMQLGRSQERRAHVDHLHQLALTLGVDIISSVQQPNCSNISAKNLQQQLEALELESRSWSAQAKEHERVLSCSLEYCTARDEISELKESFKDIKKKFNNLKFNYSKKNEKSRNLKTLQYQIQQVDTYAEKIQALRKKMEKVNNKTSDSFLSYPSNKANMLSEAMEDLKKNVDDFDKVVTDYKMNLDLTEHLQEVIEECNFWYEDASATVVRVGKYSMECQTREAVDILHRQFNKFITPSVPQQEERIQEVIDLAQRLYGLEEGQKYAEKIVTRHKEILESITELCGSLVELKEKLMQGEVPKMNSDLEDFHDNCIDLLKGPGKDDQKTFSEERNEGQVQGADVLAVNGTREDGLPMDLRRTSSDKEDSAQGLILPEDTLSGEESECISSDDISLPPLPVSPESPLAPSDMEVEELTSSSALALHISGYRMHPGTGGLGKAQESALPSPIAFADGGHSKKDTFTSHFERPYPQLKAESSLASRGSAEMSTKLHINVKCPASMPHEVHDKALQQCSQARESTLEMQEKVHADSNVTKTQDRLHAALDVSPGLGSQPDTSESHQRRVGPQGNKKNSSAENSVVSLAGQAPHFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTWFKKGQKLCADGHLQVLHKDTKHSVFIPKVCEADAGLYVAQAQNSSGTLSSKAILHVTGNHGPPITRLNWIMLCIIYVSVSVIYWLLTR
Protein: SNF1 protein kinase subunit beta-1 (SNF1-interacting protein 1) (P32578)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Promotes the PKA-regulated relocalization of the SNF1 kinase complex to the vacuolar membrane in response to various types of carbon stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11331606, ECO:0000269|PubMed:14966266}. Vacuole membrane {ECO:0000269|PubMed:11331606, ECO:0000269|PubMed:14966266}; Peripheral membrane protein {ECO:0000269|PubMed:11331606, ECO:0000269|PubMed:14966266}; Cytoplasmic side {ECO:0000269|PubMed:11331606, ECO:0000269|PubMed:14966266}. Note=Resides in the cytosol during growth in glucose and relocalizes to the vacuolar membrane in response to carbon stress. {ECO:0000269|PubMed:14966266}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit gamma
- Carbon catabolite-derepressing protein kinase
- SNF1 protein kinase subunit beta-2
- SNF1 protein kinase subunit beta-3
- SNF1-activating kinase 1
- Regulatory protein MIG1
- Protein SIP4
- Regulatory protein CAT8
- Serine/threonine-protein kinase TOS3
- Serine/threonine-protein kinase ELM1
Sequence:
MGNSPSTQDPSHSTKKEHGHHFHDAFNKDRQGSITSQLFNNRKSTHKRRASHTSEHNGAIPPRMQLLASHDPSTDCDGRMSSDTTIDKGPSHLFKKDYSLSSAADVNDTTLANLTLSDDHDVGAPEEQVKSPSFLSPGPSMATVKRTKSDLDDLSTLNYTMVDETTENERNDKPHHERHRSSIIALKKNLLESSATASPSPTRSSSVHSASLPALTKTDSIDIPVRQPYSKKPSIHAYQYQYLNNDETFSENSQMDKEGNSDSVDAEAGVLQSEDMVLNQSLLQNALKKDMQRLSRVNSSNSMYTAERISHANNNGNIENNTRNKGNAGGSNDDFTAPISATAKMMMKLYGDKTLMERDLNKHHNKTKKAQNKKIRSVSNSRRSSFASLHSLQSRKSILTNGLNLQPLHPLHPIINDNESQYSAPQHREISHHSNSMSSMSSISSTNSTENTLVVLKWKDDGTVAATTEVFIVSTDIASALKEQRELTLDENASLDSEKQLNPRIRMVYDDVHKEWFVPDLFLPAGIYRLQFSINGILTHSNFLPTATDSEGNFVNWFEVLPGYHTIEPFRNEADIDSQVEPTLDEELPKRPELKRFPSSSRKSSYYSAKGVERPSTPFSDYRGLSRSSSINMRDSFVRLKASSLDLMAEVKPERLVYSNEIPNLFNIGDGSTISVKGDSDDVHPQEPPSFTHRVVDCNQDDLFATLQQGGNIDAETAEAVFLSRYPVPDLPIYLNSSYLNRILNQSNQNSESHERDEGAINHIIPHVNLNHLLTSSIRDEIISVACTTRYEGKFITQVVYAPCYYKTQKSQISN
Protein: Basic-leucine zipper (BZIP) transcription factor family protein (F4I9R1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Basic-leucine zipper
- Activator of spomin LUC3
Sequence:
MASSKGSQSVRNLMYPGKHALLPPKIPFPSVSASYSEYIPTGLIGSRHGQKLSNEKTHHQRTSSESHLVEELPFWLDDLLNEQPESPARKCGHRRSSSDSYAYLDVANATNISLTLQNDFSYRNTVLSTQRGVQELDRNKNAQDAAFYSGASFLKQKSRQRDSLVATGACPSWLPFARENGGGKNLGALYMSQDATVISSERKNYAEPFSHDPKMLSSEENNSNPSPVTYEADNTKRAKQQFAQRSRVRKLQYISELERNVQTLQAEGSKVSAELDFLNQRNLILSMENKALKKRLESIAQEKLIKQLEQEVLEKEIGRLRALYQQQQQTQKPSASRGRATSKDLDSQFSSLSLNTKDSNCRRDSVSVMGQFHF
Protein: Thioredoxin-like protein CDSP32, chloroplastic (Chloroplastic drought-induced stress protein of 32 KDa) (OsCDSP32) (Q84NN4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Thiol-disulfide oxidoreductase that may participate in various redox reactions. May act as electron donor to the BAS1 peroxiredoxin. Possesses low insulin disulfide bonds reducing activity.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Nitrate reductase
- Nitrate reductase
- Nitrate reductase 1
- Thioredoxin X, chloroplastic
- Peroxiredoxin-2F, mitochondrial
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Os04g0416400 protein
- Thioredoxin reductase NTRC
- Peroxiredoxin-2E-2, chloroplastic
Sequence:
MASTAAFLSTLAGSTSLGGATPASGGGSGRSKTARFLRRRRRGGAVRAAVSGTEQAPETTKKKGGGGGGGDERVVQVHSAEELDGALRAAKERLVVVEFAASHSVNSSRIYPCMVELSRTCGDVDFLLVMGDESDATRELCRREGITAVPHFTFYKGAEKVHEEEGIGPDQLAGDVLYYGDHHSAVVQLHSRADVESLISDHRGEGGKLVVLDVGLKRCGPCVKVYPTVVKLSRTMADTTVFARMNGDENDSCMEFLRDMDVVEVPTFLFIRDGDIVGRYVGSGRGELIGEILRYNGVKVT
Protein: Serine/threonine-protein kinase ppk11 (EC 2.7.11.1) (O14047)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Located at the septum.
Interaction partners:
- Mo25-like protein
- Leucine-rich repeat-containing protein sog2
- cAMP-dependent protein kinase regulatory subunit
Sequence:
MEKHQYRDLQLIGQGSFGSVFRAQDVESSKIVALKVVDLDATKDQIETLTQEINFLIDLNSVHITKYYASFVDGFRLWITMEYCDGGSCLDLLKLSGTFSERVIAEVMRQVLEALVYLHGQGKMHRDIKAANILTMKDGLVKLADFGVSGQLESLRDKNDDFVGTPFWMAPEVVKQTGYNYKADIWSLGITAYELATGEPPYSGIHPMKVLLLIPKHSPPSLERSKFSRAFCDFVSNCLKKNPKDRATAEYLSKHKFIKKYCPNTSVKEVVASYAKWKESELLPEATPYNSTMGNSANTIDEVVWDFGTVRR
Protein: Annexin (Q6IRJ7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Annexin
- CD63 antigen
- CD9 antigen
- CD81 antigen
- Tumor susceptibility gene 101 protein
- Protein S100-A10
- LOC683667 protein
- Caspase-3
Sequence:
MSYPGYPPTGYPPFPGYPPAGQESSFPTSGQYPYPSGFPPMGGGAYPPAPSGGYPGAGGYPSPGGYPAPGGYPGTLNPGGPPSYPGGQGFGAPPGGAGFSGYPQPPAQSYGGGPAQVPVPGGFPGGQMPSQYPGGQSPYPGQPAAMTQGTQGTIRPASNFDAMRDAEILRKAMKGFGTDEQAIVDVVSNRSNDQRQQIKAAFKTMYGKDLIKDLKSELSGNMEELILALFMPPTYYDAWSLRKAIQGAGTQERVLIEILCTRTNQEIRDIVRCYQLEFGRELERDIRSDTSGHFERLLVSMCQGNRDESPSINHQMAQEDAQRLYQAGEGRLGTDESCFNMILATRSFPQLRATMEAYSRMANRDLLSSVSREFSGYVESGLKTILQCALNRPAFFAERLYYSMKGAGTDDSTLVRIVVTRSEIDLVQIKQMFTQMYQKTLSTMIASDTSGDYRKLLLAIVGQ
Protein: Protein E6 (Q1AHS5)
Organism: human papillomavirus 97
Subcellular location: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04006, ECO:0000256|RuleBase:RU363123}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04006, ECO:0000256|RuleBase:RU363123}.
Interaction partners:
Sequence:
MARFEDPSKRPYKLPDLCTELNTSLPEIEISCVYCKTTLERTEVYEFAFKDLFVVYRDCIAYAACTKCLTFFSKIRELRYYSHSVYGDTLEKITNTGLYNLLIRCLQCQKPLNPADKYKHLKDKRRFHHISGYYRGQCNSCYNQSRQERLSRRRETQV
Protein: Thioredoxin Y1, chloroplastic (AtTrxy1) (Q6NPF9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-disulfide oxidoreductase that poorly activates chloroplastic malate dehydrogenase (NADP-MDH) and fructose-1,6-bisphosphatase. Provides reducing equivalents for peroxiredoxin Q.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:15531707, ECO:0000269|PubMed:19259774}.
Interaction partners:
- Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
- Zinc finger BED domain-containing protein DAYSLEEPER
- Ubinuclein-2
- Expressed protein
- Ribonuclease H
- Terpenoid synthase 1
- Capsid-like protein
- ATP-dependent DNA helicase DDM1
Sequence:
MASISLSSSTVPSLNSKESSGVSAFASRSISAVKFQFPVRRVRTGDLKFPSLSSTTRCTPRRIEAKKQTFDSFEDLLVNSDKPVLVDYYATWCGPCQFMVPILNEVSETLKDKIQVVKIDTEKYPSIANKYKIEALPTFILFKDGEPCDRFEGALTAKQLIQRIEDSLKVKP
Protein: Non-specific serine/threonine protein kinase (H2KYA5)
Organism: Caenorhabditis elegans
Interaction partners:
- Paramyosin
- Zinc finger protein unc-98
- Zyxin
Sequence:
MSSKKRYGTYGRAITSPALLSSSVGWTRPDVTSQIDRLRSQATSVVSSPPPHEYAVPHAFSGSSNGTNASRPPADPKQPQRSRAERLRHRISERRTNAYMIPPSSTTGKDPAIDALMNKYLNKSKENLDEGRKSRESSRAQELLARTNREMSPTIDSLMKRYGNNNSSAHRIKDSTVSRRESMEIQDNENSRSLDNKSCREARLSGSDVRIKWEVTNTEVKPTSSVKRFSVIIDPTGGRMPVGNSGSRSGRLARISQSNIRPFGSNGGGATNSYGPGTHPMSGAEPCSPTKKEKHRFEITKKLGSGTYGKVSLAYDHKFDREVAVKLIKKSAIESKADLVRIRREIRIMSALNHPNIIQIYEVFENKDKIILVMEYSSGGELYDYVSRCGSLPEAEARRIFRQITSAVLYCHKHRVAHRDLKLENILLDQNNNAKIADFGLSNYFADKNLLTTFCGSPLYASPEIINGTPYKGPEVDCWSLGILLYTLVYGSMPFDGRDFNRMVRQIKRGAYFEPETPSTASMLIRNMLRVNPERRATIFDIASHWWLNLEENMPVIQELPENQIIDHTPLTEREETMIVQDLADEQDVFMEFGHLSSETRRKIEDFRIRRKEAEEFNDNSPVKPPKARKTDELTGKISKEQPEEMKSAEKSLRGVKEEKEKPKVVDPNDPLERLRQIENRLGQNKKDKEAAKTSARVETVKLKEVKKEKSPEQQPEDPKTARGTSKPADSRAPSFVPVKDRPETSEPERPRTRPHLTASAYRIETDSLNMLMNQVLEQMEKGPVNLNIIARIKAHPLYDTRPMVKELLESIIAAQPEPVQKQTSKVVEQQTFSRQNTLTRKKKEDPLEEEIPEVPSPSRKMKERPWHSVEVGFDPDEEPEHDRMQESIASNATEVTVQDTSFEDDSSDEEERKKTPVASTPKTPVLIVEKQESSTNAEDEESDEGDDYSDAEMEELADEVDKKGPSDSKLAPVVENLEANPPPDPSSSPQFLDAFDRGLIKRQSKGKYQHTLINNYGRGVSTECESPTQQRKFFGGPQPSAELSPFLFDKAKEILQTYPNNKLDARGIDVELRRKLRMEKVKADLLKQPKDGDKPRNSYVGSVPPRSPPPIVVKSDGEELDDEEEEEEDEEEIEETDSEEGSDFENFKPKRPIIAAVRRDDGAVVPVIHQTTRPAVVSPNSQNPRYQVASPKTSTVIQATPEKVPVAGTSAKYLVTVAELKLKPTDKKEEAQLKEQLKDSEINSERKVTKGAAPSTISQDSDGKDTFESASAYIRRKNRERRQRNRTIGTAEEALRALERPSVDPYDDRAFSPLSTDPFYSHHSSGSAAPSALGYVRPRYHDDSYRTHRDSDYRPMSPTSRYTAAVTRDDRGKSTSYDPHETTRPSYDRGYITSSNASPSYTRKFEHEQPTLNSWANDRKFEVYKTRAERDAERNTYHPTGTTGASSYRPSSYYTSASDRPVTGLRRPEESYTSSTNYGRYDGRSTTPSNDQYAISTALAENQASSMNNRFRPTARRVASAMTDADRRNYHRSRSMDRNKVDYEYGSNLLNRLTTPDSHGDYSYVNYHDSSNGRSNITLEKDGQPRSILKNKQSADIEPRVESSYEPSNGVRSVFERLRRHLSLEKSVSPQRQNTSFYGRQLRVASVGPHSRNIDSTSSALDNPKKKRSLLSFNRRKTSEVRMGADGKLVTNGYDSTPSSRDFKRPSSPIDRIKSLFRKNESSGTGHSDYYNSSRNYTSSNPVSTTREPYVAQYRKYPGSTSRDTSSALNRYSYTPGLTDQRRHWYDDPNIY
Protein: Granzyme M (Granzyme Met-ase-1 precurser) (O08643)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEVCWSLLLLLALKTLWAAGNRFETQIIGGREAVPHSRPYMASLQKAKSHVCGGVLVHRKWVLTAAHCLSEPLQNLKLVLGLHNLHDLQDPGLTFYIREAIKHPGYNHKYENDLALLKLDRRVQPSKNVKPLALPRKPRSKPAEGTWCSTAGWGMTHQGGPRARALQELDLRVLDTQMCNNSRFWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVCGKGQVDGILSFSSKTCTDIFKPPVATAVAPYSSWIRKVIGRWSPQSLV
Protein: Protein THP3 (THO-related protein 3) (Q12049)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Forms a complex with CSN12 that is recruited to transcribed genes and required for transcription elongation. May also be involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cop9 signalosome complex subunit 12
- 26S proteasome complex subunit SEM1
- 26S proteasome regulatory subunit RPN3
Sequence:
MQNPYGHFTNNTTEDREASSQGGPFGQSLNRPLDYAGSFPSLTYNNNNFIANQQPSLPLPEPRLSWNNVNQVSNPLMVTPLPGLQKRMNKNIKKKLPRVSKKASALSNGVSGNVMSNSNIVGHGAVGSASGWKVEMGGSDELERRKRRAERFSQGPSATTNSNDNLNEDFANLNAISSKSHQYDKKIHVVGRCQTLEKSYLRLTSEPNPDLIRPPNILQKMYCLLMDKYQSKTATYTYLCDQFKSMRQDLRVQMIENSFTIKVYQTHARIALENGDLGEFNQCQNRIMALFENPTIPKKSYSEFICYSVLYSMLTEDYPSISHLKLKLIDDGSSEILEDEHVKMIFELSDMKLVGNYHYFMKNYLKLHKFEKCLINSFLNLEKLIFLTIICKSYNQVNLDFVKSEFNFNSIEETTNFLNEQNLTEFILNKQITDSNGKSSNIKILNTKGCRVQLIQNYMKSKKIDIKGQK
Protein: Vacuole transporter chaperone complex subunit 5 (Vacuolar membrane polyphosphate polymerase regulatory subunit 5) (PolyP polymerase) (P38966)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (Probable). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (Probable). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (Probable). VTC5 interacts with the VTC complex to increase the rate of polyP production.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:27587415, ECO:0000269|PubMed:34544285}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to the vacuole membrane by the AP-3 complex. Membrane localization is required for VTC5 to promote VTC activity. {ECO:0000269|PubMed:34544285}.
Interaction partners:
- Vacuolar transporter chaperone complex subunit 1
- Vacuolar transporter chaperone 3 complex subunit 3
- Vacuolar transporter chaperone complex subunit 2
- Vacuolar transporter chaperone complex subunit 4
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- Pumilio homology domain family member 6
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit zeta
Sequence:
MKFEDRILNKSIPEWKFYNINYEKLKVAIKKVTAYDYDNPNDSGMEKLLNQCSVAFDQEFQNVNLFVSLKIKEISTRILSVESSIIDFSKGLNKTSRNRFNLRKLKIINAHVDDCNFELQLLSRFLIIQRIALRKLFKKLLNEFPQDSENPLTASEYVTSIRNSESLRNGHEGISFMKLDLDPYLLEVSLIVDVLHDLENKLEDATEPAVEQRSLNRSDESAHTSSSPEANNSSLPASPRSIPLLSNKKTSKMIDSSLEFDTALIDKAENLGRFLLSSEDIEGLKFMLLNIGFRIIDDSIISTSKEILDTTDNINSAGNKSIRSAKSFNDLQHTLSLSKQKNILPSAVQSNEKYVSISILDTVGNEGSPLLLTDDNINQHPNMIVSSTAEDTCIVMCHVGGLRNHVVTNDLLLRDVKNILSAMRSGNDTKNISALINSLDPSPISKIALEWIQSHRLKTIEPKLDFKRTRFISADNGDIYLIALDESITIGNVSTLPFPILEIKKLSRSSGLSQTAINEDNKFKQLMKSVVTNEFQCSLIPPDLTTWKICLELVHSNELQNDLFQLLLRDQYKLNSDDSLSPDEFFQLGKDRLEEEFDLTGPINNSQGSVDSGRRVRIHKKSKQSDNETKKKPIRYWNEFDEQEEDNLDNAFYIDTNGSRSTTDNEESLLLRNSPPDYGFILFSRNFINRTYDFCEKLRNLIRHDKKTSPDLFQNSKHPHCSSTNYGSVASFGSQSTSASYDDVQRYLQYQQQDIEDSQSIYEYRHDEVVTFLYLSALLTSCIMASVCLGIVLSLFRGQSNNEIDLEIQNILIAIIIISLLVSLILICACLLLLFSRFTLAPIWHYVGCFTMFFSVTGTVCYGMIEIFF
Protein: Testis-expressed protein 11 (Protein ZIP4 homolog) (ZIP4H) (Q8IYF3)
Organism: Homo sapiens (Human)
Function: Regulator of crossing-over during meiosis. Involved in initiation and/or maintenance of chromosome synapsis and formation of crossovers.
Subcellular location: Chromosome {ECO:0000250|UniProtKB:Q14AT2}. Note=Forms arrays of discrete foci along synaptonemal complexes in spermatocytes and fetal oocytes. {ECO:0000250|UniProtKB:Q14AT2}.
Interaction partners:
- Synaptonemal complex protein 2
- Probable ATP-dependent DNA helicase HFM1
- Protein shortage in chiasmata 1 ortholog
- MutS protein homolog 4
- Protein SPO16 homolog
- Probable E3 SUMO-protein ligase RNF212
- MutS protein homolog 5
- Testis-expressed protein 15
- HORMA domain-containing protein 1
- Meiotic recombination protein SPO11
Sequence:
MISAHCNLRLLCSSDSSASASQVAGTTEVVENLVTNDNSPNIPEAIDRLFSDIANINRESMAEITDIQIEEMAVNLWNWALTIGGGWLVNEEQKIRLHYVACKLLSMCEASFASEQSIQRLIMMNMRIGKEWLDAGNFLIADECFQAAVASLEQLYVKLIQRSSPEADLTMEKITVESDHFRVLSYQAESAVAQGDFQRASMCVLQCKDMLMRLPQMTSSLHHLCYNFGVETQKNNKYEESSFWLSQSYDIGKMDKKSTGPEMLAKVLRLLATNYLDWDDTKYYDKALNAVNLANKEHLSSPGLFLKMKILLKGETSNEELLEAVMEILHLDMPLDFCLNIAKLLMDHERESVGFHFLTIIHERFKSSENIGKVLILHTDMLLQRKEELLAKEKIEEIFLAHQTGRQLTAESMNWLHNILWRQAASSFEVQNYTDALQWYYYSLRFYSTDEMDLDFTKLQRNMACCYLNLQQLDKAKEAVAEAERHDPRNVFTQFYIFKIAVIEGNSERALQAIITLENILTDEESEDNDLVAERGSPTMLLSLAAQFALENGQQIVAEKALEYLAQHSEDQEQVLTAVKCLLRFLLPKIAEMPESEDKKKEMDRLLTCLNRAFVKLSQPFGEEALSLESRANEAQWFRKTAWNLAVQCDKDPVMMREFFILSYKMSQFCPSDQVILIARKTCLLMAVAVDLEQGRKASTAFEQTMFLSRALEEIQTCNDIHNFLKQTGTFSNDSCEKLLLLYEFEVRAKLNDPLLESFLESVWELPHLETKTFETIAIIAMEKPAHYPLIALKALKKALLLYKKEEPIDISQYSKCMHNLVNLSVPDGASNVELCPLEEVWGYFEDALSHISRTKDYPEMEILWLMVKSWNTGVLMFSRSKYASAEKWCGLALRFLNHLTSFKESYETQMNMLYSQLVEALSNNKGPVFHEHGYWSKSD
Protein: Sterol 24-C-methyltransferase (EC 2.1.1.41) (Delta(24)-sterol C-methyltransferase) (Q6FRZ7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol.
Interaction partners:
- 3-keto-steroid reductase
- C-8 sterol isomerase
- Lanosterol 14-alpha demethylase
- Delta
- Delta
- C-22 sterol desaturase ERG5
- Squalene synthase
- Candida glabrata strain CBS138 chromosome K complete sequence
- Delta
- Terpene cyclase/mutase family member
Sequence:
MSESELRQRQAEFTKELHGEGAESRTGLTALLSKNRNAQREAVSKYLRHWDGKTDKEAEDRRLEDYNEATHSYYNVVTDFYEYGWGSSFHFSRFYKGENFQAAMARHEQYLAYMAGIKKGDLVLDVGCGVGGPARTIARFTGCNIIGLNNNDYQIQKAKYYAKKYNLQDHMDFVKGDFMNMEFEPNSFDKVYAIEATCHAPKLEGVYGEIYKVLKPGGTFAVYEWVMTENYDENNEEHRKIAYEIELGDGIPKMFTVDVAKQALKNVGFEVEVSKDLADEDDEIPWYYPLTGEWKYVQSLSDIATFFRTSYFGRKFTNCMVSIMEKVGVAPQGSVEVTAALENAAVGLVEGGRKKLFTPMFLFVAKKPEDAK