wanglab/gogpt-training-data huggingface dataset:
Protein: Glycerol-3-phosphate acyltransferase 1 (AtGPAT1) (EC 2.3.1.15) (Q9SHJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Involved in pollen development, by being required for tapetum differentiation and male fertility. In addition to the sporophytic effect, it also exerts a gametophytic effect on pollen performance.
Subcellular location: Membrane {ECO:0000269|PubMed:12897259}; Multi-pass membrane protein {ECO:0000269|PubMed:12897259}. Mitochondrion {ECO:0000269|PubMed:12897259}. Note=According to PubMed:12897259 it is mitochondrial. However, no clear transit peptide is predicted by sequence analysis tools.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 9
- Glycerol-3-phosphate acyltransferase, chloroplastic
- Glycerol-3-phosphate dehydrogenase SDP6, mitochondrial
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- 1-acyl-sn-glycerol-3-phosphate acyltransferase 2
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5
- Glycerol kinase
- Non-specific phospholipase C3
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
Sequence:
MVLPELLVILAEWVLYRLLAKSCYRAARKLRGYGFQLKNLLSLSKTQSLHNNSQHHLHNHHQQNHPNQTLQDSLDPLFPSLTKYQELLLDKNRACSVSSDHYRDTFFCDIDGVLLRQHSSKHFHTFFPYFMLVAFEGGSIIRAILLLLSCSFLWTLQQETKLRVLSFITFSGLRVKDMDNVSRSVLPKFFLENLNIQVYDIWARTEYSKVVFTSLPQVLVERFLREHLNADDVIGTKLQEIKVMGRKFYTGLASGSGFVLKHKSAEDYFFDSKKKPALGIGSSSSPQDHIFISICKEAYFWNEEESMSKNNALPRERYPKPLIFHDGRLAFLPTPLATLAMFIWLPIGFLLAVFRISVGVFLPYHVANFLASMSGVRITFKTHNLNNGRPEKGNSGVLYVCNHRTLLDPVFLTTSLGKPLTAVTYSLSKFSEFIAPLKTVSLKRDRKKDGEAMQRLLSKGDLVVCPEGTTCREPYLLRFSPLFAELTEDIVPVAVDARVSMFYGTTASGLKCLDPIFFLMNPRPVYCLEILKKLPKEMTCAGGKSSFEVANFIQGELARVLGFECTNLTRRDKYLVLAGNEGIVR
Protein: Apoptosis regulator BALF1 (P0CK58)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Modulates the antiapoptotic activity of the viral protein BHRF1. May also play an active part in oncogenesis in Burkitt's lymphomy and nasopharyngeal carcinoma.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:11836425}.
Interaction partners:
Sequence:
MNLAIALDSPHPGLASYTILPRPFYHISLKPVSWPDETMRPAKSTDSVFVRTPVEAWVAPSPPDDKVAESSYLMFRAMYAVFTRDEKDLPLPALVLCRLIKASLRKDRKLYAELACRTADIGGKDTHVRLIISVLRAVYNDHYDYWSRLRVVLCYTVVFAVRNYLDDHKSAAFVLGAIAHYLALYRRLWFARLGGMPRSLRRQFPVTWALASLTDFLKSL
Protein: HL01030p (Lost PHDs of trr, isoform A) (Q9W1H0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone-lysine N-methyltransferase trr
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Retinoblastoma-binding protein 5 homolog
- LD02225p
- Protein will die slowly
- PAX-interacting protein 1
- Host cell factor
- Protein dpy-30 homolog
- GEO08286p1
- Nuclear receptor coactivator 6, isoform F
Sequence:
MSTNVVVSMEEKAVADDLPYFPEKFPGKVCCLCNLGEKSALGQGEILQLKAPAPAEIKDKYPTDRLREDGSRLLYGPKQAASSSGDCHYELDKIGQPDVVHPAEFLDEGFVYVHRMCIMWSLRKSQISDADGAYFATHFAEFLEQKCNFCGRYGASINCKMNCRQVHHWPCAAAAGCLLILESFTVFCTEHLSQVPVICSDNNVECLSCSSLGDLSKLIMCSTCGDHFHSTCIGLANLPDTRSGWNCARCTKCQICRQQDSNDTKYVKCEQCQKTYHASCLRPVISAIPKYGWKCNRCRVCTDCGSRTPGGGSSSRWHSHYTICDSCYQQRNKGFSCPICQKAYRAASHKEMVKCSWCNKFVHSTCDEEADLTAYHKKKEQNPDYDYVCPNCKSNSSGPGSSQQTIDSIVLSAMDSSSEQLSLKEIELDPLEGKPTMDPSSDELHKLPTGKKKVCLTSVRGRSGKFVLHRMGVMSQINKKRSTRGKGRQLALPTISSDRCLSRSMETDLTSDKKLLLCSARDKFIQAQDICVMCGSLGIESDSVMITCAQCGQCYHPYCAGVKPSRGILQKGWRCLDCTVCEGCGKKNDEARLLLCDECDISYHIYCVNPPLETVPTGNWKCSFCTLCQKCGRNPTEKSEFGDSNMLECPSCTSQSSCPVCKVSYSNGEMIIQCEHCELWAHFHCDSVNAQLTIDHYDNNVYKCFKCRCSTRSTNSLADAKFGNEDSLAITPQGSKPFVHITASSGPSFDSKSGAERNHPTLSGDMPESAPEALHWIDGVCLSESGLGMIKSLSTEIKRKRKMRQALGNGKDGQLEAAAEEALEKYKDGMVWDGTENAIPEGFTISINDEGVNILRKKRQRNLQKLGIGGFSVRNRGLKKDSEETTAVDQINSLMTMDKKKKIIRKKQKNKLIEAYPVYLQEAFFGKPLLEGGELVMADTDSSDEIDASMKVYFTRPEGKSPANQDTLAVNKSPAKTVKKVKAELKTENKTVFIQQMPMGIQNKNGTTPVSNVFDPLQAEISNTVFANRHPLDALASPNVPELDMANSVSTVPSAEVIEKPMRESPAVLVDSFMVPNQLPQEQKFHNQLYLGGNTLVNPAQQLQFRQQAPQNANKQNMQTIMSQVVLQTEKRPEEEQKVVEPVTETLNAGTQKTAEKMRKDEDLGLMATISAVLYANTEHPNLKELFPIWNDRCKQILKRWRSLCNEKKAPFLQKAKDNRSALRQRREQNKIPMPPKPQKQEEMGRVWKQPPKLKEDQPNMFVTYNGNAYDMGNYVGGSAQAASNNPNPHHVMPNVNDNLVIKATMQRTQVHTTAASTLKMTTVDNRLELNTAVYGTEPIGDKKLRNLLQKNSTEPMLMGANSDLFLGNDVMRLGMMQNTPITQNNPMLSISGKSQPSEGRSLEQDVKLGEPQEATSSAVELENVGFSDLLGGLGEGDDDDLLKSLTSEMGDDFNILEYADPELDVNVLNSLDFDDNEKCST
Protein: Dual specificity protein kinase CLK4 (EC 2.7.12.1) (CDC-like kinase 4) (Q9HAZ1)
Organism: Homo sapiens (Human)
Function: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates SRSF1 and SRSF3. Required for the regulation of alternative splicing of MAPT/TAU. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Dual specificity protein kinase CLK1
Sequence:
MRHSKRTHCPDWDSRESWGHESYRGSHKRKRRSHSSTQENRHCKPHHQFKESDCHYLEARSLNERDYRDRRYVDEYRNDYCEGYVPRHYHRDIESGYRIHCSKSSVRSRRSSPKRKRNRHCSSHQSRSKSHRRKRSRSIEDDEEGHLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHGMDGMHVAVKIVKNVGRYREAARSEIQVLEHLNSTDPNSVFRCVQMLEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFQIDHIRQMAYQICQSINFLHHNKLTHTDLKPENILFVKSDYVVKYNSKMKRDERTLKNTDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPIPQHMIQKTRKRKYFHHNQLDWDEHSSAGRYVRRRCKPLKEFMLCHDEEHEKLFDLVRRMLEYDPTQRITLDEALQHPFFDLLKKK
Protein: Merlin (Moesin-ezrin-radixin-like protein) (Neurofibromin-2) (Schwannomin) (P46662)
Organism: Mus musculus (Mouse)
Function: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex (By similarity). Plays a role in lens development and is required for complete fiber cell terminal differentiation, maintenance of cell polarity and separation of the lens vesicle from the corneal epithelium.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with DCAF1 in the nucleus. The intramolecular association of the FERM domain with the C-terminal tail promotes nuclear accumulation. The unphosphorylated form accumulates predominantly in the nucleus while the phosphorylated form is largely confined to the non-nuclear fractions (By similarity). {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase LATS1
- Angiomotin
- Protein KIBRA
- Angiomotin-like protein 1
- Angiomotin-like protein 2
- Serine/threonine-protein kinase LATS2
- FERM domain-containing protein 6
- CD44 antigen
- Protein salvador homolog 1
- Ezrin
Sequence:
MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGGPSSKHNTIKKLTLQSAKSRVAFFEEL
Protein: Inositol phosphate phosphatase SopB (Effector protein SopB) (A0A0H3NA16)
Organism: Salmonella typhimurium (strain SL1344)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MQIQSFYHSASLKTQEAFKSLQKTLYNGMQILSGQGKAPAKAPDARPEIIVLREPGATWGNYLQHQKASNHSLHNLYNLQRDLLTVAATVLGKQDPVLTSMANQMELAKVKADRPATKQEEAAAKALKKNLIELIAARTQQQDGLPAKEAHRFAAVAFRDAQVKQLNNQPWQTIKNTLTHNGHHYTNTQLPAAEMKIGAKDIFPSAYEGKGVCSWDTKNIHHANNLWMSTVSVHEDGKDKTLFCGIRHGVLSPYHEKDPLLRHVGAENKAKEVLTAALFSKPELLNKALAGEAVSLKLVSVGLLTASNIFGKEGTMVEDQMRAWQSLTQPGKMIHLKIRNKDGDLQTVKIKPDVAAFNVGVNELALKLGFGLKASDSYNAEALHQLLGNDLRPEARPGGWVGEWLAQYPDNYEVVNTLARQIKDIWKNNQHHKDGGEPYKLAQRLAMLAHEIDAVPAWNCKSGKDRTGMMDSEIKREIISLHQTHMLSAPGSLPDSGGQKIFQKVLLNSGNLEIQKQNTGGAGNKVMKNLSPEVLNLSYQKRVGDENIWQSVKGISSLITS
Protein: Acyl-coenzyme A oxidase (C9J0G0)
Organism: Homo sapiens (Human)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
Sequence:
MGSPVHRVSLGDTWSRQMHPDIESERYMQSFDVERLTNILDGGAQNTALRRKVESIIHSYPEFSCKDNYFMTQNERYKAAMRRAFHIRLIARRLGWLEDGRELGYAYRALSGDVALNIHRVFVRALRSLGSEEQIAKWDPLCKNIQIIATYAQTELGHGTYLQGLETEATYDAATQEFVIHSPTLTATKWWPGDLGRSATHALVQAQLICSGARRGMHAFIVPIRSLQDHTPLPGIIIGDIGPKMDFDQTDNGFLQLNHVLPDGTYVKLGTAQSNYLPMVVVRVELLSGEILPILQKACVIAMRYSVIRRQSRLRPSDPEAKVLDYQTQQQKLFPQLAISYAFHFLAVSLLEFFQHSYTAILNQDFSFLPELHALSTGMKAMMSEFCTQGAEMCRRACGGHGYSKLSGLPSLVTKLSASCTYEGENTVLYLQVARFLVKSYLQTQMSPGSTPQRSLSPSVAYLTAPDLARCPAQRAADFLCPELYTTAWAHVAVRLIKDSVQHLQTLTQSGADQHEAWNQTTVIHLQAAKVHCYYVTVKGFTEALEKLENEPAIQQVLKRLCDLHAIHGILTNSGDFLHDAFLSGAQVDMARTAYLDLLRLIRKDAILLTDAFDFTDQCLNSALGCYDGNVYERLFQWAQKSPTNTQENPAYEEYIRPLLQSWRSKL
Protein: GTP-binding nuclear protein Ran (F5H018)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU363057}.
Interaction partners:
Sequence:
MAAQGEPQLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLE
Protein: Axin-2 (Axin-like protein) (Axil) (Axis inhibition protein 2) (Conductin) (O70240)
Organism: Rattus norvegicus (Rat)
Function: Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2T1}.
Interaction partners:
- Glycogen synthase kinase-3 beta
- Catenin beta-1
- Adenomatous polyposis coli protein
- Segment polarity protein dishevelled homolog DVL-1
- Lymphoid enhancer-binding factor 1
- Adenomatous polyposis coli protein 2
- Dishevelled segment polarity protein 3
- Dishevelled segment polarity protein 2
- Poly [ADP-ribose] polymerase
- Transcription factor 7 like 1
Sequence:
MSSAVLVTLLPDPSSSFREDAPRPPVPGEEGETPPCQPSVGKVQSTKPMPVSSNARRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSVVSKQLKPATKTYIRDGIKKQQIGSVMFDQAQTEIQAVMEENAYQVFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVLCGYLPTLNEEEEWTCADLKCKLSPTVVGLSSKTLRATASVRSTETAENGFRSFKRSEPVNPYHVGSGYVFAPATSANDSELSSDALTDDSMSMTDSSVDGIPPYRMGSKKQLQREMHRSVKANGQVSLPHFPRTHRLPKEMTPVEPAAFAAELISRLEKLKLELESRHSLEERLQQIREDEEKEGSEQALSSRDGAPVQHPLALLPSGSYEEDPQTILDDHLSRVLKTPGCQSPGVGRYSPRSRSPDHHHHHHQQCHALLPTGGKLPPEAACPLLGGKSFLTKQTTKHVHHHYIHHHAVPKTKEEIEAEATQRVRCLCPGGTDYYCYSKCKSHSKPPEPLPGEQFCGSRGGTLPKRNTKGTEPGLALPAREGGMSSAAGAPQLPGEEGDRSQDVWQWMLESERQSKSKPHSTQSIRKSYPLESARAPPGERVSRHHLLGASGHPRSAARAHPFTQDPAMPPLTPPNTLAQLEEACRRLAEVSKPQKQRCCVASQQRDRNHPATGQAGPTSFSNPSLASEDHKEPKRLASVHALQASELIVTYFFCGEEIPYRRMLKAQSLTLGHFKEQLSKKGNYRYYFKKASDEFACGAVFEEIWDDETVLPMYEGRILGKVERID
Protein: Leukocyte ribonuclease A-1 (Q27J91)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAMSSLWWTAILLLALTVSMCYGVPTYQDFLRTHVDFPKTSFPNIAAYCNVMMVRRGINVHGRCKSLNTFVHTDPRNLNTLCINQPNRALRTTQQQLPVTDCKLIRSHPTCSYTGNQFNHRVRVGCWGGLPVHLDGTFP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I6ANX6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSAEVRLRQLQQLVLDPGFLGLEPLLDLLLGVHQELGASHLAQDKYVADFLQWVEPIAARLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVKGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLQPDGTVRSLVAVGTPDYLSPEILQAVGGGPGAGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYAKIVHYREHLSLPRADMGVPEEAQDLIRGLLCPAEIRLGRGGAGDFQKHPFFFGLDWEGLRDSVPPFTPDFEGATDTCNFDVVEDRLTAMETLSDMQEDMALGVHLPFVGYSYSCMASRDNQVTDPTPMELEALQLPVSDLQGLDLPPPVSPPDQAAEEADPAAVPVPPAETETMVTLRELQEALEEEVLTRQSLSRELEAIRTANQNFSSQLQEAEVRNRDLEAHVRQLQERMEMLQAPGAAGESLTHSQPGGRRVEMGHVGCMNPGAGEESRLGHRSRATALLRPPRSIHLSLLLPAVTGVPSPRATDPPSHVPRPGLSEAHCLLLFAAALAAAATLGCTGLVAYTGRLTPVWCFSGATFAP
Protein: MEI2 C-terminal RRM only like 1 (Putative RNA-binding protein) (Q4PT05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable RNA-binding protein ARP1
Sequence:
METKKPTKSLNPYAPAFTPPSRSPPLFNFNKPFPCYNKPFKAITGAHVKPEKNPFVRYGFCHRRCLPPRLLKKPLPENKLAGRTSVMVKNIPNCLGRMDLLRILDNHCRKHNEKSSYDFLYLPMDFGKRANLGYAFVNFTSSLAAERFRREFENFSWDNIGFRKKICEITVAKYQGKEELTRHFRNSRFTCHTDDYLPVVLSPPSNGFTAYTLTKLGYRVGALGGGSRNASLR
Protein: Panulirin (B3EWX6)
Organism: Panulirus argus (Caribbean spiny lobster) (Palinurus argus)
Function: Involved in the melanization cascade in response to lipopolysaccharide (LPS). In vitro, reversibly and competitively inhibits trypsin (Ki=8.6 nM) but not serine proteases chymotrypsin, elastase, subtilisin, thrombin and plasmin, cysteine peptidase papain or metallopeptidase carboxypeptidase A.
Interaction partners:
Sequence:
MKNKAVLMLMALFLVAVTQVHGDPEPSYKARSCTAYGYFCMIPPRCRGTVVANHWCRARGHICCSSPSNVYGKNQLLAA
Protein: Eukaryotic translation initiation factor 3 subunit K (eIF3k) (eIF-3 p25) (Q9SZA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03010}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit M
Sequence:
MGVEIQSPQEQSSYTVEQLVALNPFNPEILPDLENYVNVTSQTYSLEVNLCLLRLYQFEPERMNTHIVARILVKALMAMPTPDFSLCLFLIPERVQMEEQFKSLIVLSHYLETGRFQQFWDEAAKNRHILEAVPGFEQAIQAYASHLLSLSYQKVPRSVLAEAVNMDGASLDKFIEQQVTNSGWIVEKEGGSIVLPQNEFNHPELKKNTGENVPLEHIARIFPILG
Protein: Calcium-activated potassium channel subunit alpha-1a (BK channel) (Potassium large conductance calcium-activated channel, subfamily M, alpha member 1a) (Slo1a) (Slowpoke homolog) (B7ZC96)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q12791}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12791}.
Interaction partners:
- Si:ch211-38m6.7
- Si:ch211-247n2.1.
- cGMP-dependent protein kinase
- cGMP-dependent protein kinase
- Potassium large conductance calcium-activated channel, subfamily M, beta member 2.
- Uncharacterized protein.
- Potassium intermediate/small conductance calcium-activated channel, subfamily N, member 1a.
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
Sequence:
MSNNINFNKNPDSSVSISKMDVIIPFTPDVPCDNNGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCNIKNKEAQKVNNPITIQADGTTKTGNEKEEAPASEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALGIYFIDSSDPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLCSIFISTWLTAAGFIHLVENSGDPWENFQNSQPLSYWECVYLLMVTMSTVGYGDVYARTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVNGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKAGFIAQSCLAQGLSTMLANLFSMRSYIKIEEDTWQKYYLEGVANEMYTEYLSSAFVGLSFPTVCELCYVKLKLLLIAIEYKSEQRESSILINPGNHVKMQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRIEDEHPSTLSPKKKQRNGGMRNSPNCSPKMMRHDPLLIPGNEQIESMDANVKRYDSTGMFHWCPSKEIEKVILTRSEASMTVLSGHVVVCIFGDVTSALVGLRNLVMPLRASNFHYHELKPIVFVGSLDYLRREWETLHNFPKVFILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDASLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGLVRQASVTTGSNIPIITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALLAEENALRGGYSTPQTLANRDRCRVAQLALYDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLGAPSQCTKRYVITNPPYEFEMVPTDLIFCLMQFDHNAGQSRASLSHSSHSSHSSSKKSSSVHSIPATNRQNRSSKAREARDKQNATRMNRMGPEKRWFTDEAENAYPRNIQIKPMSTHMANQVNQYKSTSSLIPPIREVEDEC
Protein: Homeobox protein Hox-A10 (Homeobox protein Hox-1.8) (P31310)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to the DNA sequence 5'-AA[AT]TTTTATTAC-3'.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-A9
- Homeobox protein Meis1
- Pre-B-cell leukemia transcription factor 2
- Homeobox protein Hox-A11
- Homeobox protein Hox-D10
Sequence:
MSARKGYLLPSPNYPTTMSCSESPAANSFLVDSLISSGRGEAGVGGGSAGGGGGGYYAHGGVYLPPASDLPYGLQSCGLFPALGSKRNEAPSPGGGGGGGSGGLGPGTHGYAPAPLDLWLDAPRSCRMEPPDGPPPPQPQPQQQQQQPPPPPPQPPQPQPQATSCSFAQNIKEESSYCLYDAADKCPKGSAAADLAPFPRGPPPDGCALGASSGVPVPGYFRLSQAYGTAKGFGSGGGGTQQLASPFPAQPPGRGFDPPPALASGSTEAAGKERVLDSTPPPTLVCTGGGGSQGDEEAHASSSAAEELSPAPSENSKASPEKDSLGSSKGENAANWLTAKSGRKKRCPYTKHQTLELEKEFLFNMYLTRERRLEISRSVHLTDRQVKIWFQNRRMKLKKMNRENRIRELTANFNFS
Protein: Uncharacterized protein, isoform D (A1Z7G0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGSIYGLLPLLLLLCRLHDGGSKFVSPTRHTDLSSTIIIVEDAKACFRRVLAGKRIAPHFVRRSISCERVEECMRECGRERRFMCEGFNYRLDPSGHGQGDCELVEMPLAQMDLYSSPDRRDANLLRHPDYDYYERDRNAPSSCRRSACQDCSKGPVSSQPVYFKPSGGAGGYGDRDRDRDRDRDHYRPHSNTAVDHYRGPSGPPGSSSYEHRPPYSSEFHGSHSSSSSASSYEFSSHGSGSSSGSSSGYFGHTPPSSYGGDHPYVDRHDSPHYRPGRPDRWETLPSSSGYDSSAYRPPRPETDRIDKYRPPYRPGSDYSPYRPPSRPSHNYLDRDGAGPPGPPGSNKKPNKFVPYLIGGEDNWGHYGGSYGGSSKHSSSSSSSYWGLTESQRRKDQHDFNYFQLGAPHRESNSVLSYPGSGYEDDYPRRRNDYRQQWTRRAGPDECSAKTSEGFRLHKTAVRHAYNVPTLTECERLCSDPRPSFVCHTFSYRYNQAGRDNCMLCDRPINMLDYYVDIEPDRDYDIYSMADDMDVCRQPPPRRHDTAGPSTAISDPRNAQCFFRAIDATRFFKSIVRDSLTVRSVGECEMECIRSTKFTCRAFAFRYGQQRHAGVIDNCQLSDWPVRDMDKERHLILDAAFDIFERASYGHGCEIQPIVDEKHKKLCYLGYGSPARLLPPAIKKVISVPSEIACKKECIRFRETTPFKCFAFSYGSHASSFNCELSDLDQTELKQDVHYAHTKDRDFWLFAWNPFDWTCRDKVNTIGGSRVNNDRRMDIFREPGDVAWRHYTVSGKPCRRSSPCAKNLITGFYSCETDASEVGSWDYCCKADHPCGYSKGFDYPWCFVGDESDQWRKCSDRYFPGKNGTQPTHSHLGLPSAKEKQKHPHPHHSQPATAASSEYSQHPPRPGGLQSLSDFAAARLWPVTYLYSEGPPNATEFSNFVDCNKESC
Protein: Zinc finger and BTB domain containing 16 protein (F7IXA3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
ILFHRNSQHYTLDFLSPKTFQQILEYAYTATLQAKAEDLDDLLYAAEILEIEYLEEQCLKILETIQASDDNDTEATMADGGGEEEEDRKARYLKNIFISKHSGEESGYANVAGQSLPGPMVDQSPSVSTSFGLSAMSPTKAAVDSLMTIGQSLLQGALQPPAGPEEPTLAGGGRHPGVAEVHMEMMQVDEAPGQDSPGAAESSVSGGMGDKLEERSKEGPGTPTRGSVITSARELHYGREESGEQLSPPVEAGQGPPGRQESLAPPVEKHLGIYSVLPNHKADAVLSMPSSVTSGLHVQPALAVSMDFSTYGGLLPQGFIQRELFSKLGELAVGMKAESRPLGEQCSVCGVELPDNE
Protein: Smr domain-containing protein C11H11.03c (Q9UTP4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MEEYEKFRALASKEAEKRGYLFQEAQHAYSAGNKAKAHELSQEGKLCGERMENYNRQAASAIYLYKNSQCNPDEIDLHGLYIDEAVQAVQQRIENCIRRGDNHLHIIVGRGNHSANHVEKLRPAIVRMLEQQSIKYNSEVNEGRIYVYLPSATSPIQPNFNCIQEPQEAYSRPQHSTLTDQVEPEKIVEEIATNCFPRLKTCCAIM
Protein: Follistatin-related protein 3 (Follistatin-like protein 3) (Follistatin-related gene protein) (O95633)
Organism: Homo sapiens (Human)
Function: Isoform 1 or the secreted form is a binding and antagonizing protein for members of the TGF-beta family, such us activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiationc. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. Isoform 2 or the nuclear form is probably involved in transcriptional regulation via interaction with MLLT10.
Subcellular location: [Isoform 1]: Secreted.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Note=Although alternative initiation has been demonstrated and resulted in different localization, the major source of nuclear FSTL3 appears not to depend on translation initiation at Met-27 according to. {ECO:0000269|PubMed:16150905}.
Interaction partners:
- Growth/differentiation factor 8
- Inhibin beta A chain
- Growth/differentiation factor 11
- Inhibin beta B chain
- Bone morphogenetic protein 2
Sequence:
MRPGAPGPLWPLPWGALAWAVGFVSSMGSGNPAPGGVCWLQQGQEATCSLVLQTDVTRAECCASGNIDTAWSNLTHPGNKINLLGFLGLVHCLPCKDSCDGVECGPGKACRMLGGRPRCECAPDCSGLPARLQVCGSDGATYRDECELRAARCRGHPDLSVMYRGRCRKSCEHVVCPRPQSCVVDQTGSAHCVVCRAAPCPVPSSPGQELCGNNNVTYISSCHMRQATCFLGRSIGVRHAGSCAGTPEEPPGGESAEEEENFV
Protein: Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose reductase (EC 1.1.1.333) (Decaprenyl-phospho-2'-keto-D-arabinose reductase) (Decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase) (Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE2) (Decaprenyl-phosphoribose 2'-epimerase subunit 2) (NAD-dependent decaprenylphosphoryl-D-2-keto-erythropentose reductase) (P9WGS9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans. DprE1 catalyzes the first step of epimerization, namely FAD-dependent oxidation of the C2' hydroxyl of DPR to yield the keto intermediate decaprenyl-phospho-2'-keto-D-arabinose (DPX). The intermediate DPX is then transferred to DprE2 subunit of the epimerase complex, most probably through a 'substrate channel' at the interface of DprE1-DprE2 complex. DprE2 then catalyzes the second step of epimerization, the NAD(+)-dependent reduction of DPX that leads to the formation of DPA. Appears to be essential for the growth and survival of M.tuberculosis.
Subcellular location: Periplasm {ECO:0000305|PubMed:25906160}.
Interaction partners:
- Decaprenylphosphoryl-beta-D-ribose oxidase
- Arabinogalactan biosynthesis recruiting protein Rv3789
- Probable arabinosyltransferase C
- Galactan 5-O-arabinofuranosyltransferase
- Probable arabinosyltransferase A
- Probable arabinosyltransferase B
- Decaprenyl-phosphate phosphoribosyltransferase
- Decaprenylphosphoryl-5-phosphoribose phosphatase
- Uncharacterized protein Rv3788
Sequence:
MVLDAVGNPQTVLLLGGTSEIGLAICERYLHNSAARIVLACLPDDPRREDAAAAMKQAGARSVELIDFDALDTDSHPKMIEAAFSGGDVDVAIVAFGLLGDAEELWQNQRKAVQIAEINYTAAVSVGVLLAEKMRAQGFGQIIAMSSAAGERVRRANFVYGSTKAGLDGFYLGLSEALREYGVRVLVIRPGQVRTRMSAHLKEAPLTVDKEYVANLAVTASAKGKELVWAPAAFRYVMMVLRHIPRSIFRKLPI