wanglab/gogpt-training-data huggingface dataset:
Protein: Probable ATP-dependent RNA helicase DDX5 (EC 3.6.4.13) (DEAD box protein 5) (RNA helicase p68) (P17844)
Organism: Homo sapiens (Human)
Function: Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms.
Subcellular location: Nucleus {ECO:0000269|PubMed:22034099}. Nucleus, nucleolus {ECO:0000269|PubMed:10837141, ECO:0000269|PubMed:1996094}. Nucleus speckle {ECO:0000269|PubMed:24644279}. Cytoplasm {ECO:0000269|PubMed:22034099}. Note=During the G0 phase, predominantly located in the nucleus. Cytoplasmic levels increase during the G1/S phase. During the M phase, located at the vicinity of the condensed chromosomes. At G1, localizes in the cytoplasm. {ECO:0000269|PubMed:22034099}.
Interaction partners:
- Ribonuclease 3
- Cellular tumor antigen p53
- ATP-dependent RNA helicase A
- Probable ATP-dependent RNA helicase DDX17
- Microprocessor complex subunit DGCR8
- Estrogen receptor
- RNA-binding protein 39
- Mothers against decapentaplegic homolog 3
- Heterogeneous nuclear ribonucleoprotein H
- Histone deacetylase 1
Sequence:
MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ
Protein: H(+)/Cl(-) exchange transporter ClcA (ClC-ec1) (P37019)
Organism: Escherichia coli (strain K12)
Function: Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Fluoride-specific ion channel FluC
- Inner membrane protein RclC
Sequence:
MKTDTPSLETPQAARLRRRQLIRQLLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWLQNQRMGALVHTADNYPLLLTVAFLCSAVLAMFGYFLVRKYAPEAGGSGIPEIEGALEDQRPVRWWRVLPVKFFGGLGTLGGGMVLGREGPTVQIGGNIGRMVLDIFRLKGDEARHTLLATGAAAGLAAAFNAPLAGILFIIEEMRPQFRYTLISIKAVFIGVIMSTIMYRIFNHEVALIDVGKLSDAPLNTLWLYLILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGGLCGLLGFVAPATSGGGFNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPMLALGTVLGTAFGMVAVELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQLILPMIITGLGATLLAQFTGGKPLYSAILARTLAKQEAEQLARSKAASASENT
Protein: Nup98 (A1YK33)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
Sequence:
KLSSEADATRATNPAAQQAVLDLTSNQYKISTSNNPAPMKVKTLGSTLNRKSLFDGLEEFDASVEGFNLKPSAKRLVIKPKVKSVEGGNPSSSIGSAPNTPQSRPKGATPNKERESFSGAIPSEPLPPAGNSPGATNGRESQDNGRRESWLHPNNLEKVRQHNIQTGMDQGSPHNSTLNELVPRKPLDTYRPSSTVRLSVSTIPENPFEDQSSTITRRETFTSQQANESVLSNRSNEAEDSAANRSRLAIEAAAAEAADDESHPTGIVLRRVGYYTIPSLDDLRSYLAEDGSCVVPNFTVGREGYGNVFFGKEMDVAGLNLDEIVHFRNKEIIIYPDDENKPPIGQDLNRDAQVTLDQVWPLDKTKHEAIKDPQRLLEMDWEGKLRRVCDKNDTRFIEYRPETGSWVFRVKHF
Protein: Cytochrome b-c1 complex subunit 1, mitochondrial (Complex III subunit 1) (Core protein I) (Ubiquinol-cytochrome-c reductase complex core protein 1) (Q9CZ13)
Organism: Mus musculus (Mouse)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (By similarity). The 2 core subunits UQCRC1/QCR1 and UQCRC2/QCR2 are homologous to the 2 mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-MPP respectively, and they seem to have preserved their MPP processing properties. May be involved in the in situ processing of UQCRFS1 into the mature Rieske protein and its mitochondrial targeting sequence (MTS)/subunit 9 when incorporated into complex III (By similarity). Seems to play an important role in the maintenance of proper mitochondrial function in nigral dopaminergic neurons (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 9
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 10
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 8
Sequence:
MAASAVCRAACSGTQVLLRTRRSPALLRLPALRGTATFAQALQSVPETQVSILDNGLRVASEQSSHATCTVGVWIDAGSRYETEKNNGAGYFLEHLAFKGTKNRPGNALEKEVESIGAHLNAYSTREHTAYLIKALSKDLPKVVELLADIVQNSSLEDSQIEKERDVILREMQENDASMQNVVFDYLHATAFQGTPLAQAVEGPSENVRRLSRTDLTDYLNRHYKAPRMVLAAAGGVEHQQLLDLAQKHLSSVSRVYEEDAVPGLTPCRFTGSEIRHRDDALPLAHVAIAVEGPGWANPDNVTLQVANAIIGHYDCTYGGGVHLSSPLASVAVANKLCQSFQTFNISYSDTGLLGAHFVCDAMSIDDMVFFLQGQWMRLCTSATESEVTRGKNILRNALVSHLDGTTPVCEDIGRSLLTYGRRIPLAEWESRIQEVDAQMLRDICSKYFYDQCPAVAGYGPIEQLPDYNRIRSGMFWLRF
Protein: Steroid receptor seven-up, isoforms B/C (Nuclear receptor subfamily 2 group F member 3, isoforms B/C) (P16375)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor that is required in photoreceptors R1, R3, R4 and R6 during eye development; generation of the ganglion mother cell-2 (GMC-2) fate in the nb7-3 lineage, coinciding with the transition in the expression of HB to KR in the neuroblasts (NBs).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
Sequence:
MCASPSTAPGFFNPRPQSGAELSAFDIGLSRSMGLGVPPHSAWHEPPASLGGHLHAASAGPGTTTGSVATGGGGTTPSSVASQQSAVIKQDLSCPSLNQAGSGHHPGIKEDLSSSLPSANGGSAGGHHSGSGSGSGSGVNPGHGSDMLPLIKGHGQDMLTSIKGQPTGCGSTTPSSQANSSHSQSSNSGSQIDSKQNIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTYSCRGSRNCPIDQHHRNQCQYCRLKKCLKMGMRREAVQRGRVPPTQPGLAGMHGQYQIANGDPMGIAGFNGHSYLSSYISLLLRAEPYPTSRYGQCMQPNNIMGIDNICELAARLLFSAVEWAKNIPFFPELQVTDQVALLRLVWSELFVLNASQCSMPLHVAPLLAAAGLHASPMAADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTTDACGLSDVTHIESLQEKSQCALEEYCRTQYPNQPTRFGKLLLRLPSLRTVSSQVIEQLFFVRLVGKTPIETLIRDMLLSGNSFSWPYLPSM
Protein: Anaphase-promoting complex subunit hcn1 (20S cyclosome/APC complex protein hcn1) (Chaperone-like protein hcn1) (High copy suppressor of cut9 protein 1) (O13916)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Has a role in assembling cut9 in the 20S APC/cyclosome.
Interaction partners:
- Anaphase-promoting complex subunit cut9
- Anaphase-promoting complex subunit 4
- Mitotic spindle checkpoint component mad3
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 3
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 13
- Anaphase-promoting complex subunit 11
Sequence:
MLRRNPTAIQITAEDVLAYDEEKLRQTLDSESTTEEALQKNEESTRLSPEKKKIIRERRIGITQIFDSSMHPSQGGAAQS
Protein: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase) (Q20117)
Organism: Caenorhabditis elegans
Function: Plays a role in resistance to arsenite. May play a role in the oxidative stress response induced by reactive oxygen species produced during infection by pathogenic bacteria. Together with trxr-1, required for the reduction of disulfide groups in the cuticle during molting.
Interaction partners:
- GCS light chain
- Glutathione synthetase
- 5-oxoprolinase
- Aminopeptidase
- Glutathione reductase, mitochondrial
- Glutathione S-transferase 4
- Protein skinhead-1
- Gamma-glutamyltranspeptidase 1
- Gamma-glutamyltranspeptidase 1
- Gamma-glutamyltranspeptidase 1
Sequence:
MGLLTKGSPLTWAETVPHIDYIKKHGIAQFINLYHRLKSRHGDQLKWGDEIEYTIVKFDDANKKVRVSCKAEELLNKLQAEEQVNAMLGTANRFLWRPEFGSYMIEGTPGMPYGGLIACFNIVEANMKLRRQVVKKLLKKDETCLSISFPSLGVPGFTFPEVAADRKNDDAANSVFWPEQAVFLGHPRFKNLTKNIKGRRGSKVAINVPIFKDTNTPSPFVEDLSALGGPDDTRDAKPDHIYMDHMGFGMGCCCLQVTFQAVNVDEARWLYDQLTPITPILLALSAATPIFRGKLSNVDSRWDIISASVDDRTPEERGLEPLKNSKWVIDKSRYDSTDCYIYPCSVGYNDIPLQYDETIYKQLIDGNIDEPLAKHIAHMFIRDPHQVFRERIEQDDEKSSEHFETIQSSNWMNMRFKPPPPDAPEIGWRVEFRPTEVQLTDFENAAYCCFVVLLTRMMISFRLTYLMPISMVTENMKRAQQKDAVLNQKFLFRKGLAECKSAPENLKGSEKCGPPSQDIEEMSIDEIINGKKNGFPGLISLIRQFLDSADVDVDTRCTISQYLNFISKRATGEINTLAHWTRGFVQSHPAYKHDSDVNDNIVYDLLKKMDAISNGEDHCEKLLGCYRSKTDHAISAAVRKAEEHMIVSSQKRAH
Protein: GRB2-associated-binding protein 2 (GRB2-associated binder 2) (Growth factor receptor bound protein 2-associated protein 2) (pp100) (Q9UQC2)
Organism: Homo sapiens (Human)
Function: Adapter protein which acts downstream of several membrane receptors including cytokine, antigen, hormone, cell matrix and growth factor receptors to regulate multiple signaling pathways. Regulates osteoclast differentiation mediating the TNFRSF11A/RANK signaling. In allergic response, it plays a role in mast cells activation and degranulation through PI-3-kinase regulation. Also involved in the regulation of cell proliferation and hematopoiesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19172738}. Cell membrane {ECO:0000269|PubMed:19172738}. Membrane raft {ECO:0000250|UniProtKB:Q9Z1S8}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 11
- Growth factor receptor-bound protein 2
- SHC-transforming protein 1
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Son of sevenless homolog 1
- Son of sevenless homolog 2
- Epidermal growth factor receptor
- Tyrosine-protein kinase Lyn
- Tyrosine-protein kinase SYK
- Tyrosine-protein kinase Fyn
Sequence:
MSGGGDVVCTGWLRKSPPEKKLRRYAWKKRWFILRSGRMSGDPDVLEYYKNDHSKKPLRIINLNFCEQVDAGLTFNKKELQDSFVFDIKTSERTFYLVAETEEDMNKWVQSICQICGFNQAEESTDSLRNVSSAGHGPRSSPAELSSSSQHLLRERKSSAPSHSSQPTLFTFEPPVSNHMQPTLSTSAPQEYLYLHQCISRRAENARSASFSQGTRASFLMRSDTAVQKLAQGNGHCVNGISGQVHGFYSLPKPSRHNTEFRDSTYDLPRSLASHGHTKGSLTGSETDNEDVYTFKTPSNTLCREFGDLLVDNMDVPATPLSAYQIPRTFTLDKNHNAMTVATPGDSAIAPPPRPPKPSQAETPRWGSPQQRPPISENSRSVAATIPRRNTLPAMDNSRLHRASSCETYEYPQRGGESAGRSAESMSDGVGSFLPGKMIVGRSDSTNSEDNYVPMNPGSSTLLAMERAGDNSQSVYIPMSPGAHHFDSLGYPSTTLPVHRGPSRGSEIQPPPVNRNLKPDRKAKPTPLDLRNNTVIDELPFKSPITKSWSRANHTFNSSSSQYCRPISTQSITSTDSGDSEENYVPMQNPVSASPVPSGTNSPAPKKSTGSVDYLALDFQPSSPSPHRKPSTSSVTSDEKVDYVQVDKEKTQALQNTMQEWTDVRQSSEPSKGAKL
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y (Phosphatidylinositol-glycan biosynthesis class Y protein) (PIG-Y) (Q3MUY2)
Organism: Homo sapiens (Human)
Function: Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis. May act by regulating the catalytic subunit PIGA.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16162815}; Multi-pass membrane protein {ECO:0000269|PubMed:16162815}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Dolichol phosphate-mannose biosynthesis regulatory protein
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Protein preY, mitochondrial
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- GPI alpha-1,6-mannosyltransferase 2
Sequence:
MFLSLPTLTVLIPLVSLAGLFYSASVEENFPQGCTSTASLCFYSLLLPITIPVYVFFHLWTWMGIKLFRHN
Protein: Calmodulin-binding transcription activator, isoform I (A0A0B4LF15)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MENVPDISTSASSSSTSNSTSTLKLQSQITSKNVLIRSQSSGKLSSNEAKSAKPAATTSTTTTLRAAKLKIGAMQQQKQQHQQQHQATSGGNIILLRGTRNENGQIIIQNKQDILSLLSEQQQQQQQEKSHSSTAITLNQLPTATTVARKTIVQGSSGAGSSSSSSSSTISIVANSNNKEASSNTILLQTPINASQLESVLKAQERSKQANATQTKMVERPFMLKHATRSLSSESNCDSKSPFVLQTLKRLEKSQSILVIRNSTASTAATNTSMATSPPNGNSLATSSILSVTRTTKAAKGVAGALHKLKAAAATTATSGGASSAGATSSTATTILRLGKSATTVAINGASKLEATTSTTTAVPVPATATTSNKLSNAVTSEQQQQQQQQSTTTQTNVPLGNDGEPIKLPDNLESLPRADSFPSQRHRWNTNEEIAAILISFDKHGEWQSKEVRTRPKSGSLLLYSRKKVRYRRDGYCWKKRKDGKTTREDHMKLKVQGTECIYGCYVHSAILPTFHRRCYWLLQNPDIVLVHYLNVPYPDDNKMAVIAPSITLWGDKKEWTKEELVSQLKPMLSTINSDDDSDSGNDIEISTAETVESIVCQLMEKQRLSRQAALVKQLDCGCGDGGCVDGKTCTHPVMRRSAAMLKSSVQEKRLGEPFNGNTPNVVVASKLYSRWAERPRQHVDNHGQFHNVTQQLPQESAIKFQIIPPQQQQQQDGNYQQQQYRGGSQMLAARSNLVMQQQQQHQQQQQYHQQQQQQQQQQQQHQQQQQHLSLQRFVASQGQNSVHLNQQHRLQIANTTITATASDPATTLAAAAAVAAASGATPVALNIMDTELIENQNHMTANKITNSGSSNSSSSNASKQLAGQTNNKLNVVNNNDPGNNNFMYNQQQQLNASSNSNNSSQQQQQQQQQHYYKLQQTTATPTSGQPPPLAQVQPHSLAQPPVEAMCMSPEHRSSSQPTPATSSAGSIPSSVSVSISVSTSTPTPAPTSISTPTSGTSSTSSSLQSIIDGNQQQQITTTSTAATCDNLMSANALSEDSHTVNNQATEAPNRSQLQSQSQSLSLNQNGCATYSASSDNSSQISDESSSFGGNNQNSSNSSTSEEEPQVEALSFFNETLDLSQEDIQRTLIANMPYNTTAAGATAPSTTITTGNTKLELSQQETKEKPAMGTETATEIEDDETDDVFANLDAFDMLVEFPELDLDDKQALNNTALEQSSFLGESAPSQPRKVHNICDFSPEWSYTEGGVKVLVAGPWTSSNGGAYTVLFDAQPVPTQLVQEGVLRCYCPAHEAGFVTLQVACGGFLVSNSVMFEYKLSLLADAPFDATSSNDCLYKFTLLNRLSTIDEKLQVKTEHELTTDNTALYLEPNFEEKLVAYCHKLIKHAWSMPSTAASWTVGLRGMTLLHLAAALGYAKLVGAMLNWRSENPHIILETELDALSQDVYGFTPLAWACVRGHVECSLLLYKWNHNALKIKTQAQQTPLDLASMRGHKVLLAQMYRLEKERCRKPQLRGGLANLSMNMGVEAEAEEQHQSFSAFDLELQRKHDGVFLRPVAVHSNQSPPNGSSRYSKRSSIDSGINMDIRSKSGKPLARLHSNFESHDSYALGVDSPLDSLTGTNCLLSPLRKMDFALWDSDAKVLTLAEHIIAAMPERIKNEADEMMVLGSPLTEPLTSESSALTDSFMDPLLDSLPNTHFDSDFSFDFHDHSYRYHDVSTPCSSLSPASSGPLQSPASYSILGTDPSVSSPSPPPSTKQLTEFLHASSISSYPFEADFSKLTLTDTEQRELYEAAKCIQKAYRSYKGRQKLEEQNKERSAATVIQNYYRRYKQYAYYRQMTNAALVIQHGYRSYRRNKRFKKSGLCLSSSSDHGSVSSNSQCLSSFYDHYKQDQQQLHELGSQPSTPKETSPSGPLKRTYSQSTQNQAARKIQQFMRQSRINIWDGNLAIVTTERASRKREAGAPTQGGIPSKLAVSRAAGNVGLPRK
Protein: Inhibin alpha chain (P05111)
Organism: Homo sapiens (Human)
Function: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subcellular location: Secreted.
Interaction partners:
- Activin receptor type-2A
- Activin receptor type-2B
- Inhibin beta A chain
- Transforming growth factor beta receptor type 3
- Inhibin beta B chain
- Intestinal-type alkaline phosphatase
- Zinc finger protein GLIS3
- Bone morphogenetic protein 15
- Inhibin beta C chain
Sequence:
MVLHLLLFLLLTPQGGHSCQGLELARELVLAKVRALFLDALGPPAVTREGGDPGVRRLPRRHALGGFTHRGSEPEEEEDVSQAILFPATDASCEDKSAARGLAQEAEEGLFRYMFRPSQHTRSRQVTSAQLWFHTGLDRQGTAASNSSEPLLGLLALSPGGPVAVPMSLGHAPPHWAVLHLATSALSLLTHPVLVLLLRCPLCTCSARPEATPFLVAHTRTRPPSGGERARRSTPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIPPNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI
Protein: Glycine cleavage system P protein (EC 1.4.4.2) (Q57V19)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU364056}.
Interaction partners:
- Glycine cleavage system H protein
- Aminomethyltransferase
- Dihydrolipoyl dehydrogenase
- Dihydrolipoamide dehydrogenase, point mutation
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoamide dehydrogenase, putative
- 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic, putative
- NAD-specific glutamate dehydrogenase
- glutamine synthetase
Sequence:
MYRSAFRSLRCSTVKYARWSAAGNYVNRHVGPTAADTEVMLQMIGKKTISDLMADAIPAELMRPPMKEIEPLSEKDALSSVLSLGARNRVLKSMIGQGYYECITPSVLLRNVIENPGWYTPYTPYQAEISQGRLESLLNFQTMITDLTKMDVANASLLDQATACAEAMYLAFRHHNRKRDTFFVSKDVFPSCIEMIKTRAEPLKIKVVVDDPALFDWGEVSPCGMLVQNPDANGTVHDFTELFQKAKDHGVLCCCGADLMASLLIKPPGEMGADVVVGTSQRFGIPLGYGGPHAAFFAAKEQFKRLVPGRIVGVSKDVAGDPAIRMALQTREQHIKRERATSNICTAQALLATVSAFYAVYHGPGGLTDIANEIHQKAKTLAVGMESAGHSVVNTTFFDTLTFNLKGITPEDYASQCNEKGINVFLDYGTGTVSISVDEATTETHIMSLLEAAGLKLPVFAALTKIGRNKTAFPEALARTSSFLQHSVFCKYRSEGELMRYIHRLQRKDYGLTHGCIPLGSCTMKLNPASAMLPLSWGTFTNLHPLAPSDQVQGYSAMCFDLEQKIRDVTGLDAVSLQPNSGAQGEYAGLRVVRAYHQSKGEGQRNVCLIPVSAHGTNPASAVLAGMKVVTLKCLEDGRIDVEDLKQLCEKHSKELSCIMLTYPSTYGLFDRDILSVTSLVHQHGGQCYIDGANLNAMVGYTGPGFIGGDLCHINLHKTFSIPHGGGGPGMGPIAVRQHLAPFLPNSVLRQKVGGSQSFGQVSQAAYGSASILTVSYMLMLMLGTRGMKVCTEHAILNANYLKKRLEKHYRIMFLGEEDLCAHEFIIDLRPFKKSAEVEAEDVSKRLMDYGIHSPTVAFPIPGTLMIEPTESESKQELDRLADALISIRGEIAAIERGEQDKTNNVLKNAPHTAKCVTAENWDRPYSRRTAAFPAPHSNIEKYWPTVGRIDGAYGDRHLMCNCMSLDSFK
Protein: Oral-facial-digital syndrome 1 protein-like (G3I183)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Interaction partners:
- Serine/threonine-protein kinase PLK
- Pericentrin
- Coiled-coil domain-containing protein 41
- Centrosomal protein of 120 kDa
- Pericentriolar material 1 protein
- Kinesin light chain
- C2 domain-containing protein 3
- Centrosomal protein of 192 kDa
Sequence:
MSLKCDVLSQDELRKKLYQTFKDRGILDTLKTQLRNQLIHELMHPVLSGEVKPPSIPVEGSALLIGASNSLVADHLQRCGYEYSLSVFFPESGLAKEKVFTMQDLLQLIRINPSSSLYKSLISGFDKENKKGFLMSFLKELAEYHQAKESCDMETQTSATFPSKVSLAEKFQLIDDEFADAIPHRPKLESLETKLNEYKKEIQHQLQVEMCQKLKYFREAEITKVKMEEKRKYEKELAEFRNEFERIYQAKNEALISQEKNTLERIKKHREIETKEIYAQRQLLLNDIDLLRGREAELKERIEAFELTQKLQEEKNKSEAEAIQRREQNLKNIEETYDQKLKTELLKYQLELKDEYIARTNKLLEEERKTKEKTIHLQEELTIINSKKEELSKSVNRMKEVELELESVKAQFLAMSKQNHLLNEKMKEMSDYSLLKEEKVELQAQNKLLKQQLEENRNENLRLLDRITQPPPELLVFQKELQKAEHTVALEHKEFEMQRQALQKQLQSEIEHSTQLKGQILEYDASVKRLTIQVADLKSQLKQTQTALENEVFRNPKQSLPLHSLSGLVSGKMAPHNGDTRGDFLNVPLEQNKVMAGAVKSRILPYANTAAEASSPDSDLEFVASSTKAKVRELEQEAERLEKAFRNYHRRVTRDPNMSPQPAKSPPSAYSIGVRRSTASSSMDRHVSAEDRVVSEQPLVDMVKEEKHDVSKAFMGSVASRPRRTSSSVRLSSTPHPKSRRSLDNEMYLEGLGRLHIASSSPCLDRADGSHVASSSPCPDRTTAQPSPIQSRHSFSGPSLSSAQEKNACFYQRLTEAQDKSEFSNVDKQSLKDKEECEPPFRWNKPEAEGLHPAGDMPVMDVAAAAVPSRPISYDYPNVDESQTGEQMEEQQQWELHMKERRKREEQRQNERQEALERERRELEKLEQERVMCHLNLCTSCFSDTFSKDLELRDVSQ
Protein: Ornithine transcarbamylase, mitochondrial (OTCase) (EC 2.1.3.3) (Ornithine carbamoyltransferase, mitochondrial) (P00481)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P00480}.
Interaction partners:
- Argininosuccinate synthase
- Carbamoyl-phosphate synthase, mitochondrial
- Arginase-1
- Arginase-2, mitochondrial
- 1,4-alpha-glucan branching enzyme
- N-acetylglutamate synthase, mitochondrial
- Multifunctional protein CAD
- Aminoacylase-1A
- Ornithine aminotransferase, mitochondrial
- Argininosuccinate lyase
Sequence:
MLSNLRILLNKAALRKAHTSMVRNFRYGKPVQSQVQLKGRDLLTLKNFTGEEIQYMLWLSADLKFRIKQKGEYLPLLQGKSLGMIFEKRSTRTRLSTETGFALLGGHPSFLTTQDIHLGVNESLTDTARVLSSMTDAVLARVYKQSDLDILAKEATIPIVNGLSDLYHPIQILADYLTLQEHYGSLKGLTLSWIGDGNNILHSIMMSAAKFGMHLQAATPKGYEPDPNIVKLAEQYAKENGTRLSMTNDPLEAARGGNVLITDTWISMGQEDEKKKRLQAFQGYQVTMKTAKVAASDWTFLHCLPRKPEEVDDEVFYSPRSLVFPEAENRKWTIMAVMVSLLTDYSPVLQKPKF
Protein: Ribosome production factor 1 homolog (X6R7Q1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAKAGDKSSSSGKKSLKRKAAAEELQEAAGAGDGATENGVQPPKAAAFPPGFSISEIKNKQRRHLMFTRWKQQQRKEKLAAKKKLKKEREALGDKAPPKPVPKTIDNQRVYDETTVDPNDEEVMLEVLN
Protein: Citrate synthase, mitochondrial (EC 2.3.3.1) (Citrate (Si)-synthase) (Q9CZU6)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P00889}.
Interaction partners:
- Aconitate hydratase, mitochondrial
- Malate dehydrogenase, mitochondrial
- ATP-citrate synthase
- Cytoplasmic aconitate hydratase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate carboxylase, mitochondrial
- Malate dehydrogenase, cytoplasmic
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Acetyl-coenzyme A synthetase, cytoplasmic
Sequence:
MALLTAATRLLGAKNSSCLVLAARHASASSTNLKDVLSNLIPKEQARIKTFKQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQMPTEEQVSWLSREWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGMNRAKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSRLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVAQLYKIVPNILLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLMKFVDSK