wanglab/gogpt-training-data huggingface dataset:
Protein: Formate hydrogenlyase subunit 4 (FHL subunit 4) (Hydrogenase 3 component D) (P16430)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Formate hydrogenlyase subunit 6
- Formate hydrogenlyase subunit 2
- Formate hydrogenlyase subunit 3
- Formate hydrogenlyase subunit 7
- Formate hydrogenlyase subunit 5
- Formate dehydrogenase H
- Hydrogenase 3 maturation protease
- Formate hydrogenlyase maturation protein HycH
- Hydrogenase-4 component G
- Hydrogenase-4 component E
Sequence:
MSVLYPLIQALVLFAVAPLLSGITRVARARLHNRRGPGVLQEYRDIIKLLGRQSVGPDASGWVFRLTPYVMVGVMLTIATALPVVTVGSPLPQLGDLITLLYLFAIARFFFAISGLDTGSPFTAIGASREAMLGVLVEPMLLLGLWVAAQVAGSTNISNITDTVYHWPLSQSIPLVLALCACAFATFIEMGKLPFDLAEAEQELQEGPLSEYSGSGFGVMKWGISLKQLVVLQMFVGVFIPWGQMETFTAGGLLLALVIAIVKLVVGVLVIALFENSMARLRLDITPRITWAGFGFAFLAFVSLLAA
Protein: Armadillo repeat-containing X-linked protein 4 (Q5H9R4)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
Sequence:
MGRIQEVGWVTAGLVIWAGTCYYIYKFTKGRAQSVRTLARNGSTVKMETVVGVQSQTLAINEAEIKTKPQVEIGAETGARSGPRAEVETKATAIAIHRANSQAKAMVGAEPETQSESKVVAGTLVMTEAVTLTEVKAKAREVAMKEAVTQTDAEAGKIVKKEAVTQTKAKAWALVAKTEAKREAMTQTKAETHILAEKETEINRVMVTQSETLAVPREVAKMGATNKTGIVDETKTRALEETVSVAKTQSEARPGATVDARGNPNGMSREVAGVDMKSCAQSQAVTKIQGDDMPGTGVEDMGNCKTMSRAESGADTRASAQPQIFAKTQTEAIPGAKIDAGGNTNAMCKVGAGADVRACIQPQTVAKKQAEVTSGARVDGRGNTNVISKAITGADMRAAAQPQAVASTHAEAMSDAKVKNRGNPNAMTKAGAKANLRANSQVEALPDARDKSRGNPNVMAKVGDGTDMLSCTQPQLVASVQADTLSDGKIKVRGNVNTMPKEGAGVDMKAQGMAQSQGEALPNTRGKARGKAKAKCKTGPGMDMKTCTQPQAGVKTPAEALLDSRVDGRGNPNATSKAGTKADQRVCGQPLVVANPQGEALPGAKNKVKGNPHTVLKVGAGEGTTDSAQPEAVVSFQGEALLGTKNKVKGNPNVVLKAEVGEGAMGTAQLQIMASSKGEALLDSKNKVKGNSNAVSKAGAGTDTTGSVQPQIVANSQGEVLPGAKNKIRGNPTTVPNSGVGPYTTDSARLQAVANSQGEVLPGAKNKVKANLNAVSKAEAGMGATGSVQPQAVANSHCETLPGAKNKVRGNWNAVSKAGAGMDTRGSAQPQAVANSQGEVLPGAKNKVKGNPNVVSKAGAREDTVGSTQPQVLASSQRETLPGARNKVKGNSNVVSKAGAREDTMGSAQPQVVANSQRETLPGARNKVKGNSNAISKAEAGAGIMGSVQVQVVASFQGEVLPGAKNKVRGNSNAVPKAEAGADTVGSAQPQAVANSQSETLLGARNKVKGNTIAVPKAGTGAGTRHSAQPQIVAGSQGETLPGARDKSMSTSEAEATAEDEAYAKPEAEAMPTSESEGGSGTQACRKTQPNIHDYYWNGIGVEDWIAAERWIKFRFQTMDGDWENSVSWADDENEASIGSWSGASDKAGIIRSWAVACDETSVKSWAGARAENVVGIGTWARAGEQASGGLWAGGQTSEGTWAGDKASGGAWTGAENQASGGSWALAGNQAIGELWAAGQASDGSWPGGQASGVSWVGEEAIGGSWTGAENQASEGSWAGAGAGNMSSVSYWAGVVDQAGGGSWAGTSDQSGGGSKPRFEDQASGEGSWAGAGGQASGGSMLGPEDQSSGRSWADTADQASGGSRLGHVDQSSGGAWAGTLDQSGGGSKPRFENQTTEEGSWAGAGGQAGGGSKVGPEDQSSGRSWANSGDQISGGFLVGIVDQANGGSWTGAGHPASVGPKPIFEDQVSGRGSWADAREQVVGDSRLGLRDQSSGDSWAGTGDQASGWFCVCPGSQTNGGSWGGASGQDVGGSRPGPTNQSSAGSWDSPGSQVSGSCWTGAGAVDQAGGCSKPGFEDQAIGGGFWPGAGDQTGGGSRPGSEDQSSGIGSWGVAGGQVLGGARPGPADQSSGGSWAGTGNQSSGRSWIGPGDQAVDCSKPEFEDQACGGGSWAGAGSQASGESWAGSRPGNEAIGGSRMGSEDQATGGSWARSEDQASGRFQVSFEVEANEGFWFGPGAEAVIGSWCWTEEKADIVSRPDDKDEATTASRSGAGEEAMICSRIEAENKASSGSWIRSEEVAYMGSCVGAEAGAGAEAGAGAEAGAGAGAEAGAEAGAGAGAGPGTESGAGIWSWDGDATTVESRLGAGEEAGVESWTLARNVGEDELSRESSPDIEEISLRSLFWAESENSNTFRSKSGKDASFESGAGDNTSIKDKFEAAGGVDIGSWFCAGNENTSEDKSAPKAKAKKSSESRGIYPYMVPGAGMGSWDGAMIWSETKFAHQSEASFPVEDESRKQTRTGEKTRPWSCRCKHEANMDPRDLEKLICMIEMTEDPSVHEIANNALYNSADYSYSHEVVRNVGGISVIESLLNNPYPSVRQKALNALNNISVAAENHRKVKTYLNQVCEDTVTYPLNSNVQLAGLRLIRHLTITSEYQHMVTNYISEFLRLLTVGSGETKDHVLGMLLNFSKNPSMTKDLLIANAPTSLINIFSKKETKENILNALSLFENINYHFKRRAKAFTQDKFSKNSLYFLFQRPKACAKKLRALAAECNDPEVKERVELLISKL
Protein: Blood group Rh(D) polypeptide (RHXIII) (Rh polypeptide 2) (RhPII) (Rhesus D antigen) (CD antigen CD240D) (Q02161)
Organism: Homo sapiens (Human)
Function: May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1544931, ECO:0000269|PubMed:3142870}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSSKYPRSVRRCLPLWALTLEAALILLFYFFTHYDASLEDQKGLVASYQVGQDLTVMAAIGLGFLTSSFRRHSWSSVAFNLFMLALGVQWAILLDGFLSQFPSGKVVITLFSIRLATMSALSVLISVDAVLGKVNLAQLVVMVLVEVTALGNLRMVISNIFNTDYHMNMMHIYVFAAYFGLSVAWCLPKPLPEGTEDKDQTATIPSLSAMLGALFLWMFWPSFNSALLRSPIERKNAVFNTYYAVAVSVVTAISGSSLAHPQGKISKTYVHSAVLAGGVAVGTSCHLIPSPWLAMVLGLVAGLISVGGAKYLPGCCNRVLGIPHSSIMGYNFSLLGLLGEIIYIVLLVLDTVGAGNGMIGFQVLLSIGELSLAIVIALMSGLLTGLLLNLKIWKAPHEAKYFDDQVFWKFPHLAVGF
Protein: Putative F-box protein At5g15660 (Q9LFW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable pectinesterase/pectinesterase inhibitor 64
- Disease resistance protein RBA1
- Probable poly
- Pectinesterase inhibitor 2
- Uncharacterized protein At5g39865
- Trafficking protein particle complex subunit
- GDSL esterase/lipase At1g58725
- Folylpolyglutamate synthase
- Folylpolyglutamate synthase
- Poly
Sequence:
MRRRSKKIKTENNSNPETSEERNKFDEIPHDLVIEILERLPLKSVARFLTVSKLWATTIRSPDFRKSYRGGSSSEPRTLIVSDLNFKEPNPKLHFFRPSISSPSFLSSLTCPFTYPRHEEYYYHHVNGLISVGYGTDQIVINPTTGKFITLPRPKTRRKLVISFFGYDSVSDQYKVLCMTERLRGHPEEASSQHQVYTLGAKQKSWKMINCSIPHRPWSWNAVCINGVVYYIAKTGEGMFRRCLMRFDLKSDNLDLCTILPEEIQTSLHDYFLINYKGKVAIPNQPNFYTYDVWVMNQEGGKIEWLKNITFTIKPRKGFVRYLFVTGTTHTGEFILAPTSYTDEFYVFHYNPDMNSFRKIRVQAPGVKFSFAQKASVVFSDHSLLRLDNLHIRGSTHTATGEFILAPRFYSDDLNVIHFNPDTNSFRSTKVEVYEDYE
Protein: Prolactin-releasing peptide receptor (PrRP receptor) (PrRPR) (G-protein coupled receptor 10) (Q6VMN6)
Organism: Mus musculus (Mouse)
Function: Receptor for prolactin-releasing peptide (PrRP). Implicated in lactation, regulation of food intake and pain-signal processing.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Prolactin releasing hormone
- Pro-FMRFamide-related neuropeptide FF
Sequence:
MTSLSTETTGDPDLSSGLLPASSTPANQSAEASEGNLSATVPRAAAVTPFQSLQLVHQLKGLIVMLYSIVVVVGLVGNCLLVLVIARVRRLHNVTNFLIGNLALSDVLMCAACVPLTLAYAFEPRGWVFGGGLCHLVFFLQPVTVYVSVFTLTTIALDRYVVLVHPLRRRISLRLSAYAVLGIWALSAVLALPAAVHTYHVELKPHDVSLCEEFWGSQERQRQIYAWGLLLGTYLLPLLAILLSYVRVSVKLRNRVVPGSVTQSQADWDRARRRRTFCLLVVVVVVFAVCWLPLHIFNLLRDLDPRAIDPYAFGLVQLLCHWLAMSSACYNPFIYAWLHDSFREELRKMLLSWPRKIVPHGQNMTVSVVI
Protein: Agenet domain-containing protein (F4IY86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLLTTGRKEKLSVSKGSEIEISSQEYEYGSGNVWYCVILEENLAKSKRKKLSVRHLDPLLKYDYSPPLIKTTVHRFMRPVPPPDPFPEVDFEEGDVVDAAYKGGWCSGSVVKVLGNRRFLVYLRFQPDVIELLRKDLRPHFVWKDEEWFRCEKQQLIESDFSAGKSVEVRTKVDKLGDVWAPAMVIKEDEDGTMLVKLKTLKEEEVNCTKISVSYSEIRPSPLPIGLRDYKLMENVDALVESGWCPGVVSKVLAGKRYAVDLGPNRESKEFSRLQLRPSIEWKDGIWHRKEKVSGSEESSHAVEETAASTRIRITVRTALKEKKALGTGINVRTTRSSSGAMHNPLPASFNGGDVAEAGRVSVTVNETPLFETAAQLSGELGNSLADVVMNESAPVTSQPEIAAPKEFHPSVVLGVAAAVKTQGKTTPKKKLQAMKNQKSSTNDSVGEKVSVNKRKRGQPRKFIVAEPKQKIGVSGNNSKAATIEHADMTDDDRPLASWVHTGNSSSGQSVSRTPDIGLNTVVEKHVDIVETPPGRESTMVLPFVKKSQLWKVLESMEVFKVVPQSPHFSPLLESEEECREGDAIGRMVMFSSLLEKVNNLQVDDPISSINRIDECFLKLEKHGFNVTTPRSRIAKILSIKERQTCALEELKAVEEKITENDNKRRKYEEDIVELQRQEVLMKEAKVTLDNEIARMQSQAAVLDQEVQNVDHEFQAILAAPWK
Protein: Ankyrin repeat protein SKIP35 (SKP1-interacting partner 35) (Q9M1Y3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEKEGVCDTINLSDQMYPDEPFCSEMKTETIASSQKFEGGEGSKVVFSREAPLIGKDSAGTNSGECCGCSAKKLNFKGDDDLVEKENIEQQKKLNRQERIELGRLFQGAVTSLDWELAERLIQLADPQTLNDLLCVGLDSVWFLSTKPEFQGITGLIKKIICHGAHDFTRATLRTSFLASCVSACQSRTMSLSDTVTVMAQRLHERLQECNGDEILKAEAGAKVQKFTEWALKCIGFHSRCQGAKDRVSQNSAAEIELQLSAFKMFLDLAGNHLSGRDFTEAFDAACFPLTLFSNSFDPGWASGMSATVIQGLLGMLVEGGADNVNQCFLEASRFGSTELVRVLLQIAQRNSLDVDVDLALGFASHYCKIGTMKCLVEEGNAIAFLGPLMRAAERGCMQVVQWFVKRGCRDMELCLALTAATSSCQVEVAAYLLPRVPPPVLTALSIEILKAAGERSGGSLQGVEFLLKSDFLGDSTATYSVADSIARSSEDESVPSDLKSFLQEHWSESAFEKGMRESHDDFMNFMRVLKKGESAISLRDLPAPLRVAIAYMPLYRECMKADGRLLSQRLRGQLVEAVRQLQGCAVAVVEVSQTRNLMAVLEHHLTAIFD
Protein: AP-3 complex subunit mu-1 (AP-3 adaptor complex mu3A subunit) (Adaptor-related protein complex 3 subunit mu-1) (Mu-adaptin 3A) (Mu3A-adaptin) (Q9Y2T2)
Organism: Homo sapiens (Human)
Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Subcellular location: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.
Interaction partners:
- AP-3 complex subunit delta-1
- AP-3 complex subunit beta-1
- AP-3 complex subunit sigma-1
- AP-3 complex subunit beta-2
- AP-3 complex subunit sigma-2
- AP-3 complex subunit mu-2
- AP-1 complex subunit gamma-1
- AP-2 complex subunit alpha-1
- AP-4 complex subunit epsilon-1
- AP-1 complex subunit gamma-like 2
Sequence:
MIHSLFLINCSGDIFLEKHWKSVVSQSVCDYFFEAQEKAADVENVPPVISTPHHYLISIYRDKLFFVSVIQTEVPPLFVIEFLHRVADTFQDYFGECSEAAIKDNVVIVYELLEEMLDNGFPLATESNILKELIKPPTILRSVVNSITGSSNVGDTLPTGQLSNIPWRRAGVKYTNNEAYFDVVEEIDAIIDKSGSTVFAEIQGVIDACIKLSGMPDLSLSFMNPRLLDDVSFHPCIRFKRWESERVLSFIPPDGNFRLISYRVSSQNLVAIPVYVKHSISFKENSSCGRFDITIGPKQNMGKTIEGITVTVHMPKVVLNMNLTPTQGSYTFDPVTKVLTWDVGKITPQKLPSLKGLVNLQSGAPKPEENPSLNIQFKIQQLAISGLKVNRLDMYGEKYKPFKGVKYVTKAGKFQVRT
Protein: Simjang, isoform E (M9PF79)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Chromodomain-helicase-DNA-binding protein Mi-2 homolog
- Metastasis-associated protein MTA3
- Methyl-CpG binding domain protein-like, isoform C
- Chromatin assembly factor 1 p55 subunit
- MOG interacting and ectopic P-granules protein 1
- Histone deacetylase HDAC1
- CDK2-associated protein 1, isoform B
- Chromodomain-helicase-DNA-binding protein 3
- Histone deacetylase complex subunit SAP18
Sequence:
MAKMEVDDVVDLSLGSGRDPALTITPAPPPAALSNRDLRALTANNAGLTITPSASPATNNGTTSNSSNTNSNSSSTTTTTNNNNNSSSNTNSSSANNNNNNNSINASDGVTGATSGSIGGGQDENKVQRRVLRPRTEPKSYAEAPDIVLLPARTNGRQQNGNIDSETDDEEMPPYVPIKELSHAELKEREKSLRKLRQDLRNEETKLMLLKKLKQSQQVMKENLVVTPTSVSPNNPLSAIPAALTSKGSLSVTPTSAVPLPAHSKGSRSSLSGSGGPAVSISATNSRTGSSSSAAAAASAIAAAAMSGQHRSGSNSILPPPRSSLPAGATLAAGTTITPATSSSHRSSNLPPRTNLPNLTITPSVTITPTSAPPSSLKPRNVPGTISNSVSITPALPLSQSHQNQHNDQKNDRSTPREDAQTPAQRQAAAKMALRKQLEKTLLQIPPPKPPPPEMHFIPNPSNTDFVYLLGLETVVDYLTVNKKANAVAAPFRCAQCKIDFTPVWKWEKQTNKDPKVICEQCVTSNVKKALKAEHTNRLKQAFVKALQQEQEIEQRLASQSSPSPVDNHGSSGGGNSLSVSAVSSNSSSSHMQREREQLQASHASAAAALVNLPPSVTVIPTKCQTPTPATPRPTPPPPQSQATPPPSSGGSRSSRAAATAAAAAIAAQQAGILSPGPSPAHHHEPTTSSRSSRNDRLDHHHQSQQQQQRDQRERDQQQRDQQSQQQAQNYDKYSAATLAAAAHLSALGGMGGLNINSLASLGNLGNLGNLSQLGNLAALGGLGNFGGASTGSANPAAGLSGSSPAATAAAMQAFQQQLFRALGQGLGGNPQHMMQFAPLLYSYQMAMAQAAQVAGEMTMALTGKFITGYQECDSVTFNNNNKKSSSSSGSAKNSSSSNSMAEVQRAAELQRQYLLEMIPPQQQSGASGSRQNNWKA
Protein: Retinoschisin (X-linked juvenile retinoschisis protein) (O15537)
Organism: Homo sapiens (Human)
Function: Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides (By similarity). May play a role in cell-cell adhesion processes in the retina, via homomeric interaction between octamers present on the surface of two neighboring cells. Required for normal structure and function of the retina.
Subcellular location: Secreted {ECO:0000269|PubMed:10915776, ECO:0000269|PubMed:19849666, ECO:0000269|PubMed:26812435}. Cell membrane {ECO:0000250|UniProtKB:Q9Z1L4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z1L4}; Extracellular side {ECO:0000250|UniProtKB:Q9Z1L4}. Note=Binds to phosphatidylserine-containing lipid membranes and embeds itself partially into the lipid bilayer. Lipid-binding requires the presence of Ca(2+) ions. {ECO:0000250|UniProtKB:Q9Z1L4}.
Interaction partners:
- NAD
- Retinal-specific phospholipid-transporting ATPase ABCA4
Sequence:
MSRKIEGFLLLLLFGYEATLGLSSTEDEGEDPWYQKACKCDCQGGPNALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKFQDSSQWLQIDLKEIKVISGILTQGRCDIDEWMTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRTSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECVSKCA
Protein: Vesicular glutamate transporter 1 (VGluT1) (Brain-specific Na(+)-dependent inorganic phosphate cotransporter) (Solute carrier family 17 member 7) (Q62634)
Organism: Rattus norvegicus (Rat)
Function: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter which transports preferentially L-glutamate but also phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, may function as a K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular glutamate uptake. The vesicular K(+)/H(+) antiport activity is electroneutral. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic. Is necessary for synaptic signaling of visual-evoked responses from photoreceptors (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11001057, ECO:0000269|PubMed:11698619}. Cell membrane {ECO:0000305|PubMed:29642010}; Multi-pass membrane protein {ECO:0000305}. Synapse, synaptosome {ECO:0000269|PubMed:11698619}.
Interaction partners:
- Vesicular inhibitory amino acid transporter
- Vesicular acetylcholine transporter
- Disks large homolog 4
- Synaptic vesicular amine transporter
- Synaptotagmin-1
- Chromaffin granule amine transporter
- Vesicle-associated membrane protein 2
- Ras-related protein Rab-3A
- Vesicular glutamate transporter 2
- Synaptophysin
Sequence:
MEFRQEEFRKLAGRALGRLHRLLEKRQEGAETLELSADGRPVTTHTRDPPVVDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVSMVNNSTTHRGGHVVVQKAQFNWDPETVGLIHGSFFWGYIVTQIPGGFICQKFAANRVFGFAIVATSTLNMLIPSAARVHYGCVIFVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTAFCGSYAGAVVAMPLAGVLVQYSGWSSVFYVYGSFGIFWYLFWLLVSYESPALHPSISEEERKYIEDAIGESAKLMNPVTKFNTPWRRFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFEISKVGLVSALPHLVMTIIVPIGGQIADFLRSRHIMSTTNVRKLMNCGGFGMEATLLLVVGYSHSKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPIIVGAMTKHKTREEWQYVFLIASLVHYGGVIFYGVFASGEKQPWAEPEEMSEEKCGFVGHDQLAGSDESEMEDEVEPPGAPPAPPPSYGATHSTVQPPRPPPPVRDY
Protein: THO complex subunit 5 homolog (Fms-interacting protein) (FMIP) (Q8BKT7)
Organism: Mus musculus (Mouse)
Function: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in transcription elongation and genome stability. Involved in alternative polyadenylation site choice by recruiting CPSF6 to 5' region of target genes; probably mediates association of the TREX and CFIm complexes.
Subcellular location: Nucleus {ECO:0000269|PubMed:15221008}. Cytoplasm {ECO:0000269|PubMed:15221008}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q13769}.
Interaction partners:
- THO complex subunit 7 homolog
- THO complex subunit 3
- THO complex subunit 1
- THO complex subunit 6 homolog
- THO complex subunit 2
- Spliceosome RNA helicase Ddx39b
- THO complex subunit 4
- Aly/REF export factor 2
- Nuclear RNA export factor 1
- THO complex subunit 2
Sequence:
MSSESSKKRKPKVIRSDGTPTEGKRNRSDTEQEGKYYSEEAEVDLRDPGRDYELYKYTCQELQRLMAEIQDLKSKGSKDVAIEIEERRIQSCVHFMTLKKLNRLAHIRLKKGRDQTHEAKQKVDAYHLQLQNLLYEVMHLQKEITKCLEFKSKHEEIDLVSLEEFYSEAPPSISKAEITMGDPHQQTLARLDWELEQRKRLAEKYRECLSNKEKILKEIEVKRDYLSSLQPRLNSIMQASLPVQEYLFMPFDQAHKQYETARHLPPPLYVLFVQATAYGQACDKTLSVAIEGSVDEAKALFKPPEDSQDDESDSDAEEEQTTKRRRPTLGVQLDDKRKEMLKRHPLSVLLDLKCKDNSVLHLTFYYLMNLNIMTVKAKVTTAVELITPISAGDLLSPDSVLSCLYPGDHGKKTPNPANQYQFDKVGILTLRDYVLELGHPYLWVQKLGGLHFPKEQPQQTVMPDHSQSASHMETTMKLLKTRVQSRLALHKQFASLEHGIVPVTSDCQDLFPAKVVSRLVKWVIITHEDYMELHFTKDIVEAGLAGDTNLYYLALIERGTAKLQAAVVLNPGYSSIPPVFRLCLNWKGEKTNSNDDNIRAMESEVNVCYKELCGPRPSHQLLTNQLQRLCVLLDVYLETESHDDSFEGPKEFPQEKMCLRLFRGPSRMKPFKYNHPQGFFSHR
Protein: Fibrinogen-like protein 1 (Fibrinogen-related protein 1) (Mfrep-1) (Liver fibrinogen-related protein-1) (Mfire-1) (Q71KU9)
Organism: Mus musculus (Mouse)
Function: Immune suppressive molecule that inhibits antigen-specific T-cell activation by acting as a major ligand of LAG3. Responsible for LAG3 T-cell inhibitory function. Binds LAG3 independently from MHC class II (MHC-II). Secreted by, and promotes growth of, hepatocytes (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:30580966}. Note=Secreted in the blood plasma. {ECO:0000269|PubMed:30580966}.
Interaction partners:
- Lymphocyte activation gene 3 protein
- Apolipoprotein F
- Beta-2-glycoprotein 1
Sequence:
MGKIYSFVLVAIALMMGREGWALESESCLREQVRLRAQVHQLETRVKQQQTMIAQLLHEKEVQFLDKGSENSFIDLGGKRQYADCSEIYNDGFKQSGFYKIKPLQSLAEFSVYCDMSDGGGWTVIQRRSDGSENFNRGWNDYENGFGNFVQNNGEYWLGNKNINLLTIQGDYTLKIDLTDFEKNSSFAQYQSFKVGDKKSFYELNIGEYSGTAGDSLSGTFHPEVQWWASHQRMKFSTWDRDNDNYQGNCAEEEQSGWWFNRCHSANLNGVYYRGSYRAETDNGVVWYTWHGWWYSLKSVVMKIRPSDFIPNII
Protein: Protein arginine N-methyltransferase 1 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT1) (Q9JIF0)
Organism: Mus musculus (Mouse)
Function: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1, CHTOP and MAP3K5/ASK1. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation (By similarity). May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway (By similarity). Methylates RBM15, promoting ubiquitination and degradation of RBM15 (By similarity). Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity. Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity. Methylates MAP3K5/ASK1 at 'Arg-85' and 'Arg-87' which promotes association of MAP3K5 with thioredoxin and negatively regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 stimulation and MAP3K5-induced activation of JNK (By similarity). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). Plays a role in regulating alternative splicing in the heart.
Subcellular location: Nucleus {ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:30321814}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm, cytosol {ECO:0000269|PubMed:19858291}. Cytoplasm {ECO:0000269|PubMed:19858291}. Lysosome membrane {ECO:0000250|UniProtKB:Q99873}. Note=Mostly found in the cytoplasm (PubMed:19858291). Colocalizes with CHTOP within the nucleus (PubMed:19858291). Low levels detected also in the chromatin fraction (PubMed:22872859). Upon methionine stimulation, localizes to the lysosome membrane in an NPRL2-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q99873, ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22872859}.
Interaction partners:
- Protein arginine N-methyltransferase 5
- Protein BTG2
- Runt-related transcription factor 1
- Forkhead box protein O1
- Forkhead box protein O3
- Forkhead box protein O6
- Forkhead box protein O4
- Histone-arginine methyltransferase CARM1
- Methylosome protein WDR77
- Histone H4
Sequence:
MAAAEAANCIMENFVATLANGMSLQPPLEEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR
Protein: TBP protein (Q32MN6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDQNNSLPPYAQGLASPQGAMTPGIPIFSPMMPYGTGLTPQPIQNTNSLSILEEQQRQATQGTSGQAPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRAEIYEAFENIYPILKGFRKTT
Protein: Uncharacterized protein (Q382I4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSEEDGEGLEGEASVQKSTGFSLSTLKDPFVHELIAENEAMLAEITFLREKRHGAERLQKQCVQAAEEAVRQQLVAEEANERERRQGNFFKVALRGLHDDVAALREENTALQNIMLTVQAELGASEETRISTVLLSPRMTATGKEVTSMRSSVVPDVESKLLARYSTFLGNRSSGERPTSPTRTANPQGRKRPRPSGGDWMFTPLDGSGADRGQNGEAHST
Protein: LIM domain-containing protein pin-2 (Q19157)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9885243}. Nucleus {ECO:0000269|PubMed:9885243}.
Interaction partners:
- Integrin-linked protein kinase homolog pat-4
- Ras suppressor protein 1
- Paralyzed arrest at two-fold protein 6
- LIM domain-containing protein unc-97
- Fatty-acid and retinol-binding protein 1
Sequence:
MMTNAAQITKQRNSGKRHRACERCREQFELNEPYFLLGASSWHMRCFLCAQCMDPLVGTTYFQFENRIYCEHDFKTLYAPVCAKCNEFVIGQVVHSSNNSYHLACFTCDECNVHLNSQIAYRYQGTILCFLCNQKKPKMRIYNCNKCKQHVDNSDLLTYQENPYHAYHFKCTTCKKVLESDARTIKDDLFCPRCFDFKCEVCFDCKKVIDPQVEQSIFTMNKHWHTDHFRCATCARPFFGHEHYEKNGKAYCRDDFLELIGHHCFICDRNVGGGMVHVFGKAFCPECYRCRGCDKVLHYKDKVMELDLMPLCKKCLGNKTFQKALKYKSL