wanglab/gogpt-training-data huggingface dataset:
Protein: Peptidyl-prolyl cis-trans isomerase E (PPIase E) (EC 5.2.1.8) (Cyclophiline 33) (HcCYP) (Cyclophiline E) (Rotamase E) (Q4G338)
Organism: Haemonchus contortus (Barber pole worm)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities.
Subcellular location: Nucleus {ECO:0000269|PubMed:15830208}.
Interaction partners:
Sequence:
MAASNFPHNKKRTLYVGGFGEEVTEKVLMAAFITFGDIVAISIPMDYETGKHRGFGFVEFELAEDAAAAIDNMNESELFGRTIRCNFARPPKATERSSRPVWADDEWLKRYGKGSGIADAKESNGSASTAKGLPRVYLGVKIGIRYIGRIVIELRSDVVPRTAENFRCLCTGEKGFGYEGSSFHRIIPKFMLQGGDFTKGDGTGGKSIYGPKFEDENFKLKHLMPGTVSMANCGPNTNGSQFFICAEKTDWLDGKHVVFGHVVEGMNVVRQVEQQGTPSGKPQMVVKIVECGELDPVPQTEPQENEENSDPQTPMDVEPQKETA
Protein: BRMS1 transcriptional repressor (LD14895p) (Q9VYI2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Paired amphipathic helix protein Sin3a
- Histone deacetylase complex subunit SAP30 homolog
- FI07430p
- Histone deacetylase HDAC1
- Inhibitor of growth protein
- Chromatin assembly factor 1 p55 subunit
- PHD finger protein 12
- BRCA2-interacting transcriptional repressor EMSY
- Sin3A-associated protein 130, isoform C
- Hat-trick, isoform D
Sequence:
MPVKNGESDGEGDVSGGESEHSNSSQPHDTSDEEEANECDSDDSSELDASEIDRRRAEHIEDLLSLERQFNELREQYYVERINLIERQLAEVRSGRSEEFVQPQKELDKKYRTRIEVADVLRKYRLQNIEHKYQSEEQAAVQHFESEKHMALDNLREEFMERIRRLEEDRHNVDISWADWGTDKRQSKVRGPGRKKAVTVTGPYVVYMLREEDIMEDWTIIRKALKRSSSSATAAGTVTPTSGVSVSLSGLPAMAGASG
Protein: Large ribosomal subunit protein eL34A (60S ribosomal protein L34-A) (P87262)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein eL19A
- Large ribosomal subunit protein eL24B
- Ribosome biogenesis protein RLP24
- Large ribosomal subunit protein eL27B
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein uL22B
- Large ribosomal subunit protein uL29A
- Small ribosomal subunit protein uS7
- Ribosome biogenesis protein NSA2
- Large ribosomal subunit protein eL37B
Sequence:
MAQRVTFRRRNPYNTRSNKIKVVKTPGGILRAQHVKKLATRPKCGDCGSALQGISTLRPRQYATVSKTHKTVSRAYGGSRCANCVKERIIRAFLIEEQKIVKKVVKEQTEAAKKSEKKAKK
Protein: Karyogamy protein KAR4 (P25583)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May assist STE12 in the pheromone-dependent expression of KAR3 and CIK1. Also required for meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- N
- Nuclear fusion protein FUS1
- Protein STE12
- Protein SST2
- Kinesin-like protein KAR3
- Protein MUM2
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB/SSL2
- Factor-induced gene 1 protein
- Mitogen-activated protein kinase KSS1
- Spindle pole body-associated protein CIK1
Sequence:
MAFQDPTYDQNKSRHINNSHLQGPNQETIEMKSKHVSFKPSRDFHTNDYSNNYIHGKSLPQQHVTNIENRVDGYPKLQKLFQAKAKQINQFATTPFGCKIGIDSIVPTLNHWIQNENLTFDVVMIGCLTENQFIYPILTQLPLDRLISKPGFLFIWANSQKINELTKLLNNEIWAKKFRRSEELVFVPIDKKSPFYPGLDQDDETLMEKMQWHCWMCITGTVRRSTDGHLIHCNVDTDLSIETKDTTNGAVPSHLYRIAENFSTATRRLHIIPARTGYETPVKVRPGWVIVSPDVMLDNFSPKRYKEEIANLGSNIPLKNEIELLRPRSPVQKAQ
Protein: Iron-sulfur clusters transporter ABCB7, mitochondrial (ATP-binding cassette sub-family B member 7, mitochondrial) (ATP-binding cassette transporter 7) (ABC transporter 7 protein) (Q704E8)
Organism: Rattus norvegicus (Rat)
Function: Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis (By similarity). Moreover, through a functional complex formed of ABCB7, FECH and ABCB10, also plays a role in the cellular iron homeostasis, mitochondrial function and heme biosynthesis (By similarity). In cardiomyocytes, regulates cellular iron homeostasis and cellular reactive oxygen species (ROS) levels through its interaction with COX4I1. May also play a role in hematopoiesis (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40416}.
Interaction partners:
- Ferrochelatase
- Frataxin, mitochondrial
- Glutaredoxin-related protein 5, mitochondrial
- Mitochondrial potassium channel ATP-binding subunit
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Mitochondrial glycine transporter
- Mitoferrin-1
- Transmembrane protein 14C
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- ATP-binding cassette sub-family F member 2
Sequence:
MALLAIHSWRWAAAAVAFEKHKHSAVLTRSLVSICGSGLRWSSYQSGASGSARLSQTTESLRNSTQQRWEKNNSRQLLDASKVLQAWPLIEKRTCWHGHAGGGLHTDPKEGLKDVDTRKIIKAMLSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFEMTLVSSVLYYKCGAQFALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTRIKDKAMASPLQITPQTATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANSSSIYSEMWHTQSTRIQNHDNLGWDAKKESLSKEEERKKLQEEIVNSVKGCGNCSC
Protein: Copper transport protein CCH (Copper chaperone CCH) (O82089)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in copper homeostasis. Can complement the yeast mutants atx1 and sod1.
Interaction partners:
- Cytochrome c biogenesis protein CCS1, chloroplastic
- Copper-transporting ATPase RAN1
- Superoxide dismutase 1
- Copper chaperone for superoxide dismutase, chloroplastic/cytosolic
- Cytochrome c oxidase copper chaperone 1
- Cytochrome c oxidase subunit 5b-1, mitochondrial
- Squamosa promoter-binding-like protein 7
- Copper-transporting ATPase PAA1, chloroplastic
- Probable copper-transporting ATPase HMA5
- Copper transporter 5
Sequence:
MAQTVVLKVGMSCQGCVGAVNRVLGKMEGVESFDIDIKEQKVTVKGNVEPEAVFQTVSKTGKKTSYWPVEAEAEPKAEADPKVETVTETKTEAETKTEAKVDAKADVEPKAAEAETKPSQV
Protein: Phosphopentomutase (EC 5.4.2.7) (Glucose phosphomutase 2) (Phosphodeoxyribomutase) (Phosphoglucomutase-1) (Phosphoglucomutase-2) (PGM 2) (EC 5.4.2.2) (Q7TSV4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. Catalyzes the interconversion of glucose-1-phosphate into glucose-6-phosphate but with a lower catalytic efficiency. In vitro, has also a low glucose 1,6-bisphosphate synthase activity which is most probably not physiologically relevant.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96G03}.
Interaction partners:
- Phosphoglucomutase-1
- Ribose-phosphate pyrophosphokinase 1
- Deoxyribose-phosphate aldolase
- ribose-phosphate diphosphokinase
- Ribose-phosphate pyrophosphokinase 2
- Ribose-phosphate pyrophosphokinase 1
- UTP--glucose-1-phosphate uridylyltransferase
- Glucose-6-phosphate isomerase
- Ribose-5-phosphate isomerase
- Ribokinase
Sequence:
MAAATPTETPAPEGSGLGMDARLDQETAQWLRWDQNPLTSESVKQLIAGGNKEELRKCFGARMEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLEKQFSDLKQRGVVISFDARAHPASGGSSRRFARLAATAFITQGVPVYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLVDSSPLLHNPSASIGNDYFEDLKKYCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVKYPNPEEGKGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWKEKNQDQSNLKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGDQGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELASFLATKNLSLSQQLNAIYVEYGYHITTASYFICHDQGTIQNLFGNLRNYDGKNNYPKMCGKFEISAIRDLTTGYDDSQPDKKAVLPTSKSSQMITFTFANGGVATMRTSGTEPKIKYYAELCAPPGNSDPEHLKKELDELVGAIEEHFFQPQKYNLQPKAE
Protein: Katanin p80 WD40 repeat-containing subunit B1 (Katanin p80 subunit B1) (p80 katanin) (Q9BVA0)
Organism: Homo sapiens (Human)
Function: Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:9568719}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9568719, ECO:0000269|PubMed:9658175}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26929214}. Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles (PubMed:9658175). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (PubMed:26929214). {ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}.
Interaction partners:
- Katanin p60 ATPase-containing subunit A1
- Katanin p60 ATPase-containing subunit A-like 1
- KATNB1-like protein 1
- Leucine zipper putative tumor suppressor 2
- Katanin p60 ATPase-containing subunit A-like 2
- Abnormal spindle-like microcephaly-associated protein
- Tubulin beta-2A chain
- Tubulin alpha-1A chain
- Tubulin gamma-1 chain
- Tubulin beta chain
Sequence:
MATPVVTKTAWKLQEIVAHASNVSSLVLGKASGRLLATGGDDCRVNLWSINKPNCIMSLTGHTSPVESVRLNTPEELIVAGSQSGSIRVWDLEAAKILRTLMGHKANICSLDFHPYGEFVASGSQDTNIKLWDIRRKGCVFRYRGHSQAVRCLRFSPDGKWLASAADDHTVKLWDLTAGKMMSEFPGHTGPVNVVEFHPNEYLLASGSSDRTIRFWDLEKFQVVSCIEGEPGPVRSVLFNPDGCCLYSGCQDSLRVYGWEPERCFDVVLVNWGKVADLAICNDQLIGVAFSQSNVSSYVVDLTRVTRTGTVARDPVQDHRPLAQPLPNPSAPLRRIYERPSTTCSKPQRVKQNSESERRSPSSEDDRDERESRAEIQNAEDYNEIFQPKNSISRTPPRRSEPFPAPPEDDAATAKEAAKPSPAMDVQFPVPNLEVLPRPPVVASTPAPKAEPAIIPATRNEPIGLKASDFLPAVKIPQQAELVDEDAMSQIRKGHDTMCVVLTSRHKNLDTVRAVWTMGDIKTSVDSAVAINDLSVVVDLLNIVNQKASLWKLDLCTTVLPQIEKLLQSKYESYVQTGCTSLKLILQRFLPLITDMLAAPPSVGVDISREERLHKCRLCYKQLKSISGLVKSKSGLSGRHGSTFRELHLLMASLD
Protein: DNA primase (EC 2.7.7.101) (P9WNW1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Interaction partners:
- Replicative DNA helicase DnaB
- Deoxyguanosinetriphosphate triphosphohydrolase-like protein
- DNA polymerase I
- GTPase Der
- DNA polymerase III subunit alpha
- Ribonuclease PH
- RNA polymerase sigma factor SigA
- RNA polymerase sigma factor SigB
- Protein RecA
- DNA-directed RNA polymerase subunit beta'
Sequence:
MSGRISDRDIAAIREGARIEDVVGDYVQLRRAGADSLKGLCPFHNEKSPSFHVRPNHGHFHCFGCGEGGDVYAFIQKIEHVSFVEAVELLADRIGHTISYTGAATSVQRDRGSRSRLLAANAAAAAFYAQALQSDEAAPARQYLTERSFDAAAARKFGCGFAPSGWDSLTKHLQRKGFEFEELEAAGLSRQGRHGPMDRFHRRLLWPIRTSAGEVVGFGARRLFDDDAMEAKYVNTPETLLYKKSSVMFGIDLAKRDIAKGHQAVVVEGYTDVMAMHLAGVTTAVASCGTAFGGEHLAMLRRLMMDDSFFRGELIYVFDGDEAGRAAALKAFDGEQKLAGQSFVAVAPDGMDPCDLRLKCGDAALRDLVARRTPLFEFAIRAAIAEMDLDSAEGRVAALRRCVPMVGQIKDPTLRDEYARQLAGWVGWADVAQVIGRVRGEAKRTKHPRLGRLGSTTIARAAQRPTAGPPTELAVRPDPRDPTLWPQREALKSALQYPALAGPVFDALTVEGFTHPEYAAVRAAIDTAGGTSAGLSGAQWLDMVRQQTTSTVTSALISELGVEAIQVDDDKLPRYIAGVLARLQEVWLGRQIAEVKSKLQRMSPIEQGDEYHALFGDLVAMEAYRRSLLEQASGDDLTA
Protein: Apoptosis regulator Bcl-2 (P10417)
Organism: Mus musculus (Mouse)
Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function (By similarity). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29020630}.
Interaction partners:
- Cellular tumor antigen p53
- Bcl-2-like protein 11
- Bcl-2-like protein 1
- Beclin-1
- Bcl-2-interacting killer
- Bcl-2-binding component 3
- Phorbol-12-myristate-13-acetate-induced protein 1
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
- Apoptosis regulator BAX
- Bcl2-associated agonist of cell death
Sequence:
MAQAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDADAAPLGAAPTPGIFSFQPESNPMPAVHRDMAARTSPLRPLVATAGPALSPVPPVVHLTLRRAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK
Protein: DNA primase large subunit (Q38BT5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA polymerase
- DNA polymerase alpha subunit B
- DNA primase
- DNA polymerase epsilon catalytic subunit
- DNA polymerase
- DNA polymerase II subunit 2
- Proliferating cell nuclear antigen
- Replication factor C, subunit 2, putative
- Replication factor C, subunit 5, putative
- DNA polymerase delta subunit 2, putative
Sequence:
MQAIGTSPKAPLEGERDLLKGRTAMISMPDWSTMYTCNPAGNKTLFELEAIVVKRLELLGWIDQLLNSPNMKNLSQLLDEVGAHLPLERRKQSTQPAADHVVLGRDSVDGSTSDTPGSRAPRHSSRSLTAMLSTQNVFVFEGDEDLLSHRLARFVFCMSEKWRKWFVRTEEMLLRARLRLQLAKCEADFLPNLMRLNGLPCDALTDDQQQDPRLQKYIIYHTAVQGKGQLRRADEYFLVPLSLATRLIKARSVLCLRGHAILHRDQVQEVFVTMFLSKLNKGLHEAYLARMKLSSHEDHDERETVMKMLDAFLEYFIEDTMNEVQEASAGAVGAGDVRHLAQTHFPLCMRQVDEHLRREGHLKHQGRFTYGLFLKAIGLSMQDSMVLFSSLMTLKAGAAGKGDPESFAKTSYGYNIRHNYGMEGKKTSYSSLSCTSLLGLPPVVDKFDCHGCPFRFKNESAFRGVLLKEQLHPLGKGHSSIRLAASDIEDIIQDCKGQHYTRACYKYFMATHPGARRDTLFRSPHEYYVTSREMTDKVGDSLSDSTPAHETPGRDNLKRSIFTPTLREDVVRPRDSL
Protein: Polymerase delta-interacting protein 2 (38 kDa DNA polymerase delta interaction protein) (p38) (Q9Y2S7)
Organism: Homo sapiens (Human)
Function: Involved in DNA damage tolerance by regulating translesion synthesis (TLS) of templates carrying DNA damage lesions such as 8oxoG and abasic sites. May act by stimulating activity of DNA polymerases involved in TLS, such as PRIMPOL and polymerase delta (POLD1).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16428295}. Nucleus {ECO:0000269|PubMed:16428295}. Note=Mainly localizes to the mitochondrial matrix; a small fraction localizes in the nucleus. {ECO:0000269|PubMed:16428295}.
Interaction partners:
- Cytochrome b-245 light chain
- NADPH oxidase 4
- DNA polymerase delta subunit 2
- DNA-directed primase/polymerase protein
- Cell adhesion molecule CEACAM1
- Neutrophil cytosol factor 2
- Neutrophil cytosol factor 1
- NADPH oxidase 2
- DNA polymerase delta catalytic subunit
- NADPH oxidase activator 1
Sequence:
MAACTARRALAVGSRWWSRSLTGARWPRPLCAAAGAGAFSPASTTTTRRHLSSRNRPEGKVLETVGVFEVPKQNGKYETGQLFLHSIFGYRGVVLFPWQARLYDRDVASAAPEKAENPAGHGSKEVKGKTHTYYQVLIDARDCPHISQRSQTEAVTFLANHDDSRALYAIPGLDYVSHEDILPYTSTDQVPIQHELFERFLLYDQTKAPPFVARETLRAWQEKNHPWLELSDVHRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLSKEQPAFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLESNKDEKTPPSGLHW
Protein: Receptor expression-enhancing protein 5 (Polyposis locus protein 1) (Protein TB2) (Q00765)
Organism: Homo sapiens (Human)
Function: Plays an essential role in heart function and development by regulating the organization and function of the sarcoplasmic reticulum in cardiomyocytes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23969831}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q60870}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum tubular network (PubMed:23969831). In cardiomyocytes, localizes to the junctional sarcoplasmic reticulum membrane which is closely tethered to the cell membrane and contractile machinery (By similarity). {ECO:0000250|UniProtKB:Q60870, ECO:0000269|PubMed:23969831}.
Interaction partners:
- Reticulon-4
- Phosphoribosylformylglycinamidine synthase
- Reticulon-3
- Reticulon-1
- Atlastin-3
- Atlastin-2
- Atlastin-1
- Reticulon-2
- Prenylated Rab acceptor protein 1
- Zinc finger protein 740
Sequence:
MSAAMRERFDRFLHEKNCMTDLLAKLEAKTGVNRSFIALGVIGLVALYLVFGYGASLLCNLIGFGYPAYISIKAIESPNKEDDTQWLTYWVVYGVFSIAEFFSDIFLSWFPFYYMLKCGFLLWCMAPSPSNGAELLYKRIIRPFFLKHESQMDSVVKDLKDKAKETADAITKEAKKATVNLLGEEKKST
Protein: CTP synthase 1 (EC 6.3.4.2) (CTP synthetase 1) (UTP--ammonia ligase 1) (P17812)
Organism: Homo sapiens (Human)
Function: This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:25223282}. Note=Mainly cytosolic but when active detected in long filamentous structures (PubMed:25223282). Co-localizes with TNK2 in the cytosolic filaments (By similarity). {ECO:0000250|UniProtKB:P70698, ECO:0000269|PubMed:25223282}.
Interaction partners:
- CTP synthase 2
- GMP synthase
- Nucleoside diphosphate kinase A
- Nucleoside diphosphate kinase B
- Nucleoside diphosphate kinase 6
- Nucleoside diphosphate kinase homolog 7
- Nucleoside diphosphate kinase, mitochondrial
- Nucleoside diphosphate kinase 3
- Nucleoside diphosphate kinase
- Adenylate kinase 9
Sequence:
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
Protein: Inner membrane protein YhaH (P64590)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MDWYLKVLKNYVGFRGRARRKEYWMFILVNIIFTFVLGLLDKMLGWQRAGGEGILTTIYGILVFLPWWAVQFRRLHDTDRSAWWALLFLIPFIGWLIIIVFNCQAGTPGENRFGPDPKLEP
Protein: RRM domain-containing protein (F4HYH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MWKKGELVWVSVSFSNTWIPGRIIDPSESLGVLVSFFGLMDPRYVPKPFLRSFDRDFKTLISDSRWIRRFVNRALRAYFWNISFGLWCSCQPRIDSPYLDRENSLPRFHATSDSALGFVRDMAISIRMPLWRLAETNSSSAQILSFRRYIVDFKRSESVYEETRARTSKFECESICSVYNRTRRSAELNDRSEESGWCLEYSKKMDLCSMFPETADADIDNSRDLSLRDPLPKDLPCCSSEQHVDKVVQICTWNTRSPRTSSNSSTMKACETMVRRAVHEDDGHLSKSKECCQVEQNICLLNSEPSIEDMIEEDTTSVAASRVDVSEALPDVMIETHDDIIGLVDGPVTSTNELSPLLDSSNDKAYLAKPVSFVVPGACHTLACSVRKKYASPRNKLDSSIISAKTLNEQSLGRNSLNGTRENCSEYTLESHIVEVGQVSLPSTGTSNKEFSSDDAGAPAEQLQDLEAGTTVENQTRSVDNVRSIGVKRKASRDKASARYSKRKKKAGQQSISTDKSLNLHLMKDMRLANPKCLRMKFLCRHGDLPSKAELLKRFSVFGKIDASRTDVNPGESSAKVVFMQSIDAVTAYQFARSKKFRLGKSKVTYRLEPFEEDNEVKKVPLPQKPQKSAPSPKSCLKEHGLVDKEEGRRNMKVKFQMETNS
Protein: TBC1 domain family member 7 (Q9D0K0)
Organism: Mus musculus (Mouse)
Function: Component of the TSC-TBC complex, that contains TBC1D7 in addition to the TSC1-TSC2 complex and consists of the functional complex possessing GTPase-activating protein (GAP) activity toward RHEB in response to alterations in specific cellular growth conditions. The small GTPase RHEB is a direct activator of the protein kinase activity of mTORC1 and the TSC-TBC complex acts as a negative regulator of mTORC1 signaling cascade by acting as a GAP for RHEB. Participates in the proper sensing of growth factors and glucose, but not amino acids, by mTORC1. It is unclear whether TBC1D7 acts as a GTPase-activating protein and additional studies are required to answer this question.
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q9P0N9}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9P0N9}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9P0N9}. Note=Localizes in the cytoplasmic vesicles of the endomembrane in association with the TSC-TBC complex. Recruited to lysosomal membranes in a RHEB-dependent process in absence of nutrients. In response to nutrients, the complex dissociates from lysosomal membranes and relocalizes to the cytosol. {ECO:0000250|UniProtKB:Q9P0N9}.
Interaction partners:
- Hamartin
- Tuberin
- GTP-binding protein Rheb
- RAC-alpha serine/threonine-protein kinase
- Ribosomal protein S6 kinase alpha-1
- DNA damage-inducible transcript 4 protein
- RAC-gamma serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- Glycogen synthase kinase-3 beta
- Ribosomal protein S6 kinase alpha-2
Sequence:
MTDDSQRNFRSVYYEKVGFRGVEEKKSLEILLKDDRLDIEKLCTFSQRFPLPSMYRALVWKALLGILPPHHDTHSQVMAYRKDQYHDILHALTVVRFISDATPQAEVYLRMYQLESGKLPRSPSFPLEPEDEVFLAIAKAMEEMVEDSVDCYWISRCFVKQLNNKYRDALPQLPKAFEQYLNLEDSRLLSHLKTCSAVSKLPYDLWFQRCFAGCLPESSLQRVWDKVVSGSCKILVFVAVEILLTFKIKVMALNSAEKITKFLENIPQDSSDAIVSKAIDLWHKHCGTPVHSA
Protein: Probable transporter MCH1 (Monocarboxylate transporter homolog 1) (Q07376)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable transporter. Does not act in the transport of monocarboxylic acids across the plasma membrane.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MPLSKVEHYLSYHTRLLLPHVLSLQSSHRVAYIFSLLSAVSTGFITLISLYSQPWQKHLNYSSWQINTIASMTNLGMYLTPPILGMIADSHGPITLSLLAIIGFIPSYSYLAYVFNHPELSLGGNGDSSFNLSIICFVFIGISTSALYFSALLTCTKLYPHTKLLSISLPTTCYGISSVVGSQLLRIKWFWSSNASSSSSNSDLNLGRVFQTFALVYVVIGLLAWIATSVVSLLHFNEEQDNQKRLDDQTDVEQSPLLERSNHVQEKFTQTMLRIFSDPVTYILAVSILLSLGPLEMFIANMGSLTNLLVQLDAPTLSTKLLSTYALSSTFTRLLTGIVADFFAKKKISIKWILLTFLSLGVCAQLFLLKMTSSASPWGLVPTGSLVGIVYGGLFTVYPTLVLLVWGERSFGTVYGSLLIAPAIGSMIFCMLYAKFYDSRCMSGGGDLRNPSCISAVYKYSSIAFVVSAVLSAVVFWKLKSRKLRI