wanglab/gogpt-training-data huggingface dataset:
Protein: Protein cornichon homolog 1 (CNIH-1) (Cornichon family AMPA receptor auxiliary protein 1) (Protein cornichon homolog) (T-cell growth-associated molecule 77) (TGAM77) (O95406)
Organism: Homo sapiens (Human)
Function: Involved in the selective transport and maturation of TGF-alpha family proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17607000}; Multi-pass membrane protein {ECO:0000269|PubMed:17607000}. Golgi apparatus membrane {ECO:0000269|PubMed:17607000}. Note=Located primarily in the ER; may cycle between the ER and the Golgi apparatus.
Interaction partners:
- Glutamate receptor 1
- Pre-mRNA-processing factor 19
- Protransforming growth factor alpha
- Cytosolic 5'-nucleotidase 1A
- Transmembrane emp24 domain-containing protein 10
- Glutamate receptor 4
- Glutamate receptor 2
- Voltage-dependent calcium channel gamma-8 subunit
- Glutamate receptor 3
- Protein shisa-9
Sequence:
MAFTFAAFCYMLALLLTAALIFFAIWHIIAFDELKTDYKNPIDQCNTLNPLVLPEYLIHAFFCVMFLCAAEWLTLGLNMPLLAYHIWRYMSRPVMSGPGLYDPTTIMNADILAYCQKEGWCKLAFYLLAFFYYLYGMIYVLVSS
Protein: Glucosamine 6-phosphate N-acetyltransferase (EC 2.3.1.4) (Phosphoglucosamine acetylase) (Phosphoglucosamine transacetylase) (O93806)
Organism: Candida albicans (Yeast)
Interaction partners:
Sequence:
MMLPQGYTFRKLKLTDYDNQYLETLKVLTTVGEISKEDFTELYNHWSSLPSIYHPYVITNASGIVVATGMLFVEKKLIHECGKVGHIEDISVAKSEQGKKLGYYLVTSLTKVAQENDCYKVILDCSPENVGFYEKCGYKDGGVEMVCRF
Protein: Centromere protein K (CENP-K) (SoxLZ/Sox6 leucine zipper-binding protein in testis) (Q9ESN5)
Organism: Mus musculus (Mouse)
Function: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Acts in coordination with KNL1 to recruit the NDC80 complex to the outer kinetochore (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex (By similarity). {ECO:0000250}.
Interaction partners:
- Centromere protein I
- Centromere protein H
- Centromere protein M
- Centromere protein N
- Centromere protein O
- Centromere protein Q
- Centromere protein P
- Centromere protein U
- Centromere protein R
- Centromere protein T
Sequence:
MSENKQEVHPDTITDVEAVIDTEEELIKECEEMWKDMEDCQNKLSLIGTETLTNADAQLSLLIMQMKCLTAELGQWKKRKPEIIPLNEDVLLTLGKEEFQKLRCDLEMVLSTIQSKNEKLKEDLEREQQWLDEQQQILDTLNVLNSDVENQVVTLTESRIFNELTTKIRGIKEFKEKLLLTLGAFLDNHFPLPEASTPKKRKNIQDSNAQLITLNEILEMLINRMFDVPHDPYVKIRDSFWPPYIELLLRYGIALRHPEDPSQIRLEAFHQ
Protein: Bromodomain containing 8 (H7C127)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
GKHKLLSTGPTEPWSIREKLCLASSVMRSGDQNWVSVSRAIKPFAEPGRPPDWFSQKHCASQYSELLETTETPKRKRGEKGEVVETVEDVIVRKLTAERVEELKKVIKETQERYRRLKRDAELIQAGHMDSRLDELCNDIATKKKLEEEEAEVKRKATDAAYQARQAVKTPPRRLPTVMVRSPIDSASPGGDYPLGDLTPTTMEEATSGVTPGTLPSTPVTSFPGIPDTLPPGSAPLEAPMTPVTDDSPQKKMLGQKATPPPSPLLSELLKKGSLLPTSPRLVNESEMAVASGHLNSTGVLLEVGGVLPMIHGGEIQQTPNTVAASPAASESVSQATIVMMPALPAPSSAPAVSTTESVAPVSQPDNCVPMEAVGDPHTVTVSMDSSEISMIINSIKEECFRSGVAEAPVGSKAPSIDGKEELDLAEKMDIAVSYTGEELDFETVGDIIAIIEDKVDDHPEVLDVAAVEAALSFCEENDDPQSLPGPWEHPIQQERDKPVPLPAPEMTVKQERLDFEETENKGIHELVDIREPSAEIKVEPAEPEPVISGAEIVAGVVPATSMEPPELRSQDLDEELGSTAAGEIVEADVAIGKGDETPLTNVKTEASPESMLSPSHGSNPIEDPLEAETQHKFEMSDSLKEESGTIFGSQIKDAPGEDEEEDGVSEAASLEEPKEEDQGEGYLSEMDNEPPVSESDDGFSIHNATLQSHTLADSIPSSPASSQFSVCSEDQEAIQAQKIWKKAIMLVWRAAANHRYANVFLQPVTDDIAPGYHSIVQRPMDLSTIKKNIENGLIRSTAEFQRDIMLMFQNAVMYNSSDHDVYHMAVEMQRDVLEQIQQFLATQLIMQTSESGISAKSLRGRDSTRKQDASEKDGGTRGRRCAIEADMKMKK
Protein: Alpha-conotoxin SrIA/SrIB (P85886)
Organism: Conus spurius (Alphabet cone)
Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Has weak blocking effects on muscle nAChR composed of alpha-1/beta-1/gamma/delta subunits and the central nervous system nAChR composed of alpha-4/beta-2 subunits. Does not detectably affect the peripheral nervous system nAChR composed of alpha-3/beta-4 subunits. Low toxin concentrations potentiate currents in muscle nAChR composed of alpha-1/beta-1/gamma/delta subunits and central nervous system nAChR composed of alpha-4/beta-2 subunits, but not the peripheral nervous system nAChR composed of alpha-3/beta-4 subunits.
Subcellular location: Secreted {ECO:0000269|PubMed:17635581}.
Interaction partners:
Sequence:
MGMRMMFTVFLLVVLATTVVSFTSDSAFDSRNVAANDKVSDMIALTARRTCCSRPTCRMEYPELCGGRR
Protein: Serine/threonine-protein kinase ppk34 (EC 2.7.11.1) (Q9UU87)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSLPLPSFLSSNNYNSSETSLLTEGPESDEEDEGPLLKQYRLKNMLGYGACSTVYLAVDVSTNIEYAIKEFKKTSLRRREKFRLMQLEKELGSFNDMDSSTIEDQIRNQEKKDPYYYIRKELDVLKVLDHENVVKLYQVINSDYKDSLCMVLNYCPGGKLASVDHGISFDPMPLETCRKSFRQLVLAVNYIHGKGVIHRDIKPDNILFKENNNLCVIDFGLAEFLPKDGFVKPASGTPAFMAPELFDNELKKIKGKPLDIWSMGVTLYVIAFAEFPFNGSTILDMINVIKGKSLMIPAYCNSDLRKLLERCLEKNPEKRITIEELLRDPFLTERGKHHLTSSSIVTAFSSIWEI
Protein: Dynein light chain 2, cytoplasmic (8 kDa dynein light chain b) (DLC8) (DLC8b) (Dynein light chain LC8-type 2) (Q9D0M5)
Organism: Mus musculus (Mouse)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14561217}.
Interaction partners:
- Cytoplasmic dynein 1 intermediate chain 1
- Cytoplasmic dynein 1 intermediate chain 2
- Dynein light chain roadblock-type 1
- Cytoplasmic dynein 2 light intermediate chain 1
- Cytoplasmic dynein 1 heavy chain 1
- Dynein light chain roadblock-type 2
- Dynein light chain 1, cytoplasmic
- Cytoplasmic dynein 2 heavy chain 1
- Dynein light chain Tctex-type 3
- Cytoplasmic dynein 1 light intermediate chain 2
Sequence:
MSDRKAVIKNADMSEDMQQDAVDCATQAMEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
Protein: Ribulose-phosphate 3-epimerase (EC 5.1.3.1) (A0A0G2JW38)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQDPFFDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKHCLLQVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEAAQKRSLDR
Protein: Vacuolar protein sorting-associated protein 26B (Vesicle protein sorting 26B) (Q8C0E2)
Organism: Mus musculus (Mouse)
Function: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (By similarity). May be involved in retrograde transport of SORT1 but not of IGF2R. Acts redundantly with VSP26A in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16190980}. Membrane {ECO:0000269|PubMed:16190980}; Peripheral membrane protein {ECO:0000269|PubMed:16190980}. Early endosome {ECO:0000269|PubMed:21920005}. Late endosome {ECO:0000269|PubMed:21920005}. Note=Endosomal localization is reported controversially. Does not localize to endosomes (PubMed:16190980). Localizes to early and late endosomal structures (PubMed:18088321, PubMed:21920005). {ECO:0000269|PubMed:16190980, ECO:0000269|PubMed:18088321, ECO:0000269|PubMed:21920005}.
Interaction partners:
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-1
- Sorting nexin-27
- Sorting nexin-2
- Vacuolar protein sorting-associated protein 26A
- TBC1 domain family member 5
- Sorting nexin-3
- Sorting nexin-5
- Sorting nexin-12
Sequence:
MSFFGFGQSVEVEILLNDAESRKRAEHKTEDGKKEKYFLFYDGETVSGKVSLSLKNPNKRLEHQGIKIEFIGQIELYYDRGNHHEFVSLVKDLARPGEITQSQAFDFEFTHVEKPYESYTGQNVKLRYFLRATISRRLNDVVKEMDIVVHTLSTYPELNSSIKMEVGIEDCLHIEFEYNKSKYHLKDVIVGKIYFLLVRIKIKHMEIDIIKRETTGTGPNVYHENDTIAKYEIMDGAPVRGESIPIRLFLAGYELTPTMRDINKKFSVRYYLNLVLIDEEERRYFKQQEVVLWRKGDIVRKSMSHQAAIASQRFEGTTSLGEVRTPGQLSDNNSRQ
Protein: MOB kinase activator-like 4 (Mob as tumor suppressor protein 4) (Dmob4) (Mps one binder kinase activator-like 4) (Q7K0E3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cerebral cavernous malformation 3
- CTTNBP2 N-terminal-like protein
- LD24318p
- Connector of kinase to AP-1, isoform E
- AT25231p
- FGFR1 oncogene partner 2 homolog
- Homeobox protein goosecoid
- LD27370p
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- Serine/threonine-protein phosphatase PP2A
Sequence:
MKMADGSTILRRNRPGTKSKDFCRWPDEPLEEMDSTLAVQQYIQQLIKRDPSNVELILTMPEAQDEGVWKYEHLRQFCMELNGLAVRLQKECSPSTCTQMTATDQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVTKLGSVCRRVYRIFSHAYFHHRRIFDEFEAETYLCHRFTHFVTKYNLMSKENLIVPINVGENAAPGESEA
Protein: Deoxyhypusine hydroxylase (DOHH) (EC 1.14.99.29) (Deoxyhypusine dioxygenase) (Deoxyhypusine monooxygenase) (Ligand of eIF5A protein 1) (P47120)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Eukaryotic translation initiation factor 5A-1
- Deoxyhypusine synthase
- Eukaryotic translation initiation factor 5A-2
- Ornithine decarboxylase
- Elongation factor 3A
- Ribosome assembly protein RRB1
- MYG1 protein YER156C
- ATP-dependent RNA helicase HAS1
- [NU+] prion formation protein 1
- Ribosome biogenesis protein ERB1
Sequence:
MSTNFEKHFQENVDECTLEQLRDILVNKSGKTVLANRFRALFNLKTVAEEFATKPEEAKKAIEYIAESFVNDKSELLKHEVAYVLGQTKNLDAAPTLRHVMLDQNQEPMVRHEAAEALGALGDKDSLDDLNKAAKEDPHVAVRETCELAINRINWTHGGAKDKENLQQSLYSSIDPAPPLPLEKDATIPELQALLNDPKQPLFQRYRAMFRLRDIGTDEAILALATGFSAESSLFKHEIAYVFGQIGSPAAVPSLIEVLGRKEEAPMVRHEAAEALGAIASPEVVDVLKSYLNDEVDVVRESCIVALDMYDYENSNELEYAPTAN
Protein: Uncharacterized protein (Q38AA8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTEVVHRKLNKYEWVEAAPGKGASPRQNGMIKELLGSAAACTEKKFYLCGGFDLKARRSVSQVVEMDVATKQWSCGVPLPERVRDAAAVAFGDCCLVFGGWNDETYTDNLWFFAPKPSDPAVTPPPGSKEPVSCAWSLIPPVGAAPSARTSHNMVLGMLSGSDDAAPTSVVYLFGGFDGAKRLNDVWRLRIGPLMEKNEAEWEIVETKVGVPPVPRDAAAVAFDAAGERLIVFGGFASFLQNDLYIFTLRGGVNTWTSQACLSVPTRRQGCVAAVSGGYFVVCLGGDERGPLPQVLQLSLADFRWAQLSLEREDLSGRGGAVGCVSEKGRRIMLFGGGIPPKLNTSLLELELEKPDAGGSRKKGG
Protein: Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division protein kinase 7) (G5EFV5)
Organism: Caenorhabditis elegans
Function: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Required for maintaining chromosome ploidy. May phosphorylate the large subunit of RNA polymerase II, ama-1.
Interaction partners:
- Cyclin-H
- CDK-activating kinase assembly factor MAT1
- DNA-directed RNA polymerase II subunit RPB1
- Transcription initiation factor IIE subunit beta
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription factor IIH subunit 2
- General transcription factor IIH subunit 3
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- BSD domain-containing protein
- General transcription factor IIH subunit 4
Sequence:
MSRRYDTIKHLGEGQFANVYLAQDLESGECVAIKKIKLGSREEAKDGINRTAIREIKLLKEIHHDNIIGLRDVIGHRTSIQLVFDFMDTDLEHVIKDKEIILMPAHIKNITMQMLLGLEFLHVHWILHRDLKPNNLLMNKMGRVKLTDFGLARFFGSPNRNYTHQVVTRWYRAPELLFGARSYGVGIDIWSVGCIIAELLLRNPIFPGESDIDQLVKIFNILGCPTPETWPNMTEMNSYVIIKPQTEYMALNYYFSAAPQDLLDLMAGMWTFDPIKRLTCTQSLQMEYFRTQPFCCLDEELPLPKKQQPQKRSRRLDDDGTRPVRRLNFD
Protein: E3 ubiquitin-protein ligase RNF10 (EC 2.3.2.27) (RING finger protein 10) (Q5XI59)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional factor involved in the regulation of MAG (Myelin-associated glycoprotein) expression. Acts as a regulator of Schwann cell differentiation and myelination.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8N5U6}. Nucleus {ECO:0000269|PubMed:18941509}.
Interaction partners:
Sequence:
MPQSSPSTAATASDMDKNSGSNSSSASSGSSKGQQPPRSASAGPAGESKPKSDGKNSNGSKRYNRKREPSYPKNENFSNQSRRSNSQKSKTFNKTPPQRGGGSSKPFSSSSNGGRRDEVAEAQRAEFSPAQFSGPKKINLNHLLNFTFEPRGQAGHFEGSGHGSWGKRNKWGHKPFNKELFLQANCQFVVSEDQDYTANFADPDTLVNWDFVEQVRICSHEVPSCPICLYPPTAAKITRCGHIFCWACILHYLSLSERTWSKCPICYSSVHKKDLKSVVATESRQYVVGDTITMQLMKREKGVLVALPKSKWMNVDHPISLGDEQHSQYSKLLLASKEQVLHRVVLEEKVALEQQLAEEKHTPESCFIEAALQEVKIREEALSGVAGGRAEVTGVVTALEQLVLMAPLAKESAFQPRKGVLEYLSAFDEEAAQVCSLDPPGPLALPLVEEEEAVSEPEACEDLIADDSLGEGTVCAELSQEEPIAKPGFTQLSSSPCYYFYQAEDGQHMFLHPVNVRCLVREYGSLEQSPEKISATVVEIAGYSMSEDVRQRHRYLSHLPLTCEFSICELALQPPVVSKETLEMFSDDIEKRKRQRQKKAREERRRERRIELEENKRQGRYPEVHIPLENLQQFPAFNSYTCSSDSALGPTSTEGHGALSLSPLSRSPGSHADFLLTPLSPTASQGSPSFCVGSLEEDSPFLSFAQMLRVGKAKADGWPKAAPKKDDNSLAPPAPVDSDGESDNSDRVPVPSFQNSFSQAIEAAFMKLDTPATSDPLSDRGGRKRKRQKQKLLFSTSVVHTK
Protein: Methyltransferase type 11 domain-containing protein (Q54JJ5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MTSEKPKEFQDKFGTVGKSYKTFRPTYTEELYSIIDSYCDSKRDLAIDCGCGSGQATVKLAKYFKKVIGFEPSQGQIENAVKTENVDFRLSPAEKIDLPSGSVDLITVATAVHWFDLPVFYQEAKRLLRDNGSLILFTTGFIQILNNDEAQKINDNFRSGTLGDYWAPIVKYVIDGYVDIKPPFENVERKTISLPKLMSVNDVIGIYSSWSGYASFIKAGNNDVLPGVKENLMSAFKTTDPNAEIVETNFPVYMVLSKK
Protein: Potassium channel subfamily K member 3 (Acid-sensitive potassium channel protein TASK-1) (TWIK-related acid-sensitive K(+) channel 1) (Two pore potassium channel KT3.1) (Two pore K(+) channel KT3.1) (O14649)
Organism: Homo sapiens (Human)
Function: pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23169818}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium channel subfamily K member 9 channel 3)
- Protein S100-A10
- Keratin, type II cytoskeletal 2 oral
- Potassium channel subfamily K member 5 channel 2)
- Potassium channel subfamily K member 18
- Potassium channel subfamily K member 1
- Potassium channel subfamily K member 10
- 14-3-3 protein beta/alpha
- Sodium channel protein type 10 subunit alpha
- Annexin A2
Sequence:
MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPELIERQRLELRQQELRARYNLSQGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTLVRYLLHRAKKGLGMRRADVSMANMVLIGFFSCISTLCIGAAAFSHYEHWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTRNGQAGGGGGGGSAHTTDTASSTAAAGGGGFRNVYAEVLHFQSMCSCLWYKSREKLQYSIPMIIPRDLSTSDTCVEQSHSSPGGGGRYSDTPSRRCLCSGAPRSAISSVSTGLHSLSTFRGLMKRRSSV
Protein: Myosin regulatory light chain 2, ventricular/cardiac muscle isoform (MLC-2) (MLC-2v) (Myosin light chain 2, slow skeletal/ventricular muscle isoform) (MLC-2s/v) (P51667)
Organism: Mus musculus (Mouse)
Function: Contractile protein that plays a role in heart development and function. Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force (By similarity). During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly.
Subcellular location: Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:P08733}.
Interaction partners:
- Myosin light chain 3
- Myosin-7
- Myosin-6
- Actin, alpha cardiac muscle 1
- Myosin light chain 4
- Myosin light chain kinase 3
- Myosin-9
- Myosin-11
- Troponin C, slow skeletal and cardiac muscles
- Rho-associated protein kinase 1
Sequence:
MAPKKAKKRIEGGSSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGSLKADYVREMLTTQAERFSKEEIDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD
Protein: Ribonucleoside-diphosphate reductase small chain (EC 1.17.4.1) (Q382Q0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribonucleoside-diphosphate reductase
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
- dTMP kinase
- dTMP kinase
- Nucleoside diphosphate kinase, putative
- Nucleoside diphosphate kinase, putative
- Nucleoside diphosphate kinase
- Guanylate kinase, putative
- Guanylate kinase, putative
Sequence:
MPPKSHKRSRKEGEVEEPLLTENPDRYVIFPIKYPDIWQKYKKARSNFWAMENIYLGNDMTDWEKLDDGERHFIKHVLAFFAARDGIVLENFVQRFMCEVQVPEVRCFYGFQIAMENIHSETYSVLIDTYVVDPDEKQRLLHAIRTIPCIEKKAKWAIEWIGSQTSFPTRLVAFAAVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHTDFACLLYEKYIVNKLPRDRVLEIICNAVSIEREFICDALPVRLIGMNSQLMTQYIEFVADRLLVSLGYDRHYNSKNPFDFMDMISLQGKTNFFEKKVGEYQKAGVMSSERSSKVFSLDADF
Protein: Uncharacterized protein Rv2667 (P9WPC7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- ATP-dependent Clp protease adapter protein ClpS
- ATP-dependent Clp protease proteolytic subunit 1
- Conserved hypothetical proline rich protein
- Hypothetical alanine and valine rich protein
- Chaperone protein DnaK
- Conserved hypothetical proline and threonine rich protein
- Protein GrpE
- ATP-dependent Clp protease proteolytic subunit 2
- Possible exported alanine and valine rich protein
- Uncharacterized N-acetyltransferase Rv2669
Sequence:
MPEPTPTAYPVRLDELINAIKRVHSDVLDQLSDAVLAAEHLGEIADHLIGHFVDQARRSGASWSDIGKSMGVTKQAAQKRFVPRAEATTLDSNQGFRRFTPRARNAVVAAQNAAHGAASSEITPDHLLLGVLTDPAALATALLQQQEIDIATLRTAVTLPPAVTEPPQPIPFSGPARKVLELTFREALRLGHNYIGTEHLLLALLELEDGDGPLHRSGVDKSRAEADLITTLASLTGANAAGATDAGATDAG
Protein: Suppressor of fused homolog (Q27279)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR011844}. Nucleus {ECO:0000256|PIRNR:PIRNR011844}.
Interaction partners:
Sequence:
MAEANLDKKPEVKPPPGLKAIIDHLGQVYPNQPNPLQVTTLLKYWLGGQDPLDYISMYKFPGDVDRNVPPHWHYISFGLSDLHGDERVHLREEGVTRSGMGFELTFRLAKTEIELKQQIENPEKPQRAPTWPANLLQAIGRYCFQTGNGLCFGDNIPWRKSLDGSTTSKLQNLLVAQDPQLGCIDTPTGTVDFCQIVGVFDDELEQASRWNGRGVLNFLRQDMQTGGDWLVTNMDRQMSVFELFPETLLNLQDDLEKQGSDLAGVNADFSFRELKPTKEVKEEVDFQALSEKCANDENNRQLTDTQMKREEPSFPQSMSMSSNSLHKSCPLDFQAQAPNCISLDGIEITLAPGVAKYLLLAIKDRIRHGRHFTFKAQHLALTLVAESVTGSAVTVNEPYGVLGYWIQVLIPDELVPRLMEDFCSAGLDEKCEPKERLELEWPDKNLKLIIDQPEPVLPMSLDAAPLKM
Protein: Phosphotransferase (EC 2.7.1.-) (Q4WHC3)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Mannitol-1-phosphate 5-dehydrogenase
- Glucose-6-phosphate isomerase
- Phosphoglucomutase
- ATP-dependent 6-phosphofructokinase
- Phosphomannomutase
- Phosphoglucomutase, putative
- Mannose-6-phosphate isomerase
- Phosphoglucomutase, putative
- Beta-fructofuranosidase, putative
- Exoinulinase InuD
Sequence:
MVGIGPKRPPSRKGSMADVPQNLLQQIKDFEEMFTVDKAKLKQVVDHFVKELDKGLSVEGGNIPMNVTWVMGFPDGDEQGTFLALDMGGTNLRVCEITLTEEKGGFDICQSKYRMPEELKTGTAEELWEYIADCIQQFIEFHHGEEGLTSLPLGFTFSYPATQEYIDHGILQRWTKGFDIDGVEGQDVVPPLEETLKRKGLPIKVAALINDTTGTLIASAYTDPEMKIGCIFGTGVNAAYMENVGSVPKLAHMNLPPDMPVAINCEYGAFDNEHVVLPLTKYDHIIDRDSPRPGQQAFEKMTAGLYLGEIFRLALIDLLDSRPGLIFQNQDTSKLRKPYLLDASFLAAIEEDPYENLQETQELFERELNIKPTLAELEMIRRLAELIGTRAARLSACGVAAICKKKNIESCHVGADGSVFTKYPHFKARGAQALREILDWAPNEKDKVTIMAAEDGSGVGAALIAALTLKRVKAGNLAGIRNKDEMQKLL
Protein: Paired box protein Pax-9 (P47242)
Organism: Mus musculus (Mouse)
Function: Transcription factor required for normal development of thymus, parathyroid glands, ultimobranchial bodies, teeth, skeletal elements of skull and larynx as well as distal limbs.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein MSX-1
- Lysine-specific demethylase 5B
- Protein odd-skipped-related 2
Sequence:
MEPAFGEVNQLGGVFVNGRPLPNAIRLRIVELAQLGIRPCDISRQLRVSHGCVSKILARYNETGSILPGAIGGSKPRVTTPTVVKHIRTYKQRDPGIFAWEIRDRLLADGVCDKYNVPSVSSISRILRNKIGNLAQQGHYDSYKQHQPAPQPALPYNHIYSYPSPITAAAAKVPTPPGVPAIPGSVALPRTWPSSHSVTDILGIRSITDQGVSDSSPYHSPKVEEWSSLGRNNFPAAAPHAVNGLEKGALEQEAKYGQAPNGLPAVSSFVSASSMAPYPTPAQVSPYMTYSAAPSGYVAGHGWQHAGSTPLSPHNCDIPASLAFKGMQAAREGSHSVTASAL
Protein: Protein HIRA homolog (Protein sesame) (dHIRA) (O17468)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the periodic repression of histone gene transcription during the cell cycle (By similarity). Required for replication-independent chromatin assembly. Promotes remodeling of sperm chromatin following fertilization via the incorporation of histone H3.3 and histone H4.
Subcellular location: Nucleus {ECO:0000269|PubMed:16251970}. Note=Maternally contributed protein localizes specifically to the male nucleus in fertilized eggs. This localization persists from the initiation of sperm nucleus decondensation to the end of pronucleus formation.
Interaction partners:
- Histone chaperone asf1
- yemanuclein
- Chromatin assembly factor 1 p55 subunit
- FI18641p1
- Protein hedgehog
- Protein patched
Sequence:
MRLLKPAWVHHDDKQIFSVDIHKDCTKFATGGQGSDCGRVVIWNLLPVLSDKAEFDADVPKMLCQMDQHLACVNCVRWSQNGQNLASGSDDKLIMIWRKSAGSSGVFGTGGMQKNHESWKCFYTLRGHDGDVLDLAWSPNDVYLASCSIDNTVIIWDAQAFPHSVATLKGHTGLVKGVSWDPLGRFLASQSDDRSIKIWNTMNWSLSHTITEPFEECGGTTHILRLSWSPDGQYLVSAHAMNGGGPTAQIIEREGWKCDKDFVGHRKAVTCVRFHNSILSRQENDGSPSKPLQYCCLAVGSRDRSLSVWMTALQRPMVVIHELFNASILDLTWGPQECLLMACSVDGSIACLKFTEEELGKAISEEEQNAIIRKMYGKNYVNGLGKSAPVLEHPQRLLLPQGDKPTKFPLSNNNEANQRPISKQTETRTKDGKRRITPMFIPLHEDGPTSLSMNIVSSSGSSTTALTSCSAAIGTLPAAAPTESAATPLMPLEPLVSKIDLGRLDSRLKTQPASQRRQSLPFDPGQSNELLRTPRLEEHQSSTCSPSNLNVTATGKSEFVKAALDYRLHVSNGHLKTQHGMLAKVTASDSKEMLWEFYVGSPLVNLNLCEKYAMLCSLDGSMRLISMETGCPVFPAISLTSSAVHCAFSPDNSLVGVLTECGLLRIWDIAKKVVSLAAGCLELLNKHGTAAQFSVTNQGMPLIGFPSGNSYSYSTSLQSWLVLATKDAIMYHGIRGTLPRDMDQMQQKFPLLSMQASSQNYFSFTGSMELRHSESWQQCAKIRFIENQIKLCEALQSLDELQHWHKMLTFQLATHGSEKRMRVFLDDLLSMPEPGISQFVPKLELMQCVLDTLKPHSEWNRLHSEYTELLKECKSERQKDIFATPAPPQQKTASSAGSSPRSGEATGEEVTEKDGATAVAAAVVAGSRMAVTTGTSTTTTTTASSSLSSSGSSSSTSGSGSSSSSSSTSSLSVPQPAPSLSPEIQTLDSPTVCIDDEILSASSSLPPLDTSPVEVSPASTSGGAASTSPAASVAGSAPVSSSKTDQT
Protein: UBD (Ubiquitin-like protein FAT10) (A0A1U9X8S6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPNASCLCVHVRSEEWDLMTFDANPYDSVKKIKEHVRSKTKVPVQDQVLLLGSKILKPRRSLSSYGIDKEKTIHLTLKVVKPSDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAMIETKTGIIPETQIVTCNGKRLEDGKMMADYGIRKGNLLFLACYCIGG