MYH16_HUMAN
ID MYH16_HUMAN Reviewed; 1097 AA.
AC Q9H6N6;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Putative uncharacterized protein MYH16 {ECO:0000305};
DE AltName: Full=Myosin heavy chain 16 pseudogene {ECO:0000312|HGNC:HGNC:31038};
DE AltName: Full=myosin heavy polypeptide 5 {ECO:0000312|HGNC:HGNC:31038};
GN Name=MYH16 {ECO:0000312|HGNC:HGNC:31038};
GN Synonyms=MYH5 {ECO:0000312|HGNC:HGNC:31038};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-740.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND CAUTION.
RX PubMed=15042088; DOI=10.1038/nature02358;
RA Stedman H.H., Kozyak B.W., Nelson A., Thesier D.M., Su L.T., Low D.W.,
RA Bridges C.R., Shrager J.B., Minugh-Purvis N., Mitchell M.A.;
RT "Myosin gene mutation correlates with anatomical changes in the human
RT lineage.";
RL Nature 428:415-418(2004).
RN [4]
RP CAUTION.
RX PubMed=16376411; DOI=10.1016/j.jhevol.2005.10.003;
RA McCollum M.A., Sherwood C.C., Vinyard C.J., Lovejoy C.O., Schachat F.;
RT "Of muscle-bound crania and human brain evolution: the story behind the
RT MYH16 headlines.";
RL J. Hum. Evol. 50:232-236(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CAUTION.
RX PubMed=24240322; DOI=10.1038/nmeth.2732;
RA Branca R.M., Orre L.M., Johansson H.J., Granholm V., Huss M.,
RA Perez-Bercoff A., Forshed J., Kaell L., Lehtioe J.;
RT "HiRIEF LC-MS enables deep proteome coverage and unbiased proteogenomics.";
RL Nat. Methods 11:59-62(2014).
CC -!- FUNCTION: Has most probably lost the function in masticatory muscles
CC contraction suspected for its homologs in dog (AC F1PT61) and apes.
CC {ECO:0000303|PubMed:15042088}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in muscles of the head
CC including temporalis and tensor veli palatini.
CC {ECO:0000269|PubMed:15042088}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: An inactivating mutation in MYH16 probably appeared 2.4
CC million years ago in a hominid ancestor (PubMed:15042088). The
CC inactivation and its correlation with evolution of the skull and
CC cranial capacity in hominids is not clear (PubMed:15042088,
CC PubMed:16376411). However, the gene is transcribed and the N-terminally
CC truncated protein shown here was detected in a human cell line
CC (PubMed:24240322). Its biological significance remains unclear since it
CC lacks most of the domains important for the function of myosins
CC (PubMed:15042088). {ECO:0000269|PubMed:15042088,
CC ECO:0000269|PubMed:16376411, ECO:0000269|PubMed:24240322}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15219.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AC004834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK025690; BAB15219.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; Q9H6N6; -.
DR SMR; Q9H6N6; -.
DR IntAct; Q9H6N6; 1.
DR iPTMnet; Q9H6N6; -.
DR PhosphoSitePlus; Q9H6N6; -.
DR BioMuta; HGNC:31038; -.
DR jPOST; Q9H6N6; -.
DR MassIVE; Q9H6N6; -.
DR PeptideAtlas; Q9H6N6; -.
DR PRIDE; Q9H6N6; -.
DR GeneCards; MYH16; -.
DR HGNC; HGNC:31038; MYH16.
DR neXtProt; NX_Q9H6N6; -.
DR PathwayCommons; Q9H6N6; -.
DR SignaLink; Q9H6N6; -.
DR Pharos; Q9H6N6; Tdark.
DR PRO; PR:Q9H6N6; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9H6N6; protein.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR Gene3D; 1.20.5.370; -; 4.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF01576; Myosin_tail_1; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Reference proteome.
FT CHAIN 1..1097
FT /note="Putative uncharacterized protein MYH16"
FT /id="PRO_0000433095"
FT COILED 31..1087
FT /evidence="ECO:0000255"
FT CONFLICT 11
FT /note="H -> R (in Ref. 2; BAB15219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1097 AA; 128290 MW; DC459CD5FA5D0BC4 CRC64;
MGLKVIQQNV HKFLQLRFWG WWKLYNKVKP LLNVARQEEE MKAKEEELRK AMAQTQELVN
KVKELEEKTA TLSQEKNDLT IQLQAEQENL MDAEERLTWM MKTKMDLESQ ISDMRERLEE
EEGMAASLSA AKRKLEGELS DLKRDLEGLE TTLAKTEKEK QALDHKVRTL TGDLSLREDS
ITKLQKEKRA LEELHQKTLD DLQAEEDKVN HLTKNNSKLS TQIHELEDNW EQEKKIRAEV
EKARRKAESD LKMTIDNLNE MERSKLDLEE VVKKRDLEIN SVNSKYEDEQ SLNSTLQRKL
KEHQDRIEEL EEELEAERAM RAKIEQNRKR EAELLKLRRE LEEAALQSEA TASTLRKKHV
DSMAELTEHV ESLQRVKSKL EKDKQVMKAE IDDLNASMET IQKSKMNAEA HVRKLEDSLS
EANAKVAELE RNQAEINAIR TRLQAENSEL SREYEESQSR LNQILRIKTS LTSQVDDYKR
QLDEESKSRS TAVVSLANTK HDLDLVKEQL EEEQGGKSEL QRLVSKLNTE VTTWRTKYET
DAIQRTEELE ETKRKLAARL QEAEEAAETA QARAASLEKN KQRLQAEVED LTIDLEKANA
AAAALDKKQR LFDKMLAEWQ QKCEELQVEV DSSQKECRMY MTESFKIKTA YEESLEHLES
VKKENKTLQE EIKDLIDQLG EGGRSVHELQ KLKKKLEMEK EELQVALEEA ESSLEVEESK
VIRIQLELAQ VKADIDRRIH EKEEEFEATR KNHQRAIESL QASLEAEAKG RAEALRLKKK
METDLNEMEI QLDHANKNNS ELVKTLKRLQ QQIKDLQVQM DEDARQHEEL RKQYNLQERR
LSLLQTELEE VRSALEGSER SRKLLEQEVV EITEWHNEIN IQNQSLLVVK RKLESDVQRI
SNEHEELISE FRLTEERAKK AMMDAARMAE ELRQEQDHCM HLEKIKKNYE VTIKDLQAKM
EEAEQLALKG GKRTIMKLEA RIKELETELD GEQKQHVETV KTLCKNERRL KELVFQTEED
HKTNQRMQAL VEKLQNKLKV YKRQIEEAED QANQTLARYR KTVHELDDAE DRAGMAETAL
NKLRTRHRVA GKGITSV