Q13459 (MYO9B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Unconventional myosin-IXb

Alternative name(s):
Unconventional myosin-9b

Gene names

Name:	MYO9B
Synonyms:	MYR5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2157 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. May be involved in the remodeling of the actin cytoskeleton. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions. Also acts as a GTPase activating protein on Rho.
Subcellular location	Cytoplasm › cell cortex. Cytoplasm › perinuclear region. Cytoplasm › cytoskeleton. Note: In undifferentiated cells colocalizes with F-actin in the cell periphery while in differentiated cells its localization is cytoplasmic with the highest levels in the perinuclear region.
Tissue specificity	Expressed predominantly in peripheral blood leukocytes and at lower levels, in thymus, spleen, testis, prostate, ovary, brain, small intestine and lung.
Involvement in disease	Celiac disease 4 (CELIAC4) [MIM:609753]: A multifactorial, chronic disorder of the small intestine caused by intolerance to gluten. It is characterized by immune-mediated enteropathy associated with failed intestinal absorption, and malnutrition. In predisposed individuals, the ingestion of gluten-containing food such as wheat and rye induces a flat jejunal mucosa with infiltration of lymphocytes. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.6
Sequence similarities	Contains 4 IQ domains. Contains 1 myosin head-like domain. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 Ras-associating domain. Contains 1 Rho-GAP domain.
Caution	Represents a unconventional myosin. This protein should not be confused with the conventional myosin-9 (MYH9).
Sequence caution	The sequence AAC50402.1 differs from that shown. Reason: The C-terminal sequence from position 1917 onwards appears to be not correctly spliced. The sequence BAA92132.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat Zinc-finger
Ligand	ATP-binding Actin-binding Calmodulin-binding Metal-binding Nucleotide-binding Zinc
Molecular function	GTPase activation Motor protein Myosin
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Inferred by curator Ref.4. Source: UniProtKB actin filament-based movement Traceable author statement Ref.1. Source: UniProtKB
Cellular_component	cell cortex Inferred from direct assay Ref.1. Source: UniProtKB cytosol Traceable author statement. Source: Reactome filamentous actin Inferred from direct assay PubMed 16338935PubMed 16616011Ref.1. Source: UniProtKB myosin complex Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	ADP binding Inferred from direct assay PubMed 16338935. Source: UniProtKB ATP binding Inferred from direct assay PubMed 16338935. Source: UniProtKB ATPase activity Inferred from direct assay PubMed 16338935. Source: UniProtKB Rho GTPase activator activity Inferred from direct assay PubMed 15644318Ref.4. Source: UniProtKB actin binding Inferred from direct assay PubMed 16338935PubMed 16616011Ref.4. Source: UniProtKB calmodulin binding Inferred from direct assay PubMed 16338935Ref.4. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW microfilament motor activity Inferred from direct assay PubMed 11901422PubMed 16616011Ref.4. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARFGEF1	Q9Y6D6	2	EBI-6251250,EBI-1044254

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q13459-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: Q13459-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2021-2022: PP → QY
     2023-2157: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2157	2157	Unconventional myosin-IXb		PRO_0000123469
Regions
	Domain	1 – 939	939	Myosin head-like
	Domain	15 – 114	100	Ras-associating
	Domain	957 – 977	21	IQ 1
	Domain	979 – 1000	22	IQ 2
	Domain	1001 – 1023	23	IQ 3
	Domain	1024 – 1053	30	IQ 4
	Domain	1703 – 1888	186	Rho-GAP
	Nucleotide binding	239 – 246	8	ATP Potential
	Zinc finger	1632 – 1681	50	Phorbol-ester/DAG-type
	Region	844 – 855	12	Actin-binding
	Region	940 – 1044	105	Neck or regulatory domain
	Region	1045 – 2157	1113	Tail
	Coiled coil	1046 – 1071	26	Potential
	Coiled coil	1880 – 1901	22	Potential
	Coiled coil	1959 – 1989	31	Potential
Amino acid modifications
	Modified residue	716	1	Phosphoserine Ref.11
	Modified residue	1242	1	Phosphoserine By similarity
	Modified residue	1267	1	Phosphoserine Ref.9 Ref.13 Ref.16
	Modified residue	1271	1	Phosphothreonine Ref.9 Ref.13 Ref.16
	Modified residue	1290	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16
	Modified residue	1323	1	Phosphoserine Ref.14
	Modified residue	1346	1	Phosphothreonine Ref.14
	Modified residue	1348	1	Phosphothreonine By similarity
	Modified residue	1354	1	Phosphoserine Ref.11 Ref.16
	Modified residue	1405	1	Phosphoserine Ref.10
	Modified residue	1992	1	Phosphoserine Ref.11 Ref.12 Ref.13 Ref.16
Natural variations
	Alternative sequence	2021 – 2022	2	PP → QY in isoform Short.		VSP_003361
	Alternative sequence	2023 – 2157	135	Missing in isoform Short.		VSP_003362
Experimental info
	Sequence conflict	237 – 238	2	IS → YP in AAC50402. Ref.1
	Sequence conflict	276	1	G → C in AAC50402. Ref.1
	Sequence conflict	1011	1	S → A in AAC50402. Ref.1
	Sequence conflict	1693	1	V → A in AAC50402. Ref.1
	Sequence conflict	1946	1	L → P in BAA92132. Ref.4
	Sequence conflict	2039 – 2044	6	TVAAPP → PWPPLH in AAC26597. Ref.3
	Sequence conflict	2048	1	P → L in AAC26597. Ref.3
	Sequence conflict	2066	1	P → S in AAC26597. Ref.3
	Sequence conflict	2156 – 2157	2	NG → MAESHS in AAC26597. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified March 8, 2011. Version 3. Checksum: A3E72CAB759CD5FD	FASTA	2,157	243,401
	10 20 30 40 50 60 MSVKEAGSSG RREQAAYHLH IYPQLSTTES QASCRVTATK DSTTSDVIKD AIASLRLDGT 70 80 90 100 110 120 KCYVLVEVKE SGGEEWVLDA NDSPVHRVLL WPRRAQDEHP QEDGYYFLLQ ERNADGTIKY 130 140 150 160 170 180 VHMQLVAQAT ATRRLVERGL LPRQQADFDD LCNLPELTEG NLLKNLKHRF LQQKIYTYAG 190 200 210 220 230 240 SILVAINPFK FLPIYNPKYV KMYENQQLGK LEPHVFALAD VAYYTMLRKR VNQCIVISGE 250 260 270 280 290 300 SGSGKTQSTN FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI 310 320 330 340 350 360 QVSYLESGIV RGAVVEKYLL EKSRLVSQEK DERNYHVFYY LLLGVSEEER QEFQLKQPED 370 380 390 400 410 420 YFYLNQHNLK IEDGEDLKHD FERLKQAMEM VGFLPATKKQ IFAVLSAILY LGNVTYKKRA 430 440 450 460 470 480 TGREEGLEVG PPEVLDTLSQ LLKVKREILV EVLTKRKTVT VNDKLILPYS LSEAITARDS 490 500 510 520 530 540 MAKSLYSALF DWIVLRINHA LLNKKDVEEA VSCLSIGVLD IFGFEDFERN SFEQFCINYA 550 560 570 580 590 600 NEQLQYYFNQ HIFKLEQEEY QGEGITWHNI GYTDNVGCIH LISKKPTGLF YLLDEESNFP 610 620 630 640 650 660 HATSQTLLAK FKQQHEDNKY FLGTPVMEPA FIIQHFAGKV KYQIKDFREK NMDYMRPDIV 670 680 690 700 710 720 ALLRGSDSSY VRELIGMDPV AVFRWAVLRA AIRAMAVLRE AGRLRAERAE KAAGMSSPGA 730 740 750 760 770 780 QSHPEELPRG ASTPSEKLYR DLHNQMIKSI KGLPWQGEDP RSLLQSLSRL QKPRAFILKS 790 800 810 820 830 840 KGIKQKQIIP KNLLDSKSLK LIISMTLHDR TTKSLLHLHK KKKPPSISAQ FQTSLNKLLE 850 860 870 880 890 900 ALGKAEPFFI RCIRSNAEKK ELCFDDELVL QQLRYTGMLE TVRIRRSGYS AKYTFQDFTE 910 920 930 940 950 960 QFQVLLPKDA QPCREVISTL LEKMKIDKRN YQIGKTKVFL KETERQALQE TLHREVVRKI 970 980 990 1000 1010 1020 LLLQSWFRMV LERRHFLQMK RAAVTIQACW RSYRVRRALE RTQAAVYLQA SWRGYWQRKL 1030 1040 1050 1060 1070 1080 YRHQKQSIIR LQSLCRGHLQ RKSFSQMISE KQKAEEKERE ALEAARAGAE EGGQGQAAGG 1090 1100 1110 1120 1130 1140 QQVAEQGPEP AEDGGHLASE PEVQPSDRSP LEHSSPEKEA PSPEKTLPPQ KTVAAESHEK 1150 1160 1170 1180 1190 1200 VPSSREKRES RRQRGLEHVK FQNKHIQSCK EESALREPSR RVTQEQGVSL LEDKKESRED 1210 1220 1230 1240 1250 1260 ETLLVVETEA ENTSQKQPTE QPQAMAVGKV SEETEKTLPS GSPRPGQLER PTSLALDSRV 1270 1280 1290 1300 1310 1320 SPPAPGSAPE TPEDKSKPCG SPRVQEKPDS PGGSTQIQRY LDAERLASAV ELWRGKKLVA 1330 1340 1350 1360 1370 1380 AASPSAMLSQ SLDLSDRHRA TGAALTPTEE RRTSFSTSDV SKLLPSLAKA QPAAETTDGE 1390 1400 1410 1420 1430 1440 RSAKKPAVQK KKPGDASSLP DAGLSPGSQV DSKSTFKRLF LHKTKDKKYS LEGAEELENA 1450 1460 1470 1480 1490 1500 VSGHVVLEAT TMKKGLEAPS GQQHRHAAGE KRTKEPGGKG KKNRNVKIGK ITVSEKWRES 1510 1520 1530 1540 1550 1560 VFRQITNANE LKYLDEFLLN KINDLRSQKT PIESLFIEAT EKFRSNIKTM YSVPNGKIHV 1570 1580 1590 1600 1610 1620 GYKDLMENYQ IVVSNLATER GQKDTNLVLN LFQSLLDEFT RGYTKNDFEP VKQSKAQKKK 1630 1640 1650 1660 1670 1680 RKQERAVQEH NGHVFASYQV SIPQSCEQCL SYIWLMDKAL LCSVCKMTCH KKCVHKIQSH 1690 1700 1710 1720 1730 1740 CSYTYGRKGE PGVEPGHFGV CVDSLTSDKA SVPIVLEKLL EHVEMHGLYT EGLYRKSGAA 1750 1760 1770 1780 1790 1800 NRTRELRQAL QTDPAAVKLE NFPIHAITGV LKQWLRELPE PLMTFAQYGD FLRAVELPEK 1810 1820 1830 1840 1850 1860 QEQLAAIYAV LEHLPEANHN SLERLIFHLV KVALLEDVNR MSPGALAIIF APCLLRCPDN 1870 1880 1890 1900 1910 1920 SDPLTSMKDV LKITTCVEML IKEQMRKYKV KMEEISQLEA AESIAFRRLS LLRQNAPWPL 1930 1940 1950 1960 1970 1980 KLGFSSPYEG VLNKSPKTRD IQEEELEVLL EEEAAGGDED REKEILIERI QSIKEEKEDI 1990 2000 2010 2020 2030 2040 TYRLPELDPR GSDEENLDSE TSASTESLLE ERAGRGASEG PPAPALPCPG APTPSPLPTV 2050 2060 2070 2080 2090 2100 AAPPRRRPSS FVTVRVKTPR RTPIMPTANI KLPPGLPSHL PRWAPGAREA AAPVRRREPP 2110 2120 2130 2140 2150 ARRPDQIHSV YITPGADLPV QGALEPLEED GQPPGAKRRY SDPPTYCLPP ASGQTNG
	Isoform Short [UniParc]. Checksum: D0E47A7EAF86A929	FASTA	2,022	229,143
	10 20 30 40 50 60 MSVKEAGSSG RREQAAYHLH IYPQLSTTES QASCRVTATK DSTTSDVIKD AIASLRLDGT 70 80 90 100 110 120 KCYVLVEVKE SGGEEWVLDA NDSPVHRVLL WPRRAQDEHP QEDGYYFLLQ ERNADGTIKY 130 140 150 160 170 180 VHMQLVAQAT ATRRLVERGL LPRQQADFDD LCNLPELTEG NLLKNLKHRF LQQKIYTYAG 190 200 210 220 230 240 SILVAINPFK FLPIYNPKYV KMYENQQLGK LEPHVFALAD VAYYTMLRKR VNQCIVISGE 250 260 270 280 290 300 SGSGKTQSTN FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI 310 320 330 340 350 360 QVSYLESGIV RGAVVEKYLL EKSRLVSQEK DERNYHVFYY LLLGVSEEER QEFQLKQPED 370 380 390 400 410 420 YFYLNQHNLK IEDGEDLKHD FERLKQAMEM VGFLPATKKQ IFAVLSAILY LGNVTYKKRA 430 440 450 460 470 480 TGREEGLEVG PPEVLDTLSQ LLKVKREILV EVLTKRKTVT VNDKLILPYS LSEAITARDS 490 500 510 520 530 540 MAKSLYSALF DWIVLRINHA LLNKKDVEEA VSCLSIGVLD IFGFEDFERN SFEQFCINYA 550 560 570 580 590 600 NEQLQYYFNQ HIFKLEQEEY QGEGITWHNI GYTDNVGCIH LISKKPTGLF YLLDEESNFP 610 620 630 640 650 660 HATSQTLLAK FKQQHEDNKY FLGTPVMEPA FIIQHFAGKV KYQIKDFREK NMDYMRPDIV 670 680 690 700 710 720 ALLRGSDSSY VRELIGMDPV AVFRWAVLRA AIRAMAVLRE AGRLRAERAE KAAGMSSPGA 730 740 750 760 770 780 QSHPEELPRG ASTPSEKLYR DLHNQMIKSI KGLPWQGEDP RSLLQSLSRL QKPRAFILKS 790 800 810 820 830 840 KGIKQKQIIP KNLLDSKSLK LIISMTLHDR TTKSLLHLHK KKKPPSISAQ FQTSLNKLLE 850 860 870 880 890 900 ALGKAEPFFI RCIRSNAEKK ELCFDDELVL QQLRYTGMLE TVRIRRSGYS AKYTFQDFTE 910 920 930 940 950 960 QFQVLLPKDA QPCREVISTL LEKMKIDKRN YQIGKTKVFL KETERQALQE TLHREVVRKI 970 980 990 1000 1010 1020 LLLQSWFRMV LERRHFLQMK RAAVTIQACW RSYRVRRALE RTQAAVYLQA SWRGYWQRKL 1030 1040 1050 1060 1070 1080 YRHQKQSIIR LQSLCRGHLQ RKSFSQMISE KQKAEEKERE ALEAARAGAE EGGQGQAAGG 1090 1100 1110 1120 1130 1140 QQVAEQGPEP AEDGGHLASE PEVQPSDRSP LEHSSPEKEA PSPEKTLPPQ KTVAAESHEK 1150 1160 1170 1180 1190 1200 VPSSREKRES RRQRGLEHVK FQNKHIQSCK EESALREPSR RVTQEQGVSL LEDKKESRED 1210 1220 1230 1240 1250 1260 ETLLVVETEA ENTSQKQPTE QPQAMAVGKV SEETEKTLPS GSPRPGQLER PTSLALDSRV 1270 1280 1290 1300 1310 1320 SPPAPGSAPE TPEDKSKPCG SPRVQEKPDS PGGSTQIQRY LDAERLASAV ELWRGKKLVA 1330 1340 1350 1360 1370 1380 AASPSAMLSQ SLDLSDRHRA TGAALTPTEE RRTSFSTSDV SKLLPSLAKA QPAAETTDGE 1390 1400 1410 1420 1430 1440 RSAKKPAVQK KKPGDASSLP DAGLSPGSQV DSKSTFKRLF LHKTKDKKYS LEGAEELENA 1450 1460 1470 1480 1490 1500 VSGHVVLEAT TMKKGLEAPS GQQHRHAAGE KRTKEPGGKG KKNRNVKIGK ITVSEKWRES 1510 1520 1530 1540 1550 1560 VFRQITNANE LKYLDEFLLN KINDLRSQKT PIESLFIEAT EKFRSNIKTM YSVPNGKIHV 1570 1580 1590 1600 1610 1620 GYKDLMENYQ IVVSNLATER GQKDTNLVLN LFQSLLDEFT RGYTKNDFEP VKQSKAQKKK 1630 1640 1650 1660 1670 1680 RKQERAVQEH NGHVFASYQV SIPQSCEQCL SYIWLMDKAL LCSVCKMTCH KKCVHKIQSH 1690 1700 1710 1720 1730 1740 CSYTYGRKGE PGVEPGHFGV CVDSLTSDKA SVPIVLEKLL EHVEMHGLYT EGLYRKSGAA 1750 1760 1770 1780 1790 1800 NRTRELRQAL QTDPAAVKLE NFPIHAITGV LKQWLRELPE PLMTFAQYGD FLRAVELPEK 1810 1820 1830 1840 1850 1860 QEQLAAIYAV LEHLPEANHN SLERLIFHLV KVALLEDVNR MSPGALAIIF APCLLRCPDN 1870 1880 1890 1900 1910 1920 SDPLTSMKDV LKITTCVEML IKEQMRKYKV KMEEISQLEA AESIAFRRLS LLRQNAPWPL 1930 1940 1950 1960 1970 1980 KLGFSSPYEG VLNKSPKTRD IQEEELEVLL EEEAAGGDED REKEILIERI QSIKEEKEDI 1990 2000 2010 2020 TYRLPELDPR GSDEENLDSE TSASTESLLE ERAGRGASEG QY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail." Wirth J.A., Jensen K.A., Post P.L., Bement W.M., Mooseker M.S. J. Cell Sci. 109:653-661(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG/SHORT). Tissue: Liver and Small intestine.
[2]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Cloning of the murine unconventional myosin gene Myo9b and identification of alternative splicing." Grewal P.K., Jones A.-M., Maconochie M., Lemmers R.J.F., Frants R.R., Hewitt J.E. Gene 240:389-398(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[4]	"Human myosin-IXb is a mechanochemically active motor and a GAP for rho." Post P.L., Bokoch G.M., Mooseker M.S. J. Cell Sci. 111:941-950(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1940-2157 (ISOFORM LONG).
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1828-2022 (ISOFORM SHORT). Tissue: Placenta.
[6]	"Myosin IXB variant increases the risk of celiac disease and points toward a primary intestinal barrier defect." Monsuur A.J., de Bakker P.I., Alizadeh B.Z., Zhernakova A., Bevova M.R., Strengman E., Franke L., van't Slot R., van Belzen M.J., Lavrijsen I.C., Diosdado B., Daly M.J., Mulder C.J., Mearin M.L., Meijer J.W., Meijer G.A., van Oort E., Wapenaar M.C., Koeleman B.P., Wijmenga C. Nat. Genet. 37:1341-1344(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH CELIAC DISEASE 4.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290, MASS SPECTROMETRY. Tissue: T-cell.
[9]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1267; THR-1271 AND SER-1290, MASS SPECTROMETRY. Tissue: Platelet.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290 AND SER-1405, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716; SER-1290; SER-1354 AND SER-1992, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290 AND SER-1992, MASS SPECTROMETRY.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1267; THR-1271 AND SER-1992, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290; SER-1323 AND THR-1346, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1267; THR-1271; SER-1290; SER-1354 AND SER-1992, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Wikipedia

MYO9B entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	U42391 mRNA. Translation: AAC50402.1. Sequence problems. AC020913 Genomic DNA. No translation available. AC020908 Genomic DNA. No translation available. AF143684 mRNA. Translation: AAF00119.1. AF020267 mRNA. Translation: AAC26597.1. AK002201 mRNA. Translation: BAA92132.1. Different initiation.
IPI	IPI00306933. IPI00336047.
RefSeq	NP_004136.2. NM_004145.3.
UniGene	Hs.123198. Hs.736097.
3D structure databases
ProteinModelPortal	Q13459.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13459. 7 interactions.
MINT	MINT-1419073.
STRING	9606.ENSP00000380444.
PTM databases
PhosphoSite	Q13459.
Polymorphism databases
DMDM	14548118.
Proteomic databases
PaxDb	Q13459.
PRIDE	Q13459.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000397274; ENSP00000380444; ENSG00000099331. ENST00000595618; ENSP00000471457; ENSG00000099331.
GeneID	4650.
KEGG	hsa:4650.
UCSC	uc002nfi.3. human. uc002nfj.1. human.
Organism-specific databases
CTD	4650.
GeneCards	GC19P017186.
HGNC	HGNC:7609. MYO9B.
HPA	CAB037190. HPA042043.
MIM	602129. gene. 609753. phenotype.
neXtProt	NX_Q13459.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5022.
HOGENOM	HOG000113707.
HOVERGEN	HBG052558.
InParanoid	Q13459.
KO	K10360.
OMA	HLHIYPQ.
OrthoDB	EOG408N75.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q13459.
Bgee	Q13459.
CleanEx	HS_MYO9B.
Genevestigator	Q13459.
GermOnline	ENSG00000099331. Homo sapiens.
Family and domain databases
Gene3D	1.10.555.10. 1 hit.
InterPro	IPR000048. IQ_motif_EF-hand-BS. IPR001609. Myosin_head_motor_dom. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR000159. Ras-assoc. IPR008936. Rho_GTPase_activation_prot. IPR000198. RhoGAP_dom. [Graphical view]
Pfam	PF00612. IQ. 4 hits. PF00063. Myosin_head. 1 hit. PF00788. RA. 1 hit. PF00620. RhoGAP. 1 hit. [Graphical view]
PRINTS	PR00193. MYOSINHEAVY.
SMART	SM00109. C1. 1 hit. SM00015. IQ. 4 hits. SM00242. MYSc. 1 hit. SM00314. RA. 1 hit. SM00324. RhoGAP. 1 hit. [Graphical view]
SUPFAM	SSF48350. Rho_GAP. 1 hit.
PROSITE	PS50096. IQ. 3 hits. PS50200. RA. 1 hit. PS50238. RHOGAP. 1 hit. PS00479. ZF_DAG_PE_1. 1 hit. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MYO9B. human.
GenomeRNAi	4650.
NextBio	17928.
SOURCE	Search...

Entry information

Entry name

MYO9B_HUMAN

Accession

Primary (citable) accession number: Q13459
Secondary accession number(s): O75314, Q9NUJ2, Q9UHN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	March 8, 2011
Last modified:	May 1, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.