Q9ULV0 (MYO5B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Unconventional myosin-Vb

Gene names

Name:	MYO5B
Synonyms:	KIAA1119

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	1848 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Required in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Together with RAB11A participates in CFTR trafficking to the plasma membrane and TF (transferrin) recycling in nonpolarized cells. Together with RAB11A and RAB8A participates in epithelial cell polarization. Together with RAB25 regulates transcytosis By similarity. Ref.7 Ref.9 Ref.11
Subunit structure	Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Interacts with RAB11FIP2, RAB11A, and RAB8A. Found in a complex with CFTR and RAB11A. Interacts with NPC1L1. Ref.5 Ref.6 Ref.7 Ref.9 Ref.11
Involvement in disease	Diarrhea 2, with microvillus atrophy (DIAR2) [MIM:251850]: A disease characterized by onset of intractable life-threatening watery diarrhea during infancy. Two forms are recognized: early-onset microvillus inclusion disease with diarrhea beginning in the neonatal period, and late-onset, with first symptoms appearing after 3 or 4 months of life. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12
Sequence similarities	Contains 1 dilute domain. Contains 6 IQ domains. Contains 1 myosin head-like domain.
Sequence caution	The sequence BAA86433.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Protein transport Transport
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Coiled coil Repeat
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Motor protein Myosin
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW transmembrane transport Traceable author statement. Source: Reactome vesicle-mediated transport Inferred from mutant phenotype Ref.7. Source: UniProtKB water transport Traceable author statement. Source: Reactome
Cellular_component	cytoplasmic vesicle membrane Traceable author statement. Source: Reactome myosin complex Inferred from electronic annotation. Source: UniProtKB-KW protein complex Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microfilament motor activity Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1848	1848	Unconventional myosin-Vb		PRO_0000123460
Regions
	Domain	1 – 764	764	Myosin head-like
	Domain	769 – 798	30	IQ 1
	Domain	792 – 821	30	IQ 2
	Domain	817 – 848	32	IQ 3
	Domain	840 – 869	30	IQ 4
	Domain	865 – 896	32	IQ 5
	Domain	888 – 917	30	IQ 6
	Domain	1526 – 1803	278	Dilute
	Nucleotide binding	163 – 170	8	ATP Potential
	Region	640 – 662	23	Actin-binding Potential
	Coiled coil	899 – 1266	368	Potential
	Coiled coil	1341 – 1471	131	Potential
	Compositional bias	801 – 916	116	Arg-rich
Amino acid modifications
	Modified residue	1446	1	Phosphoserine Ref.10
Natural variations
	Natural variant	10	1	C → G. Corresponds to variant rs16951438 [ dbSNP | Ensembl ].		VAR_056182
	Natural variant	108	1	V → G in DIAR2. Ref.12		VAR_054993
	Natural variant	126	1	T → A. Ref.1 Ref.3 Corresponds to variant rs1815930 [ dbSNP | Ensembl ].		VAR_063141
	Natural variant	219	1	R → H in DIAR2. Ref.12		VAR_054994
	Natural variant	307	1	K → N. Corresponds to variant rs17659179 [ dbSNP | Ensembl ].		VAR_056183
	Natural variant	656	1	R → C in DIAR2. Ref.12		VAR_054995
	Natural variant	918	1	R → H. Corresponds to variant rs2298624 [ dbSNP | Ensembl ].		VAR_056184
	Natural variant	942	1	K → R. Corresponds to variant rs2277716 [ dbSNP | Ensembl ].		VAR_056185
	Natural variant	1055	1	L → LL. Ref.1 Ref.3 Corresponds to variant rs72530399 [ dbSNP | Ensembl ].		VAR_063142
Experimental info
	Mutagenesis	1300	1	Q → L: Abolishes interaction with RAB8A and has no effect on RAB11A interaction; when associated with C-1307. Ref.11
	Mutagenesis	1307	1	Y → C: Abolishes interaction with RAB8A and has no effect on RAB11A interaction; when associated with L-1300. Ref.11
	Mutagenesis	1714	1	Y → E: Abolishes interaction with RAB11A; has no effect on RAB8A interaction. Ref.11
	Mutagenesis	1748	1	Q → R: Abolishes interaction with RAB11A; has no effect on RAB8A interaction. Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Q9ULV0 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 4EB8FA02F6B38707	FASTA	1,848	213,672
	10 20 30 40 50 60 MSVGELYSQC TRVWIPDPDE VWRSAELTKD YKEGDKSLQL RLEDETILEY PIDVQRNQLP 70 80 90 100 110 120 FLRNPDILVG ENDLTALSYL HEPAVLHNLK VRFLESNHIY TYCGIVLVAI NPYEQLPIYG 130 140 150 160 170 180 QDVIYTYSGQ NMGDMDPHIF AVAEEAYKQM ARDEKNQSII VSGESGAGKT VSAKYAMRYF 190 200 210 220 230 240 ATVGGSASET NIEEKVLASS PIMEAIGNAK TTRNDNSSRF GKYIQIGFDK RYHIIGANMR 250 260 270 280 290 300 TYLLEKSRVV FQADDERNYH IFYQLCAAAG LPEFKELALT SAEDFFYTSQ GGDTSIEGVD 310 320 330 340 350 360 DAEDFEKTRQ AFTLLGVKES HQMSIFKIIA SILHLGSVAI QAERDGDSCS ISPQDVYLSN 370 380 390 400 410 420 FCRLLGVEHS QMEHWLCHRK LVTTSETYVK TMSLQQVINA RNALAKHIYA QLFGWIVEHI 430 440 450 460 470 480 NKALHTSLKQ HSFIGVLDIY GFETFEVNSF EQFCINYANE KLQQQFNSHV FKLEQEEYMK 490 500 510 520 530 540 EQIPWTLIDF YDNQPCIDLI EAKLGILDLL DEECKVPKGT DQNWAQKLYD RHSSSQHFQK 550 560 570 580 590 600 PRMSNTAFII VHFADKVEYL SDGFLEKNRD TVYEEQINIL KASKFPLVAD LFHDDKDPVP 610 620 630 640 650 660 ATTPGKGSSS KISVRSARPP MKVSNKEHKK TVGHQFRTSL HLLMETLNAT TPHYVRCIKP 670 680 690 700 710 720 NDEKLPFHFD PKRAVQQLRA CGVLETIRIS AAGYPSRWAY HDFFNRYRVL VKKRELANTD 730 740 750 760 770 780 KKAICRSVLE NLIKDPDKFQ FGRTKIFFRA GQVAYLEKLR ADKFRTATIM IQKTVRGWLQ 790 800 810 820 830 840 KVKYHRLKGA TLTLQRYCRG HLARRLAEHL RRIRAAVVLQ KHYRMQRARQ AYQRVRRAAV 850 860 870 880 890 900 VIQAFTRAMF VRRTYRQVLM EHKATTIQKH VRGWMARRHF QRLRDAAIVI QCAFRMLKAR 910 920 930 940 950 960 RELKALRIEA RSAEHLKRLN VGMENKVVQL QRKIDEQNKE FKTLSEQLSV TTSTYTMEVE 970 980 990 1000 1010 1020 RLKKELVHYQ QSPGEDTSLR LQEEVESLRT ELQRAHSERK ILEDAHSREK DELRKRVADL 1030 1040 1050 1060 1070 1080 EQENALLKDE KEQLNNQILC QSKDEFAQNS VKENLMKKEL EEERSRYQNL VKEYSQLEQR 1090 1100 1110 1120 1130 1140 YDNLRDEMTI IKQTPGHRRN PSNQSSLESD SNYPSISTSE IGDTEDALQQ VEEIGLEKAA 1150 1160 1170 1180 1190 1200 MDMTVFLKLQ KRVRELEQER KKLQVQLEKR EQQDSKKVQA EPPQTDIDLD PNADLAYNSL 1210 1220 1230 1240 1250 1260 KRQELESENK KLKNDLNELR KAVADQATQN NSSHGSPDSY SLLLNQLKLA HEELEVRKEE 1270 1280 1290 1300 1310 1320 VLILRTQIVS ADQRRLAGRN AEPNINARSS WPNSEKHVDQ EDAIEAYHGV CQTNSKTEDW 1330 1340 1350 1360 1370 1380 GYLNEDGELG LAYQGLKQVA RLLEAQLQAQ SLEHEEEVEH LKAQLEALKE EMDKQQQTFC 1390 1400 1410 1420 1430 1440 QTLLLSPEAQ VEFGVQQEIS RLTNENLDLK ELVEKLEKNE RKLKKQLKIY MKKAQDLEAA 1450 1460 1470 1480 1490 1500 QALAQSERKR HELNRQVTVQ RKEKDFQGML EYHKEDEALL IRNLVTDLKP QMLSGTVPCL 1510 1520 1530 1540 1550 1560 PAYILYMCIR HADYTNDDLK VHSLLTSTIN GIKKVLKKHN DDFEMTSFWL SNTCRLLHCL 1570 1580 1590 1600 1610 1620 KQYSGDEGFM TQNTAKQNEH CLKNFDLTEY RQVLSDLSIQ IYQQLIKIAE GVLQPMIVSA 1630 1640 1650 1660 1670 1680 MLENESIQGL SGVKPTGYRK RSSSMADGDN SYCLEAIIRQ MNAFHTVMCD QGLDPEIILQ 1690 1700 1710 1720 1730 1740 VFKQLFYMIN AVTLNNLLLR KDVCSWSTGM QLRYNISQLE EWLRGRNLHQ SGAVQTMEPL 1750 1760 1770 1780 1790 1800 IQAAQLLQLK KKTQEDAEAI CSLCTSLSTQ QIVKILNLYT PLNEFEERVT VAFIRTIQAQ 1810 1820 1830 1840 LQERNDPQQL LLDAKHMFPV LFPFNPSSLT MDSIHIPACL NLEFLNEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain." Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O. DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-126 AND LEU-1055 INS. Tissue: Brain.
[2]	Ohara O., Nagase T., Yamakawa H., Kikuno R. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO N-TERMINUS AND 918.
[3]	"Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free recombination: preparation of full-length cDNA clones encoding motor proteins." Yamakawa H., Kikuno R.F., Nagase T., Ohara O. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-126 AND LEU-1055 INS. Tissue: Brain.
[4]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Identification and characterization of a family of Rab11-interacting proteins." Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R. J. Biol. Chem. 276:39067-39075(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB11FIP2.
[6]	"CART: an Hrs/actinin-4/BERP/myosin V protein complex required for efficient receptor recycling." Yan Q., Sun W., Kujala P., Lotfi Y., Vida T.A., Bean A.J. Mol. Biol. Cell 16:2470-2482(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CART COMPLEX.
[7]	"Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells." Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S., Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E., Langford G.M., Fukuda M., Stanton B.A. J. Biol. Chem. 282:23725-23736(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAB11A, IDENTIFICATION IN A COMPLEX WITH RAB11A AND CFTR.
[8]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface." Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., Song B.-L. J. Biol. Chem. 284:22481-22490(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NPC1L1.
[10]	"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-1446, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization." Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R. Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAB11A AND RAB8A, MUTAGENESIS OF GLN-1300; TYR-1307; TYR-1714 AND GLN-1748.
[12]	"MYO5B mutations cause microvillus inclusion disease and disrupt epithelial cell polarity." Mueller T., Hess M.W., Schiefermeier N., Pfaller K., Ebner H.L., Heinz-Erian P., Ponstingl H., Partsch J., Roellinghoff B., Koehler H., Berger T., Lenhartz H., Schlenck B., Houwen R.J., Taylor C.J., Zoller H., Lechner S., Goulet O. , Utermann G., Ruemmele F.M., Huber L.A., Janecke A.R. Nat. Genet. 40:1163-1165(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DIAR2 GLY-108; HIS-219 AND CYS-656.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB032945 mRNA. Translation: BAA86433.2. Different initiation. AB290160 mRNA. Translation: BAG06714.1. AC090227 Genomic DNA. No translation available. AC092705 Genomic DNA. No translation available. AC105224 Genomic DNA. No translation available.
IPI	IPI00479962.
RefSeq	NP_001073936.1. NM_001080467.2.
UniGene	Hs.720076.
3D structure databases
ProteinModelPortal	Q9ULV0.
SMR	Q9ULV0. Positions 5-816, 1501-1797.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ULV0. 3 interactions.
MINT	MINT-1209283.
STRING	9606.ENSP00000285039.
PTM databases
PhosphoSite	Q9ULV0.
Polymorphism databases
DMDM	296439293.
Proteomic databases
PaxDb	Q9ULV0.
PRIDE	Q9ULV0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000285039; ENSP00000285039; ENSG00000167306.
GeneID	4645.
KEGG	hsa:4645.
UCSC	uc002leb.2. human.
Organism-specific databases
CTD	4645.
GeneCards	GC18M047349.
H-InvDB	HIX0014446.
HGNC	HGNC:7603. MYO5B.
HPA	HPA040593. HPA040902.
MIM	251850. phenotype. 606540. gene.
neXtProt	NX_Q9ULV0.
Orphanet	2290. Microvillous inclusion disease.
PharmGKB	PA31408.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5022.
HOGENOM	HOG000171839.
HOVERGEN	HBG052556.
InParanoid	Q9ULV0.
KO	K10357.
OMA	SQMEHWL.
OrthoDB	EOG4KPT8Z.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	Q9ULV0.
Bgee	Q9ULV0.
CleanEx	HS_MYO5B.
Genevestigator	Q9ULV0.
GermOnline	ENSG00000167306. Homo sapiens.
Family and domain databases
InterPro	IPR018444. Dil_domain. IPR002710. Dilute. IPR000048. IQ_motif_EF-hand-BS. IPR001609. Myosin_head_motor_dom. [Graphical view]
Pfam	PF01843. DIL. 1 hit. PF00612. IQ. 6 hits. PF00063. Myosin_head. 1 hit. [Graphical view]
PRINTS	PR00193. MYOSINHEAVY.
SMART	SM00015. IQ. 6 hits. SM00242. MYSc. 1 hit. [Graphical view]
PROSITE	PS51126. DILUTE. 1 hit. PS50096. IQ. 6 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MYO5B. human.
GenomeRNAi	4645.
NextBio	17900.
SOURCE	Search...

Entry information

Entry name

MYO5B_HUMAN

Accession

Primary (citable) accession number: Q9ULV0
Secondary accession number(s): B0I1R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 121 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.