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Q8IXI2 (MIRO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial Rho GTPase 1

Short name=MIRO-1
Short name=hMiro-1
EC=3.6.5.-
Alternative name(s):
Rac-GTP-binding protein-like protein
Ras homolog gene family member T1
Gene names
Name:RHOT1
Synonyms:ARHT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length618 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. Ref.2 Ref.9

Subunit structure

Interacts with the kinesin-binding proteins TRAK1/OIP106 and TRAK2/GRIF1, forming a link between mitochondria and the trafficking apparatus of the microtubules. Ref.9

Subcellular location

Mitochondrion outer membrane; Single-pass type IV membrane protein. Note: Colocalizes with MGARP and RHOT2 at the mitochondria. Ref.2 Ref.10

Tissue specificity

Ubiquitously expressed. Expressed at high level in heart and skeletal muscle. Ref.2

Sequence similarities

Belongs to the mitochondrial Rho GTPase family.

Contains 2 EF-hand domains.

Contains 2 Miro domains.

Sequence caution

The sequence AAH41114.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH68463.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA91969.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB14185.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IXI2-1)

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 2 (identifier: Q8IXI2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     580-580: P → PEDHYRDRLSRDMGHTDRIENLRKIWVFLKTAL
Isoform 3 (identifier: Q8IXI2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     580-580: P → PEDHYRDRLSRDMGHTDRIENLRKIWVFLKTAFHARLRCMCTCNRCTFCICQNFLNSDLLQSVKNKIFTAVLNR
Isoform 4 (identifier: Q8IXI2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     581-618: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8IXI2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     582-618: VTQADLKSST...AMYKALLKQR → ARLRCMCTCN...TAVLNRIISA
Note: No experimental confirmation available.
Isoform 6 (identifier: Q8IXI2-6)

The sequence of this isoform differs from the canonical sequence as follows:
     224-247: QALEDVKNVVRKHISDGVADSGLT → RFGFEQVLVLLFLQFWALLCTKHY
     248-618: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q8IXI2-7)

The sequence of this isoform differs from the canonical sequence as follows:
     580-580: P → PHARLRCMCTCNRCTFCICQNFLNSDLLQSVKNKIFTAVLNR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 618618Mitochondrial Rho GTPase 1
PRO_0000239313

Regions

Topological domain1 – 592592Mitochondrial intermembrane Potential
Transmembrane593 – 61523Helical; Anchor for type IV membrane protein; Potential
Topological domain616 – 6183Cytoplasmic Potential
Domain1 – 177177Miro 1
Domain184 – 21936EF-hand 1
Domain304 – 33936EF-hand 2
Domain412 – 561150Miro 2
Nucleotide binding11 – 188GTP 1
Nucleotide binding57 – 615GTP 1 Potential
Nucleotide binding118 – 1214GTP 1 Potential
Calcium binding197 – 208121 Probable
Calcium binding317 – 328122 Probable
Nucleotide binding425 – 4328GTP 2
Nucleotide binding463 – 4675GTP 2 Potential
Nucleotide binding527 – 5304GTP 2 Potential

Natural variations

Alternative sequence224 – 24724QALED…DSGLT → RFGFEQVLVLLFLQFWALLC TKHY in isoform 6.
VSP_019153
Alternative sequence248 – 618371Missing in isoform 6.
VSP_019154
Alternative sequence5801P → PEDHYRDRLSRDMGHTDRIE NLRKIWVFLKTAL in isoform 2.
VSP_019155
Alternative sequence5801P → PEDHYRDRLSRDMGHTDRIE NLRKIWVFLKTAFHARLRCM CTCNRCTFCICQNFLNSDLL QSVKNKIFTAVLNR in isoform 3.
VSP_019156
Alternative sequence5801P → PHARLRCMCTCNRCTFCICQ NFLNSDLLQSVKNKIFTAVL NR in isoform 7.
VSP_047651
Alternative sequence581 – 61838Missing in isoform 4.
VSP_019157
Alternative sequence582 – 61837VTQAD…LLKQR → ARLRCMCTCNRCTFCICQNF LNSDLLQSVKNKIFTAVLNR IISA in isoform 5.
VSP_019158

Experimental info

Mutagenesis131P → V: Causes constitutive activation inducing an aggregation of the mitochondrial network. Ref.2 Ref.8 Ref.9
Mutagenesis181T → N: Causes constitutive inactivation. Ref.2 Ref.9
Mutagenesis2081E → K: Abolishes the formation of thread-like mitochondria. Ref.9
Mutagenesis3281E → K: Abolishes the formation of thread-like mitochondria. Ref.9
Mutagenesis4271K → V: No effect. Ref.9
Mutagenesis4321S → N: No effect. Ref.9
Sequence conflict751A → V in AAM15734. Ref.3
Sequence conflict2461L → F in AAH60781. Ref.7
Sequence conflict2461L → F in BAA91969. Ref.5
Sequence conflict3311D → G in AAH60781. Ref.7
Sequence conflict5871L → P in CAD56956. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: FE47AC3A4AF6F6C2

FASTA61870,784
        10         20         30         40         50         60 
MKKDVRILLV GEPRVGKTSL IMSLVSEEFP EEVPPRAEEI TIPADVTPER VPTHIVDYSE 

        70         80         90        100        110        120 
AEQSDEQLHQ EISQANVICI VYAVNNKHSI DKVTSRWIPL INERTDKDSR LPLILVGNKS 

       130        140        150        160        170        180 
DLVEYSSMET ILPIMNQYTE IETCVECSAK NLKNISELFY YAQKAVLHPT GPLYCPEEKE 

       190        200        210        220        230        240 
MKPACIKALT RIFKISDQDN DGTLNDAELN FFQRICFNTP LAPQALEDVK NVVRKHISDG 

       250        260        270        280        290        300 
VADSGLTLKG FLFLHTLFIQ RGRHETTWTV LRRFGYDDDL DLTPEYLFPL LKIPPDCTTE 

       310        320        330        340        350        360 
LNHHAYLFLQ STFDKHDLDR DCALSPDELK DLFKVFPYIP WGPDVNNTVC TNERGWITYQ 

       370        380        390        400        410        420 
GFLSQWTLTT YLDVQRCLEY LGYLGYSILT EQESQASAVT VTRDKKIDLQ KKQTQRNVFR 

       430        440        450        460        470        480 
CNVIGVKNCG KSGVLQALLG RNLMRQKKIR EDHKSYYAIN TVYVYGQEKY LLLHDISESE 

       490        500        510        520        530        540 
FLTEAEIICD VVCLVYDVSN PKSFEYCARI FKQHFMDSRI PCLIVAAKSD LHEVKQEYSI 

       550        560        570        580        590        600 
SPTDFCRKHK MPPPQAFTCN TADAPSKDIF VKLTTMAMYP HVTQADLKSS TFWLRASFGA 

       610 
TVFAVLGFAM YKALLKQR 

« Hide

Isoform 2 [UniParc].

Checksum: 9E2A92E79F9160E1
Show »

FASTA65074,752
Isoform 3 [UniParc].

Checksum: 478FF7C2F8DD1986
Show »

FASTA69179,547
Isoform 4 [UniParc].

Checksum: EC42DCCD95811BC3
Show »

FASTA58066,541
Isoform 5 [UniParc].

Checksum: 3968C61EE9945024
Show »

FASTA62571,687
Isoform 6 [UniParc].

Checksum: 3802160B22935376
Show »

FASTA24728,265
Isoform 7 [UniParc].

Checksum: 82C8A91A753D656F
Show »

FASTA65975,546

References

« Hide 'large scale' references
[1]"Complete physical map and gene content of the human NF1 tumor suppressor region in human and mouse."
Jenne D.E., Tinschert S., Dorschner M.O., Hameister H., Stephens K., Kehrer-Sawatzki H.
Genes Chromosomes Cancer 37:111-120(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[2]"Atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis."
Fransson A., Ruusala A., Aspenstroem P.
J. Biol. Chem. 278:6495-6502(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-13 AND THR-18.
[3]"Cloning a novel Rac-GTP binding protein-like gene from human fetal brain."
Zeng L., Xie Y., Mao Y.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Fetal brain.
[4]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Uterus.
[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. expand/collapse author list , 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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-618 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-618 (ISOFORM 3).
Tissue: Amygdala, Placenta and Teratocarcinoma.
[6]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-618 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-550 (ISOFORM 6).
Tissue: Brain, Lung, Testis and Uterus.
[8]"Rho GTPases have diverse effects on the organization of the actin filament system."
Aspenstroem P., Fransson A., Saras J.
Biochem. J. 377:327-337(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PRO-13.
[9]"The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking."
Fransson S., Ruusala A., Aspenstroem P.
Biochem. Biophys. Res. Commun. 344:500-510(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TRAK1 AND TRAK2, MUTAGENESIS OF PRO-13; THR-18; GLU-208; GLU-328; LYS-427 AND SER-432.
[10]"HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial distribution and transport."
Li Y., Lim S., Hoffman D., Aspenstrom P., Federoff H.J., Rempe D.A.
J. Cell Biol. 185:1065-1081(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ496730 mRNA. Translation: CAD43139.1.
AJ517412 mRNA. Translation: CAD56956.1.
AY094972 mRNA. Translation: AAM15734.1.
AL136929 mRNA. Translation: CAB66863.1.
AK001902 mRNA. Translation: BAA91969.1. Different initiation.
AK022695 mRNA. Translation: BAB14185.1. Different initiation.
AK294407 mRNA. Translation: BAG57659.1.
AC116407 Genomic DNA. No translation available.
AC026620 Genomic DNA. No translation available.
BC015698 mRNA. Translation: AAH15698.1.
BC041114 mRNA. Translation: AAH41114.1. Different initiation.
BC051818 mRNA. Translation: AAH51818.1.
BC060781 mRNA. Translation: AAH60781.2.
BC068463 mRNA. Translation: AAH68463.1. Different initiation.
BC125104 mRNA. Translation: AAI25105.1.
BC125105 mRNA. Translation: AAI25106.1.
CCDSCCDS32610.1. [Q8IXI2-3]
CCDS32611.1. [Q8IXI2-7]
CCDS32612.1. [Q8IXI2-1]
RefSeqNP_001028738.1. NM_001033566.2. [Q8IXI2-7]
NP_001028739.2. NM_001033567.2.
NP_001028740.1. NM_001033568.2. [Q8IXI2-3]
NP_001275683.1. NM_001288754.1. [Q8IXI2-2]
NP_001275684.1. NM_001288755.1.
NP_001275687.1. NM_001288758.1.
NP_060777.3. NM_018307.4. [Q8IXI2-1]
UniGeneHs.655325.

3D structure databases

ProteinModelPortalQ8IXI2.
SMRQ8IXI2. Positions 6-159, 180-581.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120576. 8 interactions.
IntActQ8IXI2. 9 interactions.
MINTMINT-3972897.

PTM databases

PhosphoSiteQ8IXI2.

Polymorphism databases

DMDM108860796.

Proteomic databases

MaxQBQ8IXI2.
PaxDbQ8IXI2.
PRIDEQ8IXI2.

Protocols and materials databases

DNASU55288.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333942; ENSP00000334724; ENSG00000126858. [Q8IXI2-1]
ENST00000358365; ENSP00000351132; ENSG00000126858. [Q8IXI2-3]
ENST00000394692; ENSP00000378184; ENSG00000126858. [Q8IXI2-2]
ENST00000545287; ENSP00000439737; ENSG00000126858. [Q8IXI2-7]
ENST00000581031; ENSP00000464094; ENSG00000126858. [Q8IXI2-5]
ENST00000581094; ENSP00000462669; ENSG00000126858. [Q8IXI2-4]
GeneID55288.
KEGGhsa:55288.
UCSCuc002hgv.3. human. [Q8IXI2-1]
uc002hgw.3. human. [Q8IXI2-3]
uc010wby.2. human. [Q8IXI2-2]

Organism-specific databases

CTD55288.
GeneCardsGC17P030470.
HGNCHGNC:21168. RHOT1.
HPAHPA010687.
MIM613888. gene.
neXtProtNX_Q8IXI2.
PharmGKBPA134906318.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOVERGENHBG079778.
KOK07870.
OMAHEISQAN.
OrthoDBEOG7PK8Z0.
PhylomeDBQ8IXI2.
TreeFamTF300814.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ8IXI2.
BgeeQ8IXI2.
CleanExHS_RHOT1.
GenevestigatorQ8IXI2.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
3.40.50.300. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR013566. EF_hand_assoc_1.
IPR013567. EF_hand_assoc_2.
IPR002048. EF_hand_dom.
IPR020860. MIRO.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR021181. Rho_GTPase_Mt.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamPF13405. EF-hand_6. 1 hit.
PF08355. EF_assoc_1. 1 hit.
PF08356. EF_assoc_2. 1 hit.
PF08477. Miro. 1 hit.
PF00071. Ras. 1 hit.
[Graphical view]
PIRSFPIRSF037488. Mt_Rho_GTPase. 1 hit.
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS51423. MIRO. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRHOT1. human.
GeneWikiRHOT1.
GenomeRNAi55288.
NextBio59462.
PROQ8IXI2.
SOURCESearch...

Entry information

Entry nameMIRO1_HUMAN
AccessionPrimary (citable) accession number: Q8IXI2
Secondary accession number(s): A4FVB6 expand/collapse secondary AC list , A6NFV0, B4DG48, J9JIH9, Q6NUR3, Q6P9F8, Q6PJG1, Q6YMW8, Q86UB0, Q8IW28, Q8IXJ7, Q9H067, Q9H9N8, Q9NUZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM