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Reviewed, UniProtKB/Swiss-Prot Q96TC7 (RMD3_HUMAN)

Last modified July 7, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Regulator of microtubule dynamics protein 3
      Short name=RMD-3
      Short name=hRMD-3
Alternative name(s):
    Protein FAM82A2
    Protein FAM82C
    Protein tyrosine phosphatase-interacting protein 51
    TCPTP-interacting protein 51
    Cerebral protein 10
Gene names
Name: FAM82A2
Synonyms: FAM82C, PTPIP51
ORF Names: hucep-10, UNQ3122/PRO10274
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis. Ref.8

Subunit structure

Interacts with PTPN2. Interacts with microtubules. Ref.6 Ref.7

Subcellular location

Mitochondrion membrane; Single-pass membrane protein. Cytoplasm. Nucleus. Note: In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. Ref.8 Ref.6 Ref.9

Tissue specificity

Present at high level in epidermis and seminiferous epithelium: while basal cells in the epidermis and spermatogonia show no perceptible amount, keratinocytes of suprabasal layers and differentiating first-order spermatocytes up to spermatids exhibit high expression. In skeletal muscle, its presence is restricted to fibers of the fast twitch type. In surface epithelia containing ciliated cells, it is associated with the microtubular structures responsible for ciliary movement. Also present in specific structures of the central nervous system such as neurons of the hippocampal region, ganglion cells of the autonomic nervous system, and axons of the peripheral nervous system (at protein level). Widely expressed. Ref.8 Ref.7

Induction

By EGF, TGF-beta, retinoic acid-and 1,25-Dihydroxyvitamin D3. Ref.9

Domain

The transmembrane region is required for mitochondrial localization.

Sequence similarities

Belongs to the FAM82/RMD family.

Sequence caution

The sequence BAB15298.1 differs from that shown. Reason: Erroneous termination at position 453. Translated as Glu.

The sequence BAC85554.1 differs from that shown. Reason: Frameshift at position 383.

Ontologies

Keywords
   Biological processApoptosis
Differentiation
   Cellular componentCytoplasm
Membrane
Microtubule
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Transmembrane
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processapoptosis

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96TC7-1)

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: Q96TC7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-129: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470Regulator of microtubule dynamics protein 3
PRO_0000287510

Regions

Transmembrane13 – 3523 Potential
Coiled coil92 – 12433 Potential

Amino acid modifications

Modified residue441Phosphoserine Ref.12
Modified residue461Phosphoserine Ref.10 Ref.11
Modified residue1891Phosphoserine By similarity
Modified residue2121Phosphoserine Ref.12

Natural variations

Alternative sequence1 – 129129Missing in isoform 2.
VSP_025531
Natural variant331Q → H: dbSNP rs11558807.
VAR_049029

Experimental info

Sequence conflict4161F → V in BAB46923. Ref.1
Sequence conflict4691R → Q in BAC85554. Ref.3

Sequences

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

Last modified May 15, 2007. Version 2.
Checksum: 1C8D1022E6CF7B6A

FASTA47052,118
        10         20         30         40         50         60 
MSRLGALGGA RAGLGLLLGT AAGLGFLCLL YSQRWKRTQR HGRSQSLPNS LDYTQTSDPG 

        70         80         90        100        110        120 
RHVMLLRAVP GGAGDASVLP SLPREGQEKV LDRLDFVLTS LVALRREVEE LRSSLRGLAG 

       130        140        150        160        170        180 
EIVGEVRCHM EENQRVARRR RFPFVRERSD STGSSSVYFT ASSGATFTDA ESEGGYTTAN 

       190        200        210        220        230        240 
AESDNERDSD KESEDGEDEV SCETVKMGRK DSLDLEEEAA SGASSALEAG GSSGLEDVLP 

       250        260        270        280        290        300 
LLQQADELHR GDEQGKREGF QLLLNNKLVY GSRQDFLWRL ARAYSDMCEL TEEVSEKKSY 

       310        320        330        340        350        360 
ALDGKEEAEA ALEKGDESAD CHLWYAVLCG QLAEHESIQR RIQSGFSFKE HVDKAIALQP 

       370        380        390        400        410        420 
ENPMAHFLLG RWCYQVSHLS WLEKKTATAL LESPLSATVE DALQSFLKAE ELQPGFSKAG 

       430        440        450        460        470 
RVYISKCYRE LGKNSEARWW MKLALELPDV TKEDLAIQKD LEELEVILRD 

« Hide

Isoform 2.

Checksum: 6015D71ECA057A27
Show »

FASTA34138,247

References

« Hide 'large scale' references
[1]"Molecular cloning of a novel gene expressed in human cerebral cortex."
Yoshimoto M., Yazaki M., Matsumoto K., Takayama K.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Teratocarcinoma.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Uterus.
[5]"A protein interacting with T-cell tyrosine phosphatase."
Porsche A., Hofer W.H.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-470.
[6]"RMD-1, a novel microtubule-associated protein, functions in chromosome segregation in Caenorhabditis elegans."
Oishi K., Okano H., Sawa H.
J. Cell Biol. 179:1149-1162(2007) [PubMed: 18070910] [Abstract]
Cited for: IDENTIFICATION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[7]"The novel protein PTPIP51 exhibits tissue- and cell-specific expression."
Stenzinger A., Kajosch T., Tag C., Porsche A., Welte I., Hofer H.W., Steger K., Wimmer M.
Histochem. Cell Biol. 123:19-28(2005) [PubMed: 15609043] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH PTPN2.
[8]"Protein tyrosine phosphatase interacting protein 51 (PTPIP51) is a novel mitochondria protein with an N-terminal mitochondrial targeting sequence and induces apoptosis."
Lv B.F., Yu C.F., Chen Y.Y., Lu Y., Guo J.H., Song Q.S., Ma D.L., Shi T.P., Wang L.
Apoptosis 11:1489-1501(2006) [PubMed: 16820967] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"Epidermal growth factor-, transforming growth factor-beta-, retinoic acid-and 1,25-dihydroxyvitamin D(3)-regulated expression of the novel protein PTPIP51 in keratinocytes."
Stenzinger A., Schreiner D., Pfeiffer T., Tag C., Hofer H.W., Wimmer M.
Cells Tissues Organs 184:76-87(2006) [PubMed: 17361080] [Abstract]
Cited for: INDUCTION, SUBCELLULAR LOCATION.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY.
[11]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY.
[12]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-212, MASS SPECTROMETRY.
[13]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

AB000782 mRNA. Translation: BAB46923.1.
AY358793 mRNA. Translation: AAQ89153.1.
AK001441 mRNA. Translation: BAA91693.1.
AK025963 mRNA. Translation: BAB15298.1. Sequence problems.
AK123192 mRNA. Translation: BAC85554.1. Frameshift.
BC008970 mRNA. Translation: AAH08970.2.
BC063844 mRNA. Translation: AAH63844.1.
AJ242719 Genomic DNA. Translation: CAC39480.1.
BR000691 mRNA. Translation: FAA00416.1.
IPIIPI00410079.
IPI00845345.
RefSeqNP_060615.1.
UniGeneHs.511067

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ96TC7. 2 interactions.

PTM databases

PhosphoSiteQ96TC7.

Proteomic databases

PeptideAtlasQ96TC7.
PRIDEQ96TC7.

Genome annotation databases

EnsemblENSG00000137824. Homo sapiens. [Contig view]
GeneID55177.
KEGGhsa:55177.
UCSCuc001zmo.1. human.

Organism-specific databases

GeneCardsGC15M038817.
HGNCHGNC:25550. FAM82A2.
HPAHPA009975.
MIM611873. gene.
PharmGKBPA142671850.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ96TC7.
HOVERGENQ96TC7.
OMAQ96TC7. EVRSHME.

Gene expression databases

ArrayExpressQ96TC7.
BgeeQ96TC7.
CleanExHS_FAM82A2.

Family and domain databases

InterProIPR011990. TPR-like_helical.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 1 hit.
ProtoNetSearch...

Other Resources

NextBio58979.
SOURCESearch...

Entry information

Entry nameRMD3_HUMAN
AccessionPrimary (citable) accession number: Q96TC7
Secondary accession number(s): A9UMZ9 expand/collapse secondary AC list , Q6ZWE9, Q96H23, Q96SD6, Q9H6G1, Q9NVQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: July 7, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents