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Protein

Regulator of microtubule dynamics protein 3

Gene

RMDN3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis.2 Publications

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • cellular calcium ion homeostasis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of microtubule dynamics protein 3
Short name:
RMD-3
Short name:
hRMD-3
Alternative name(s):
Cerebral protein 10
Protein FAM82A2
Protein FAM82C
Protein tyrosine phosphatase-interacting protein 51
TCPTP-interacting protein 51
Gene namesi
Name:RMDN3
Synonyms:FAM82A2, FAM82C, PTPIP51
ORF Names:hucep-10, UNQ3122/PRO10274
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:25550. RMDN3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei13 – 3523HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Microtubule, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162387926.

Polymorphism and mutation databases

BioMutaiRMDN3.
DMDMi147643203.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Regulator of microtubule dynamics protein 3PRO_0000287510Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei46 – 461PhosphoserineCombined sources
Modified residuei50 – 501PhosphoserineCombined sources
Modified residuei57 – 571PhosphoserineBy similarity
Modified residuei183 – 1831PhosphoserineCombined sources
Modified residuei193 – 1931PhosphoserineCombined sources
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei232 – 2321PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96TC7.
MaxQBiQ96TC7.
PaxDbiQ96TC7.
PeptideAtlasiQ96TC7.
PRIDEiQ96TC7.
TopDownProteomicsiQ96TC7-1. [Q96TC7-1]
Q96TC7-2. [Q96TC7-2]

PTM databases

iPTMnetiQ96TC7.
PhosphoSiteiQ96TC7.
SwissPalmiQ96TC7.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

By EGF, TGFB1, retinoic acid-and 1,25-dihydroxyvitamin D3.1 Publication

Gene expression databases

BgeeiQ96TC7.
CleanExiHS_FAM82A2.
ExpressionAtlasiQ96TC7. baseline and differential.
GenevisibleiQ96TC7. HS.

Organism-specific databases

HPAiHPA009975.

Interactioni

Subunit structurei

Interacts with PTPN2. Interacts with microtubules. Interacts with VAPB.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN1P180314EBI-1056589,EBI-968788
YWHABP319465EBI-1056589,EBI-359815

Protein-protein interaction databases

BioGridi120476. 34 interactions.
IntActiQ96TC7. 16 interactions.
MINTiMINT-1631442.
STRINGi9606.ENSP00000260385.

Structurei

3D structure databases

ProteinModelPortaliQ96TC7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili92 – 12433Sequence analysisAdd
BLAST

Domaini

The transmembrane region is required for mitochondrial localization.

Sequence similaritiesi

Belongs to the RMDN family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IIGM. Eukaryota.
ENOG41101S6. LUCA.
GeneTreeiENSGT00530000063162.
HOVERGENiHBG072518.
InParanoidiQ96TC7.
OMAiEVRSHME.
OrthoDBiEOG7BP834.
PhylomeDBiQ96TC7.
TreeFamiTF315854.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR011990. TPR-like_helical_dom.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96TC7-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSRLGALGGA RAGLGLLLGT AAGLGFLCLL YSQRWKRTQR HGRSQSLPNS
60 70 80 90 100
LDYTQTSDPG RHVMLLRAVP GGAGDASVLP SLPREGQEKV LDRLDFVLTS
110 120 130 140 150
LVALRREVEE LRSSLRGLAG EIVGEVRCHM EENQRVARRR RFPFVRERSD
160 170 180 190 200
STGSSSVYFT ASSGATFTDA ESEGGYTTAN AESDNERDSD KESEDGEDEV
210 220 230 240 250
SCETVKMGRK DSLDLEEEAA SGASSALEAG GSSGLEDVLP LLQQADELHR
260 270 280 290 300
GDEQGKREGF QLLLNNKLVY GSRQDFLWRL ARAYSDMCEL TEEVSEKKSY
310 320 330 340 350
ALDGKEEAEA ALEKGDESAD CHLWYAVLCG QLAEHESIQR RIQSGFSFKE
360 370 380 390 400
HVDKAIALQP ENPMAHFLLG RWCYQVSHLS WLEKKTATAL LESPLSATVE
410 420 430 440 450
DALQSFLKAE ELQPGFSKAG RVYISKCYRE LGKNSEARWW MKLALELPDV
460 470
TKEDLAIQKD LEELEVILRD
Length:470
Mass (Da):52,118
Last modified:May 15, 2007 - v2
Checksum:i1C8D1022E6CF7B6A
GO
Isoform 2 (identifier: Q96TC7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-129: Missing.

Note: No experimental confirmation available.
Show »
Length:341
Mass (Da):38,247
Checksum:i6015D71ECA057A27
GO

Sequence cautioni

The sequence BAB15298.1 differs from that shown. Reason: Erroneous termination at position 453. Translated as Glu.Curated
The sequence BAC85554.1 differs from that shown. Reason: Frameshift at position 383. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti416 – 4161F → V in BAB46923 (Ref. 1) Curated
Sequence conflicti469 – 4691R → Q in BAC85554 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331Q → H.
Corresponds to variant rs11558807 [ dbSNP | Ensembl ].
VAR_049029

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 129129Missing in isoform 2. 1 PublicationVSP_025531Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000782 mRNA. Translation: BAB46923.1.
AY358793 mRNA. Translation: AAQ89153.1.
AK001441 mRNA. Translation: BAA91693.1.
AK025963 mRNA. Translation: BAB15298.1. Sequence problems.
AK092058 mRNA. Translation: BAG52475.1.
AK123282 mRNA. Translation: BAG53885.1.
AK123192 mRNA. Translation: BAC85554.1. Frameshift.
CH471125 Genomic DNA. Translation: EAW92436.1.
BC008970 mRNA. Translation: AAH08970.2.
BC063844 mRNA. Translation: AAH63844.1.
AJ242719 Genomic DNA. Translation: CAC39480.1.
BR000691 mRNA. Translation: FAA00416.1.
CCDSiCCDS10063.1. [Q96TC7-1]
RefSeqiNP_001291731.1. NM_001304802.1. [Q96TC7-1]
NP_060615.1. NM_018145.2. [Q96TC7-1]
XP_005254588.1. XM_005254531.1. [Q96TC7-1]
UniGeneiHs.511067.
Hs.632944.

Genome annotation databases

EnsembliENST00000260385; ENSP00000260385; ENSG00000137824. [Q96TC7-1]
ENST00000338376; ENSP00000342493; ENSG00000137824. [Q96TC7-1]
GeneIDi55177.
KEGGihsa:55177.
UCSCiuc001zmp.1. human. [Q96TC7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000782 mRNA. Translation: BAB46923.1.
AY358793 mRNA. Translation: AAQ89153.1.
AK001441 mRNA. Translation: BAA91693.1.
AK025963 mRNA. Translation: BAB15298.1. Sequence problems.
AK092058 mRNA. Translation: BAG52475.1.
AK123282 mRNA. Translation: BAG53885.1.
AK123192 mRNA. Translation: BAC85554.1. Frameshift.
CH471125 Genomic DNA. Translation: EAW92436.1.
BC008970 mRNA. Translation: AAH08970.2.
BC063844 mRNA. Translation: AAH63844.1.
AJ242719 Genomic DNA. Translation: CAC39480.1.
BR000691 mRNA. Translation: FAA00416.1.
CCDSiCCDS10063.1. [Q96TC7-1]
RefSeqiNP_001291731.1. NM_001304802.1. [Q96TC7-1]
NP_060615.1. NM_018145.2. [Q96TC7-1]
XP_005254588.1. XM_005254531.1. [Q96TC7-1]
UniGeneiHs.511067.
Hs.632944.

3D structure databases

ProteinModelPortaliQ96TC7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120476. 34 interactions.
IntActiQ96TC7. 16 interactions.
MINTiMINT-1631442.
STRINGi9606.ENSP00000260385.

PTM databases

iPTMnetiQ96TC7.
PhosphoSiteiQ96TC7.
SwissPalmiQ96TC7.

Polymorphism and mutation databases

BioMutaiRMDN3.
DMDMi147643203.

Proteomic databases

EPDiQ96TC7.
MaxQBiQ96TC7.
PaxDbiQ96TC7.
PeptideAtlasiQ96TC7.
PRIDEiQ96TC7.
TopDownProteomicsiQ96TC7-1. [Q96TC7-1]
Q96TC7-2. [Q96TC7-2]

Protocols and materials databases

DNASUi55177.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260385; ENSP00000260385; ENSG00000137824. [Q96TC7-1]
ENST00000338376; ENSP00000342493; ENSG00000137824. [Q96TC7-1]
GeneIDi55177.
KEGGihsa:55177.
UCSCiuc001zmp.1. human. [Q96TC7-1]

Organism-specific databases

CTDi55177.
GeneCardsiRMDN3.
HGNCiHGNC:25550. RMDN3.
HPAiHPA009975.
MIMi611873. gene.
neXtProtiNX_Q96TC7.
PharmGKBiPA162387926.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIGM. Eukaryota.
ENOG41101S6. LUCA.
GeneTreeiENSGT00530000063162.
HOVERGENiHBG072518.
InParanoidiQ96TC7.
OMAiEVRSHME.
OrthoDBiEOG7BP834.
PhylomeDBiQ96TC7.
TreeFamiTF315854.

Miscellaneous databases

GenomeRNAii55177.
PROiQ96TC7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96TC7.
CleanExiHS_FAM82A2.
ExpressionAtlasiQ96TC7. baseline and differential.
GenevisibleiQ96TC7. HS.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR011990. TPR-like_helical_dom.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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] (ISOFORMS 1 AND 2).
    Tissue: Amygdala and Teratocarcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Brain and Uterus.
  6. "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.
  7. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH PTPN2.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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] [Europe PMC] [Abstract]
    Cited for: INDUCTION, SUBCELLULAR LOCATION.
  12. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis."
    De Vos K.J., Morotz G.M., Stoica R., Tudor E.L., Lau K.F., Ackerley S., Warley A., Shaw C.E., Miller C.C.
    Hum. Mol. Genet. 21:1299-1311(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELLULAR CALCIUM HOMEOSTASIS REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH VAPB.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-183; SER-193; SER-212 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRMD3_HUMAN
AccessioniPrimary (citable) accession number: Q96TC7
Secondary accession number(s): A9UMZ9
, B3KRR3, Q6ZWE9, Q96H23, Q96SD6, Q9H6G1, Q9NVQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: June 8, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.