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Q9H6Z4

- RANB3_HUMAN

UniProt

Q9H6Z4 - RANB3_HUMAN

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Protein

Ran-binding protein 3

Gene

RANBP3

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

Functioni

Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export.5 Publications

GO - Molecular functioni

  1. Ran GTPase binding Source: ProtInc
  2. R-SMAD binding Source: UniProtKB

GO - Biological processi

  1. intracellular transport Source: InterPro
  2. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

SignaLinkiQ9H6Z4.

Names & Taxonomyi

Protein namesi
Recommended name:
Ran-binding protein 3
Short name:
RanBP3
Gene namesi
Name:RANBP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9850. RANBP3.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34211.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 567566Ran-binding protein 3PRO_0000097165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei9 – 91N6-acetyllysineBy similarity
Modified residuei21 – 211N6-acetyllysine1 Publication
Modified residuei100 – 1001Phosphoserine1 Publication
Modified residuei101 – 1011Phosphoserine1 Publication
Modified residuei108 – 1081Phosphoserine2 Publications
Modified residuei124 – 1241Phosphothreonine1 Publication
Modified residuei219 – 2191PhosphoserineBy similarity
Modified residuei333 – 3331Phosphoserine3 Publications
Modified residuei353 – 3531Phosphoserine1 Publication
Modified residuei355 – 3551Phosphoserine1 Publication
Modified residuei539 – 5391Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H6Z4.
PaxDbiQ9H6Z4.
PeptideAtlasiQ9H6Z4.
PRIDEiQ9H6Z4.

PTM databases

PhosphoSiteiQ9H6Z4.

Expressioni

Tissue specificityi

Widely expressed with high levels in testis and heart.1 Publication

Gene expression databases

BgeeiQ9H6Z4.
CleanExiHS_RANBP3.
ExpressionAtlasiQ9H6Z4. baseline and differential.
GenevestigatoriQ9H6Z4.

Organism-specific databases

HPAiHPA043375.
HPA043389.

Interactioni

Subunit structurei

Interacts with CHC1 in a Ran-stimulated manner. Interacts with XPO1. Interacts (via its C-terminal R domain) with SMAD2 (dephosphorylated form via its MH1 and MH2 domains); the interaction results in the nuclear export of SMAD2 and termination of the TGF-beta signaling. Interacts (via its C-terminal R domain) with SMAD3 (dephosphorylated form via its MH1 domain); the interaction results in the nuclear export of SMAD3 and termination of the TGF-beta signaling.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPM1AP358134EBI-992681,EBI-989143
RCC1P187542EBI-992681,EBI-992720
SMAD2Q157962EBI-992681,EBI-1040141

Protein-protein interaction databases

BioGridi114070. 37 interactions.
IntActiQ9H6Z4. 7 interactions.
MINTiMINT-3068756.
STRINGi9606.ENSP00000341483.

Structurei

Secondary structure

1
567
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni389 – 3913
Beta strandi399 – 41214
Turni413 – 4164
Beta strandi417 – 43216
Turni434 – 4363
Beta strandi439 – 4479
Turni448 – 4503
Beta strandi453 – 4586
Beta strandi465 – 4695
Beta strandi472 – 4765
Beta strandi487 – 4915
Helixi494 – 51926

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CRFNMR-A380-516[»]
2Y8FX-ray2.10A/B/C/D388-522[»]
2Y8GX-ray1.61A/B388-522[»]
ProteinModelPortaliQ9H6Z4.
SMRiQ9H6Z4. Positions 390-516.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H6Z4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini378 – 518141RanBD1PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi76 – 816Poly-Pro
Compositional biasi537 – 5437Poly-Asp

Sequence similaritiesi

Contains 1 RanBD1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG304969.
GeneTreeiENSGT00530000063644.
HOVERGENiHBG061383.
InParanoidiQ9H6Z4.
KOiK15304.
OMAiTSFASPN.
OrthoDBiEOG7TJ3JQ.
PhylomeDBiQ9H6Z4.
TreeFamiTF313181.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamiPF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTiSM00160. RanBD. 1 hit.
[Graphical view]
PROSITEiPS50196. RANBD1. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H6Z4-1) [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
MADLANEEKP AIAPPVFVFQ KDKGQKSPAE QKNLSDSGEE PRGEAEAPHH
60 70 80 90 100
GTGHPESAGE HALEPPAPAG ASASTPPPPA PEAQLPPFPR ELAGRSAGGS
110 120 130 140 150
SPEGGEDSDR EDGNYCPPVK RERTSSLTQF PPSQSEERSS GFRLKPPTLI
160 170 180 190 200
HGQAPSAGLP SQKPKEQQRS VLRPAVLQAP QPKALSQTVP SSGTNGVSLP
210 220 230 240 250
ADCTGAVPAA SPDTAAWRSP SEAADEVCAL EEKEPQKNES SNASEEEACE
260 270 280 290 300
KKDPATQQAF VFGQNLRDRV KLINESVDEA DMENAGHPSA DTPTATNYFL
310 320 330 340 350
QYISSSLENS TNSADASSNK FVFGQNMSER VLSPPKLNEV SSDANRENAA
360 370 380 390 400
AESGSESSSQ EATPEKESLA ESAAAYTKAT ARKCLLEKVE VITGEEAESN
410 420 430 440 450
VLQMQCKLFV FDKTSQSWVE RGRGLLRLND MASTDDGTLQ SRLVMRTQGS
460 470 480 490 500
LRLILNTKLW AQMQIDKASE KSIRITAMDT EDQGVKVFLI SASSKDTGQL
510 520 530 540 550
YAALHHRILA LRSRVEQEQE AKMPAPEPGA APSNEEDDSD DDDVLAPSGA
560
TAAGAGDEGD GQTTGST
Length:567
Mass (Da):60,210
Last modified:March 1, 2001 - v1
Checksum:i203B5A900512743C
GO
Isoform 2 (identifier: Q9H6Z4-2) [UniParc]FASTAAdd to Basket

Also known as: Ranbp3-a

The sequence of this isoform differs from the canonical sequence as follows:
     226-230: Missing.

Show »
Length:562
Mass (Da):59,694
Checksum:i453AF2CD380BA7F1
GO
Isoform 3 (identifier: Q9H6Z4-3) [UniParc]FASTAAdd to Basket

Also known as: Ranbp3-b

The sequence of this isoform differs from the canonical sequence as follows:
     27-94: Missing.

Show »
Length:499
Mass (Da):53,411
Checksum:i3356FC66E6A21796
GO

Sequence cautioni

The sequence AAH04349.1 differs from that shown. Reason: Aberrant splicing.
The sequence CAB43293.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti358 – 3592SS → PF in CAA69956. (PubMed:9637251)Curated
Sequence conflicti367 – 3671E → G in CAA69957. (PubMed:9637251)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti314 – 3141A → V.
Corresponds to variant rs10417885 [ dbSNP | Ensembl ].
VAR_051303

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei27 – 9468Missing in isoform 3. 3 PublicationsVSP_011163Add
BLAST
Alternative sequencei226 – 2305Missing in isoform 2. 1 PublicationVSP_011162

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08697 mRNA. Translation: CAA69956.1.
Y08698 mRNA. Translation: CAA69957.1.
AK025300 mRNA. Translation: BAB15106.1.
AK314343 mRNA. Translation: BAG36985.1.
AL050149 mRNA. Translation: CAB43293.1. Different initiation.
AC004602 Genomic DNA. Translation: AAC14485.1.
AC104532 Genomic DNA. No translation available.
AC093050 Genomic DNA. No translation available.
AC005784 Genomic DNA. No translation available.
BC004349 mRNA. Translation: AAH04349.1. Sequence problems.
CCDSiCCDS42477.1. [Q9H6Z4-3]
CCDS42478.1. [Q9H6Z4-1]
CCDS45935.1. [Q9H6Z4-2]
PIRiT08778.
RefSeqiNP_003615.2. NM_003624.2. [Q9H6Z4-2]
NP_015559.2. NM_007320.2. [Q9H6Z4-3]
NP_015561.1. NM_007322.2. [Q9H6Z4-1]
UniGeneiHs.531752.

Genome annotation databases

GeneIDi8498.
KEGGihsa:8498.
UCSCiuc002mdv.3. human. [Q9H6Z4-1]
uc002mdx.3. human. [Q9H6Z4-2]
uc002mdy.3. human. [Q9H6Z4-3]

Polymorphism databases

DMDMi51316528.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08697 mRNA. Translation: CAA69956.1 .
Y08698 mRNA. Translation: CAA69957.1 .
AK025300 mRNA. Translation: BAB15106.1 .
AK314343 mRNA. Translation: BAG36985.1 .
AL050149 mRNA. Translation: CAB43293.1 . Different initiation.
AC004602 Genomic DNA. Translation: AAC14485.1 .
AC104532 Genomic DNA. No translation available.
AC093050 Genomic DNA. No translation available.
AC005784 Genomic DNA. No translation available.
BC004349 mRNA. Translation: AAH04349.1 . Sequence problems.
CCDSi CCDS42477.1. [Q9H6Z4-3 ]
CCDS42478.1. [Q9H6Z4-1 ]
CCDS45935.1. [Q9H6Z4-2 ]
PIRi T08778.
RefSeqi NP_003615.2. NM_003624.2. [Q9H6Z4-2 ]
NP_015559.2. NM_007320.2. [Q9H6Z4-3 ]
NP_015561.1. NM_007322.2. [Q9H6Z4-1 ]
UniGenei Hs.531752.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CRF NMR - A 380-516 [» ]
2Y8F X-ray 2.10 A/B/C/D 388-522 [» ]
2Y8G X-ray 1.61 A/B 388-522 [» ]
ProteinModelPortali Q9H6Z4.
SMRi Q9H6Z4. Positions 390-516.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114070. 37 interactions.
IntActi Q9H6Z4. 7 interactions.
MINTi MINT-3068756.
STRINGi 9606.ENSP00000341483.

PTM databases

PhosphoSitei Q9H6Z4.

Polymorphism databases

DMDMi 51316528.

Proteomic databases

MaxQBi Q9H6Z4.
PaxDbi Q9H6Z4.
PeptideAtlasi Q9H6Z4.
PRIDEi Q9H6Z4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 8498.
KEGGi hsa:8498.
UCSCi uc002mdv.3. human. [Q9H6Z4-1 ]
uc002mdx.3. human. [Q9H6Z4-2 ]
uc002mdy.3. human. [Q9H6Z4-3 ]

Organism-specific databases

CTDi 8498.
GeneCardsi GC19M005916.
HGNCi HGNC:9850. RANBP3.
HPAi HPA043375.
HPA043389.
MIMi 603327. gene.
neXtProti NX_Q9H6Z4.
PharmGKBi PA34211.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG304969.
GeneTreei ENSGT00530000063644.
HOVERGENi HBG061383.
InParanoidi Q9H6Z4.
KOi K15304.
OMAi TSFASPN.
OrthoDBi EOG7TJ3JQ.
PhylomeDBi Q9H6Z4.
TreeFami TF313181.

Enzyme and pathway databases

SignaLinki Q9H6Z4.

Miscellaneous databases

ChiTaRSi RANBP3. human.
EvolutionaryTracei Q9H6Z4.
GeneWikii RANBP3.
GenomeRNAii 8498.
NextBioi 31793.
PROi Q9H6Z4.
SOURCEi Search...

Gene expression databases

Bgeei Q9H6Z4.
CleanExi HS_RANBP3.
ExpressionAtlasi Q9H6Z4. baseline and differential.
Genevestigatori Q9H6Z4.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view ]
Pfami PF00638. Ran_BP1. 1 hit.
[Graphical view ]
SMARTi SM00160. RanBD. 1 hit.
[Graphical view ]
PROSITEi PS50196. RANBD1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human RanBP3, a group of nuclear RanGTP binding proteins."
    Mueller L., Cordes V.C., Bischoff F.R., Ponstingl H.
    FEBS Lett. 427:330-336(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CHC1.
  2. "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 3).
    Tissue: Colon and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  4. "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].
  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] OF 1-418 (ISOFORM 3).
    Tissue: Eye.
  6. "RanBP3 influences interactions between CRM1 and its nuclear protein export substrates."
    Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W., Kutay U.
    EMBO Rep. 2:926-932(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH XPO1.
  7. "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export."
    Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G.
    J. Cell Biol. 153:1391-1402(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH XPO1.
  8. "Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor."
    Nemergut M.E., Lindsay M.E., Brownawell A.M., Macara I.G.
    J. Biol. Chem. 277:17385-17388(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHC1.
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-101; SER-108; THR-124; SER-333; SER-353; SER-355 AND SER-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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].
  13. "Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling."
    Dai F., Lin X., Chang C., Feng X.H.
    Dev. Cell 16:345-357(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMAD2 AND SMAD3, SUBCELLULAR LOCATION, FUNCTION.
  14. "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-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. "Solution structure of the RAN_BP1 domain of RAN-binding protein-3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 380-516.

Entry informationi

Entry nameiRANB3_HUMAN
AccessioniPrimary (citable) accession number: Q9H6Z4
Secondary accession number(s): B2RAT8
, O60405, O75759, O75760, Q9BT47, Q9UG74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 114 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3