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Q96S59

- RANB9_HUMAN

UniProt

Q96S59 - RANB9_HUMAN

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Protein

Ran-binding protein 9

Gene

RANBP9

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

Functioni

May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA (By similarity).By similarity

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. Ran GTPase binding Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Reactome
  2. microtubule nucleation Source: UniProtKB
  3. protein complex assembly Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_22205. L1CAM interactions.
SignaLinkiQ96S59.

Names & Taxonomyi

Protein namesi
Recommended name:
Ran-binding protein 9
Short name:
RanBP9
Alternative name(s):
BPM-L
BPM90
Ran-binding protein M
Short name:
RanBPM
RanBP7
Gene namesi
Name:RANBP9
Synonyms:RANBPM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:13727. RANBP9.

Subcellular locationi

Cytoplasmcytosol. Nucleus
Note: =Predominantly cytoplasmic. A phosphorylated form is associated with the plasma membrane.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. microtubule associated complex Source: ProtInc
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34215.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 729729Ran-binding protein 9PRO_0000097169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei405 – 4051N6-acetyllysine1 Publication
Modified residuei487 – 4871Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated in response to stress. Can be phosphorylated by the cleaved p110 form of CDC2L1 (p110C).3 Publications
Ubiquitinated. Polyubiquitination targets the protein for rapid degradation via the ubiquitin system. Can be deubiquitinated by USP11.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ96S59.
PaxDbiQ96S59.
PRIDEiQ96S59.

PTM databases

PhosphoSiteiQ96S59.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in testes, placenta, heart, and muscle, and lowest levels in lung. Within the brain, expressed predominantly by neurons in the gray matter of cortex, the granular layer of cerebellum and the Purkinje cells.3 Publications

Gene expression databases

BgeeiQ96S59.
CleanExiHS_RANBP9.
ExpressionAtlasiQ96S59. baseline and differential.
GenevestigatoriQ96S59.

Organism-specific databases

HPAiCAB033767.
HPA050007.

Interactioni

Subunit structurei

Interacts with NGFR and DDX4 (By similarity). Interacts with GTP-bound Ran, AR, CDC2L1/p110C, CALB1, S100A7, USP11, MKLN1, SOS1 or SOS2, GID8, and FMR1. Interacts with the Dyrk kinases HIPK2, DYRK1A, and DYRK1B. Interacts with TP73 isoform Alpha but not with TP53. Interacts with the HGF receptor MET and the integrins ITGB1 and ITGB2, but not with ITGAL. Part of a complex consisting of RANBP9, MKLN1 and GID8. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5. Directly interacts with RANBP10.By similarity15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DISC1Q9NRI56EBI-636085,EBI-529989
DYRK1BQ9Y4634EBI-636085,EBI-634187
ENTPD1P499615EBI-636085,EBI-8074749
Grm2P314214EBI-636085,EBI-7090147From a different organism.
OPRM1P353725EBI-636085,EBI-2624570
PPP1CCP36873-23EBI-636085,EBI-3964623
S100A7P311513EBI-636085,EBI-357520

Protein-protein interaction databases

BioGridi115359. 104 interactions.
IntActiQ96S59. 35 interactions.
MINTiMINT-243263.
STRINGi9606.ENSP00000011619.

Structurei

3D structure databases

ProteinModelPortaliQ96S59.
SMRiQ96S59. Positions 216-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 334188B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST
Domaini365 – 39733LisHPROSITE-ProRule annotationAdd
BLAST
Domaini403 – 46058CTLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni401 – 4077Interaction with CALB1Curated
Regioni615 – 729115Interaction with FMR1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 106Poly-Pro
Compositional biasi11 – 188Poly-Gln
Compositional biasi21 – 244Poly-Pro
Compositional biasi25 – 131107Ala-richAdd
BLAST
Compositional biasi62 – 665Poly-Ala
Compositional biasi71 – 777Poly-Pro
Compositional biasi82 – 9211Poly-ProAdd
BLAST

Domaini

The SPRY domain mediates the interaction with MET, AR, and CDC2L1.

Sequence similaritiesi

Belongs to the RANBP9/10 family.Curated
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 CTLH domain.PROSITE-ProRule annotation
Contains 1 LisH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG316575.
GeneTreeiENSGT00530000063160.
HOGENOMiHOG000008133.
HOVERGENiHBG053444.
InParanoidiQ96S59.
OMAiYSNPWAS.
OrthoDBiEOG76MK7Z.
PhylomeDBiQ96S59.
TreeFamiTF331658.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR013144. CRA_dom.
IPR024964. CTLH/CRA.
IPR006595. CTLH_C.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF10607. CLTH. 1 hit.
PF08513. LisH. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00757. CRA. 1 hit.
SM00668. CTLH. 1 hit.
SM00667. LisH. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50897. CTLH. 1 hit.
PS50896. LISH. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96S59-1) [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
MSGQPPPPPP QQQQQQQQLS PPPPAALAPV SGVVLPAPPA VSAGSSPAGS
60 70 80 90 100
PGGGAGGEGL GAAAAALLLH PPPPPPPATA APPPPPPPPP PPASAAAPAS
110 120 130 140 150
GPPAPPGLAA GPGPAGGAPT PALVAGSSAA APFPHGDSAL NEQEKELQRR
160 170 180 190 200
LKRLYPAVDE QETPLPRSWS PKDKFSYIGL SQNNLRVHYK GHGKTPKDAA
210 220 230 240 250
SVRATHPIPA ACGIYYFEVK IVSKGRDGYM GIGLSAQGVN MNRLPGWDKH
260 270 280 290 300
SYGYHGDDGH SFCSSGTGQP YGPTFTTGDV IGCCVNLINN TCFYTKNGHS
310 320 330 340 350
LGIAFTDLPP NLYPTVGLQT PGEVVDANFG QHPFVFDIED YMREWRTKIQ
360 370 380 390 400
AQIDRFPIGD REGEWQTMIQ KMVSSYLVHH GYCATAEAFA RSTDQTVLEE
410 420 430 440 450
LASIKNRQRI QKLVLAGRMG EAIETTQQLY PSLLERNPNL LFTLKVRQFI
460 470 480 490 500
EMVNGTDSEV RCLGGRSPKS QDSYPVSPRP FSSPSMSPSH GMNIHNLASG
510 520 530 540 550
KGSTAHFSGF ESCSNGVISN KAHQSYCHSN KHQSSNLNVP ELNSINMSRS
560 570 580 590 600
QQVNNFTSND VDMETDHYSN GVGETSSNGF LNGSSKHDHE MEDCDTEMEV
610 620 630 640 650
DSSQLRRQLC GGSQAAIERM IHFGRELQAM SEQLRRDCGK NTANKKMLKD
660 670 680 690 700
AFSLLAYSDP WNSPVGNQLD PIQREPVCSA LNSAILETHN LPKQPPLALA
710 720
MGQATQCLGL MARSGIGSCA FATVEDYLH
Length:729
Mass (Da):77,847
Last modified:December 1, 2001 - v1
Checksum:i50DF1127B7FDA6C8
GO
Isoform 2 (identifier: Q96S59-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-341: Missing.

Show »
Length:388
Mass (Da):43,064
Checksum:i28332F38EEB013B8
GO
Isoform 3 (identifier: Q96S59-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-229: Missing.

Note: No experimental confirmation available.

Show »
Length:500
Mass (Da):55,082
Checksum:iCB0A1FD22BCF1B82
GO

Sequence cautioni

The sequence AAH19886.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH52781.1 differs from that shown. Reason: Frameshift at positions 13, 30 and 34.
The sequence AAK15469.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA23216.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871P → S in BAA23216. (PubMed:9817760)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 341341Missing in isoform 2. 1 PublicationVSP_013175Add
BLAST
Alternative sequencei1 – 229229Missing in isoform 3. 1 PublicationVSP_056049Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB055311 mRNA. Translation: BAB62525.1.
AK313334 mRNA. Translation: BAG36138.1.
AL441883, Z93020 Genomic DNA. Translation: CAI19841.1.
Z93020, AL441883 Genomic DNA. Translation: CAI21594.1.
BC019886 mRNA. Translation: AAH19886.1. Sequence problems.
BC052781 mRNA. Translation: AAH52781.1. Frameshift.
BC063849 mRNA. Translation: AAH63849.1.
AB008515 mRNA. Translation: BAA23216.1. Different initiation.
AF306510 mRNA. Translation: AAK15469.1. Different initiation.
CCDSiCCDS4529.1. [Q96S59-1]
RefSeqiNP_005484.2. NM_005493.2. [Q96S59-1]
XP_006715008.1. XM_006714945.1.
UniGeneiHs.708182.

Genome annotation databases

EnsembliENST00000011619; ENSP00000011619; ENSG00000010017. [Q96S59-1]
ENST00000539980; ENSP00000438162; ENSG00000010017. [Q96S59-2]
GeneIDi10048.
KEGGihsa:10048.
UCSCiuc003nba.3. human. [Q96S59-1]

Polymorphism databases

DMDMi61215334.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB055311 mRNA. Translation: BAB62525.1 .
AK313334 mRNA. Translation: BAG36138.1 .
AL441883 , Z93020 Genomic DNA. Translation: CAI19841.1 .
Z93020 , AL441883 Genomic DNA. Translation: CAI21594.1 .
BC019886 mRNA. Translation: AAH19886.1 . Sequence problems.
BC052781 mRNA. Translation: AAH52781.1 . Frameshift.
BC063849 mRNA. Translation: AAH63849.1 .
AB008515 mRNA. Translation: BAA23216.1 . Different initiation.
AF306510 mRNA. Translation: AAK15469.1 . Different initiation.
CCDSi CCDS4529.1. [Q96S59-1 ]
RefSeqi NP_005484.2. NM_005493.2. [Q96S59-1 ]
XP_006715008.1. XM_006714945.1.
UniGenei Hs.708182.

3D structure databases

ProteinModelPortali Q96S59.
SMRi Q96S59. Positions 216-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115359. 104 interactions.
IntActi Q96S59. 35 interactions.
MINTi MINT-243263.
STRINGi 9606.ENSP00000011619.

PTM databases

PhosphoSitei Q96S59.

Polymorphism databases

DMDMi 61215334.

Proteomic databases

MaxQBi Q96S59.
PaxDbi Q96S59.
PRIDEi Q96S59.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000011619 ; ENSP00000011619 ; ENSG00000010017 . [Q96S59-1 ]
ENST00000539980 ; ENSP00000438162 ; ENSG00000010017 . [Q96S59-2 ]
GeneIDi 10048.
KEGGi hsa:10048.
UCSCi uc003nba.3. human. [Q96S59-1 ]

Organism-specific databases

CTDi 10048.
GeneCardsi GC06M013621.
H-InvDB HIX0032741.
HGNCi HGNC:13727. RANBP9.
HPAi CAB033767.
HPA050007.
MIMi 603854. gene.
neXtProti NX_Q96S59.
PharmGKBi PA34215.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG316575.
GeneTreei ENSGT00530000063160.
HOGENOMi HOG000008133.
HOVERGENi HBG053444.
InParanoidi Q96S59.
OMAi YSNPWAS.
OrthoDBi EOG76MK7Z.
PhylomeDBi Q96S59.
TreeFami TF331658.

Enzyme and pathway databases

Reactomei REACT_22205. L1CAM interactions.
SignaLinki Q96S59.

Miscellaneous databases

ChiTaRSi RANBP9. human.
GeneWikii RANBP9.
GenomeRNAii 10048.
NextBioi 35467774.
PROi Q96S59.
SOURCEi Search...

Gene expression databases

Bgeei Q96S59.
CleanExi HS_RANBP9.
ExpressionAtlasi Q96S59. baseline and differential.
Genevestigatori Q96S59.

Family and domain databases

InterProi IPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR013144. CRA_dom.
IPR024964. CTLH/CRA.
IPR006595. CTLH_C.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR003877. SPRY_dom.
[Graphical view ]
Pfami PF10607. CLTH. 1 hit.
PF08513. LisH. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view ]
SMARTi SM00757. CRA. 1 hit.
SM00668. CTLH. 1 hit.
SM00667. LisH. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS50188. B302_SPRY. 1 hit.
PS50897. CTLH. 1 hit.
PS50896. LISH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex."
    Nishitani H., Hirose E., Uchimura Y., Nakamura M., Umeda M., Nishii K., Mori N., Nishimoto T.
    Gene 272:25-33(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  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] (ISOFORM 3).
    Tissue: Testis.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Lymph, Spinal ganglion and Testis.
  5. "When overexpressed, a novel centrosomal protein, RanBPM, causes ectopic microtubule nucleation similar to gamma-tubulin."
    Nakamura M., Masuda H., Horii J., Kuma K., Yokoyama N., Ohba T., Nishitani H., Miyata T., Tanaka M., Nishimoto T.
    J. Cell Biol. 143:1041-1052(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-729 (ISOFORM 1), INTERACTION WITH RAN.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-729 (ISOFORM 1), INTERACTION WITH HIPK2, SUBCELLULAR LOCATION.
  7. "RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor."
    Rao M.A., Cheng H., Quayle A.N., Nishitani H., Nelson C.C., Rennie P.S.
    J. Biol. Chem. 277:48020-48027(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 148-729 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH AR.
    Tissue: Prostate.
  8. "Structural and functional characterization of the USP11 deubiquitinating enzyme, which interacts with the RanGTP-associated protein RanBPM."
    Ideguchi H., Ueda A., Tanaka M., Yang J., Tsuji T., Ohno S., Hagiwara E., Aoki A., Ishigatsubo Y.
    Biochem. J. 367:87-95(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP11, UBIQUITINATION.
  9. "RanBPM interacts with psoriasin in vitro and their expression correlates with specific clinical features in vivo in breast cancer."
    Emberley E.D., Gietz R.D., Campbell J.D., Hayglass K.T., Murphy L.C., Watson P.H.
    BMC Cancer 2:28-28(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH S100A7.
  10. "Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM."
    Wang D., Li Z., Messing E.M., Wu G.
    J. Biol. Chem. 277:36216-36222(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RAS SIGNALING, INTERACTION WITH MET AND SOS, TISSUE SPECIFICITY.
  11. "Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy."
    Lutz W., Frank E.M., Craig T.A., Thompson R., Venters R.A., Kojetin D., Cavanagh J., Kumar R.
    Biochem. Biophys. Res. Commun. 303:1186-1192(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CALB1.
  12. "The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM."
    Mikolajczyk M., Shi J., Vaillancourt R.R., Sachs N.A., Nelson M.
    Biochem. Biophys. Res. Commun. 310:14-18(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC2L1, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  13. "A novel nuclear protein, Twa1, and Muskelin comprise a complex with RanBPM."
    Umeda M., Nishitani H., Nishimoto T.
    Gene 303:47-54(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MKLN1 AND GID8, IDENTIFICATION IN A COMPLEX WITH MKLN1 AND GID8.
  14. "Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M."
    Zou Y., Lim S., Lee K., Deng X., Friedman E.
    J. Biol. Chem. 278:49573-49581(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DYRK1A AND DYRK1B, IDENTIFICATION IN A COMPLEX WITH RAN; DYRK1B AND COPS5.
  15. "A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling."
    Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.
    Biochem. Biophys. Res. Commun. 313:320-326(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAN AND MET.
  16. "RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1."
    Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S., Fabbri M., Pardi R., Bianchi E.
    J. Biol. Chem. 279:13027-13034(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ITGB1 AND ITGB2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  17. "The C-terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre."
    Menon R.P., Gibson T.J., Pastore A.
    J. Mol. Biol. 343:43-53(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FMR1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  18. "Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells."
    Kramer S., Ozaki T., Miyazaki K., Kato C., Hanamoto T., Nakagawara A.
    Oncogene 24:938-944(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP73.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  20. "RanBP10 acts as a novel coactivator for the androgen receptor."
    Harada N., Yokoyama T., Yamaji R., Nakano Y., Inui H.
    Biochem. Biophys. Res. Commun. 368:121-125(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RANBP10, SUBCELLULAR LOCATION.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRANB9_HUMAN
AccessioniPrimary (citable) accession number: Q96S59
Secondary accession number(s): A0PJA2
, B2R8E1, O94764, Q6P3T7, Q7LBR2, Q7Z7F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 118 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3