Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q86UR5 (RIMS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Regulating synaptic membrane exocytosis protein 1
Alternative name(s):
Rab-3-interacting molecule 1
Short name=RIM 1
Rab-3-interacting protein 2
Gene names
Name:RIMS1
Synonyms:KIAA0340, RAB3IP2, RIM1
ORF Names:Nbla00761
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1692 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Rab effector involved in exocytosis. May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short-term synaptic plasticity By similarity.

Subunit structure

Binds RAB3A, RAB3B and RAB3D that have been activated by GTP-binding. Interacts with RAB3C, RAB10, RAB26 AND RAB37. Binds UNC13A. Interacts with BZRAP1/RIMBP1 and RIMBP2. Interacts with PPFIA3 and PPFIA4. Interacts with ERC1 By similarity. Binds SNAP25, SYT1 and CACNA1B. Interaction with SYT1 is enhanced by calcium ions. Interaction with SNAP25 is weaker in the presence of calcium ions. Ref.7

Subcellular location

Cell membrane; Peripheral membrane protein By similarity. Cell junctionsynapse By similarity. Cell junctionsynapsepresynaptic cell membrane; Peripheral membrane protein By similarity.

Tissue specificity

Detected in brain and retina.

Post-translational modification

Phosphorylated by BRSK1 By similarity.

Involvement in disease

Cone-rod dystrophy 7 (CORD7) [MIM:603649]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.1

Sequence similarities

Contains 2 C2 domains.

Contains 1 FYVE-type zinc finger.

Contains 1 PDZ (DHR) domain.

Contains 1 RabBD (Rab-binding) domain.

Sequence caution

The sequence BAA20798.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI39600.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI42135.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processExocytosis
Neurotransmitter transport
Sensory transduction
Transport
Vision
   Cellular componentCell junction
Cell membrane
Membrane
Synapse
   Coding sequence diversityAlternative splicing
   DiseaseCone-rod dystrophy
Disease mutation
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion-dependent exocytosis

Traceable author statement Ref.7. Source: UniProtKB

calcium ion-dependent exocytosis of neurotransmitter

Inferred from electronic annotation. Source: Ensembl

glutamate secretion

Traceable author statement. Source: Reactome

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

membrane fusion

Non-traceable author statement Ref.7. Source: UniProtKB

neurotransmitter secretion

Traceable author statement. Source: Reactome

protein complex assembly

Inferred from direct assay Ref.7. Source: UniProtKB

regulated secretory pathway

Non-traceable author statement Ref.7. Source: UniProtKB

regulation of catalytic activity

Traceable author statement Ref.7. Source: GOC

regulation of long-term neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of membrane potential

Inferred from electronic annotation. Source: Ensembl

response to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

secretion

Non-traceable author statement Ref.7. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

synaptic vesicle exocytosis

Traceable author statement Ref.7. Source: UniProtKB

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

presynaptic membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

small GTPase regulator activity

Traceable author statement Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABL1P005192EBI-1043236,EBI-375543

Alternative products

This entry describes 13 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q86UR5-1)

Also known as: RIM1 alpha;

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: Q86UR5-2)

Also known as: RIM short form;

The sequence of this isoform differs from the canonical sequence as follows:
     1040-1692: Missing.
Note: May be due to intron retention.
Isoform 3 (identifier: Q86UR5-3)

Also known as: RIM long form; Rab3 interacting protein variant 2;

The sequence of this isoform differs from the canonical sequence as follows:
     1039-1102: Missing.
     1133-1245: Missing.
     1540-1573: Missing.
Isoform 4 (identifier: Q86UR5-4)

Also known as: Rab3 interacting protein variant 1;

The sequence of this isoform differs from the canonical sequence as follows:
     1065-1102: Missing.
     1133-1245: Missing.
Isoform 5 (identifier: Q86UR5-5)

Also known as: Rab3 interacting protein variant 3;

The sequence of this isoform differs from the canonical sequence as follows:
     924-924: Missing.
     1038-1244: Missing.
     1377-1385: Missing.
Isoform 6 (identifier: Q86UR5-6)

Also known as: Rab3 interacting protein variant 4;

The sequence of this isoform differs from the canonical sequence as follows:
     1039-1102: Missing.
     1161-1245: Missing.
     1284-1455: Missing.
Isoform 7 (identifier: Q86UR5-7)

Also known as: Rab3 interacting protein variant 5;

The sequence of this isoform differs from the canonical sequence as follows:
     924-924: Missing.
     1039-1102: Missing.
     1133-1245: Missing.
     1284-1455: Missing.
Isoform 8 (identifier: Q86UR5-8)

Also known as: Rab3 interacting protein variant 6;

The sequence of this isoform differs from the canonical sequence as follows:
     924-924: Missing.
     1018-1245: Missing.
     1284-1455: Missing.
Isoform 9 (identifier: Q86UR5-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MSSAVGPRGPRPPTVPPP → MFAGFLQFLLLHTLHSGT
     19-559: Missing.
     1039-1102: Missing.
     1133-1160: Missing.
     1185-1245: Missing.
     1284-1455: Missing.
Note: No experimental confirmation available.
Isoform 10 (identifier: Q86UR5-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-607: Missing.
     1039-1102: Missing.
     1133-1160: Missing.
     1185-1245: Missing.
     1284-1455: Missing.
Note: No experimental confirmation available.
Isoform 11 (identifier: Q86UR5-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1473: Missing.
Note: No experimental confirmation available.
Isoform 12 (identifier: Q86UR5-12)

The sequence of this isoform differs from the canonical sequence as follows:
     1-559: MSSAVGPRGP...ELESESVSEK → MCAPGIHVSSEGWEEVRSVDSEEGTIEARRAVA
     924-924: Missing.
     1039-1102: Missing.
     1133-1160: Missing.
     1185-1245: Missing.
Isoform 13 (identifier: Q86UR5-13)

The sequence of this isoform differs from the canonical sequence as follows:
     1-559: MSSAVGPRGP...ELESESVSEK → MCAPGIHVSSEGWEEVRSVDSEEGTIEARRAVA
     1039-1102: Missing.
     1133-1245: Missing.
     1284-1455: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16921692Regulating synaptic membrane exocytosis protein 1
PRO_0000190198

Regions

Domain22 – 182161RabBD
Domain605 – 69187PDZ
Domain744 – 850107C2 1
Domain1538 – 1640103C2 2
Zinc finger110 – 17061FYVE-type
Compositional bias1336 – 140267Ser-rich

Amino acid modifications

Modified residue16771Phosphoserine Ref.9
Modified residue16801Phosphoserine Ref.9
Modified residue16831Phosphoserine Ref.9
Modified residue16921Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 14731473Missing in isoform 11.
VSP_045485
Alternative sequence1 – 607607Missing in isoform 10.
VSP_045486
Alternative sequence1 – 559559MSSAV…SVSEK → MCAPGIHVSSEGWEEVRSVD SEEGTIEARRAVA in isoform 12 and isoform 13.
VSP_046796
Alternative sequence1 – 1818MSSAV…TVPPP → MFAGFLQFLLLHTLHSGT in isoform 9.
VSP_043177
Alternative sequence19 – 559541Missing in isoform 9.
VSP_043178
Alternative sequence9241Missing in isoform 5, isoform 7, isoform 8 and isoform 12.
VSP_008161
Alternative sequence1018 – 1245228Missing in isoform 8.
VSP_008162
Alternative sequence1038 – 1244207Missing in isoform 5.
VSP_008163
Alternative sequence1039 – 110264Missing in isoform 3, isoform 6, isoform 7, isoform 9, isoform 10, isoform 12 and isoform 13.
VSP_008164
Alternative sequence1040 – 1692653Missing in isoform 2.
VSP_008165
Alternative sequence1065 – 110238Missing in isoform 4.
VSP_008166
Alternative sequence1133 – 1245113Missing in isoform 3, isoform 4, isoform 7 and isoform 13.
VSP_008167
Alternative sequence1133 – 116028Missing in isoform 9, isoform 10 and isoform 12.
VSP_043179
Alternative sequence1161 – 124585Missing in isoform 6.
VSP_008168
Alternative sequence1185 – 124561Missing in isoform 9, isoform 10 and isoform 12.
VSP_043180
Alternative sequence1284 – 1455172Missing in isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 13.
VSP_008169
Alternative sequence1377 – 13859Missing in isoform 5.
VSP_008170
Alternative sequence1540 – 157334Missing in isoform 3.
VSP_008171
Natural variant8201R → H in CORD7. Ref.1
VAR_016804

Experimental info

Mutagenesis796 – 7972RR → AA: Abolishes interaction with SYT1 and CACNA1B. Ref.7
Mutagenesis1591 – 15922KK → AA: Abolishes interaction with SYT1 and CACNA1B. Ref.7
Sequence conflict1571V → Y in CAI16961. Ref.5
Sequence conflict484 – 49411Missing in BAB87121. Ref.2
Sequence conflict484 – 49411Missing in BAB87242. Ref.2
Sequence conflict484 – 49411Missing in BAA20798. Ref.3
Sequence conflict484 – 49411Missing in AAI51854. Ref.6
Sequence conflict484 – 49411Missing in AAI52436. Ref.6
Sequence conflict12721P → S in BAH11945. Ref.4
Sequence conflict16061Q → R in BAH11906. Ref.4
Sequence conflict16091V → A in BAH13358. Ref.4
Sequence conflict16621S → P in AK309185. Ref.4

Secondary structure

.................... 1692
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RIM1 alpha) [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 0A96642DC832C15E

FASTA1,692189,073
        10         20         30         40         50         60 
MSSAVGPRGP RPPTVPPPMQ ELPDLSHLTE EERNIIMAVM DRQKEEEEKE EAMLKCVVRD 

        70         80         90        100        110        120 
MAKPAACKTP RNAENQPHQP SPRLHQQFES YKEQVRKIGE EARRYQGEHK DDAPTCGICH 

       130        140        150        160        170        180 
KTKFADGCGH LCSYCRTKFC ARCGGRVSLR SNNEDKVVMW VCNLCRKQQE ILTKSGAWFF 

       190        200        210        220        230        240 
GSGPQQTSQD GTLSDTATGA GSEVPREKKA RLQERSRSQT PLSTAAASSQ DAAPPSAPPD 

       250        260        270        280        290        300 
RSKGAEPSQQ ALGPEQKQAS SRSRSEPPRE RKKTPGLSEQ NGKGALKSER KRVPKTSAQP 

       310        320        330        340        350        360 
VEGAVEERER KERRESRRLE KGRSQDYPDT PEKRDEGKAA DEEKQRKEED YQTRYRSDPN 

       370        380        390        400        410        420 
LARYPVKPPP EEQQMRMHAR VSRARHERRH SDVALPRTEA GAALPEGKAG KRAPAAARAS 

       430        440        450        460        470        480 
PPDSPRAYSA ERTAETRAPG AKQLTNHSPP APRHGPVPAE APELKAQEPL RKQSRLDPSS 

       490        500        510        520        530        540 
AVLMRKAKRE KVETMLRNDS LSSDQSESVR PSPPKPHRSK RGGKKRQMSV SSSEEEGVST 

       550        560        570        580        590        600 
PEYTSCEDVE LESESVSEKG DLDYYWLDPA TWHSRETSPI SSHPVTWQPS KEGDRLIGRV 

       610        620        630        640        650        660 
ILNKRTTMPK DSGALLGLKV VGGKMTDLGR LGAFITKVKK GSLADVVGHL RAGDEVLEWN 

       670        680        690        700        710        720 
GKPLPGATNE EVYNIILESK SEPQVEIIVS RPIGDIPRIP ESSHPPLESS SSSFESQKME 

       730        740        750        760        770        780 
RPSISVISPT SPGALKDAPQ VLPGQLSVKL WYDKVGHQLI VNVLQATDLP ARVDGRPRNP 

       790        800        810        820        830        840 
YVKMYFLPDR SDKSKRRTKT VKKILEPKWN QTFVYSHVHR RDFRERMLEI TVWDQPRVQE 

       850        860        870        880        890        900 
EESEFLGEIL IELETALLDD EPHWYKLQTH DESSLPLPQP SPFMPRRHIH GESSSKKLQR 

       910        920        930        940        950        960 
SQRISDSDIS DYEVDDGIGV VPPVGYRSSA RESKSTTLTV PEQQRTTHHR SRSVSPHRGN 

       970        980        990       1000       1010       1020 
DQGKPRSRLP NVPLQRSLDE IHPTRRSRSP TRHHDASRSP VDHRTRDVDS QYLSEQDSEL 

      1030       1040       1050       1060       1070       1080 
LMLPRAKRGR SAECLHTTRH LVRHYKTLPP KMPLLQSSSH WNIYSSILPA HTKTKSVTRQ 

      1090       1100       1110       1120       1130       1140 
DISLHHECFN STVLRFTDEI LVSELQPFLD RARSASTNCL RPDTSLHSPE RERGRWSPSL 

      1150       1160       1170       1180       1190       1200 
DRRRPPSPRI QIQHASPEND RHSRKSERSS IQKQTRKGTA SDAERVLPTC LSRRGHAAPR 

      1210       1220       1230       1240       1250       1260 
ATDQPVIRGK HPARSRSSEH SSIRTLCSMH HLVPGGSAPP SPLLTRMHRQ RSPTQSPPAD 

      1270       1280       1290       1300       1310       1320 
TSFSSRRGRQ LPQVPVRSGS IEQASLVVEE RTRQMKMKVH RFKQTTGSGS SQELDREQYS 

      1330       1340       1350       1360       1370       1380 
KYNIHKDQYR SCDNVSAKSS DSDVSDVSAI SRTSSASRLS STSFMSEQSE RPRGRISSFT 

      1390       1400       1410       1420       1430       1440 
PKMQGRRMGT SGRSIMKSTS VSGEMYTLEH NDGSQSDTAV GTVGAGGKKR RSSLSAKVVA 

      1450       1460       1470       1480       1490       1500 
IVSRRSRSTS QLSQTESGHK KLKSTIQRST ETGMAAEMRK MVRQPSREST DGSINSYSSE 

      1510       1520       1530       1540       1550       1560 
GNLIFPGVRL GADSQFSDFL DGLGPAQLVG RQTLATPAMG DIQIGMEDKK GQLEVEVIRA 

      1570       1580       1590       1600       1610       1620 
RSLTQKPGSK STPAPYVKVY LLENGACIAK KKTRIARKTL DPLYQQSLVF DESPQGKVLQ 

      1630       1640       1650       1660       1670       1680 
VIVWGDYGRM DHKCFMGVAQ ILLEELDLSS MVIGWYKLFP PSSLVDPTLT PLTRRASQSS 

      1690 
LESSTGPPCI RS 

« Hide

Isoform 2 (RIM short form) [UniParc].

Checksum: EF56FBC20E5A629E
Show »

FASTA1,039116,704
Isoform 3 (RIM long form) (Rab3 interacting protein variant 2) [UniParc].

Checksum: F34E4B8FAF1D35FD
Show »

FASTA1,481165,360
Isoform 4 (Rab3 interacting protein variant 1) [UniParc].

Checksum: 98A7006DC8206CB3
Show »

FASTA1,541172,224
Isoform 5 (Rab3 interacting protein variant 3) [UniParc].

Checksum: 8192B1AF38A1661B
Show »

FASTA1,475164,580
Isoform 6 (Rab3 interacting protein variant 4) [UniParc].

Checksum: 815C71ECFEF6D8C5
Show »

FASTA1,371153,500
Isoform 7 (Rab3 interacting protein variant 5) [UniParc].

Checksum: 87E88E425651F382
Show »

FASTA1,342150,109
Isoform 8 (Rab3 interacting protein variant 6) [UniParc].

Checksum: 8D52C8AD83A640AD
Show »

FASTA1,291144,361
Isoform 9 [UniParc].

Checksum: C20C62181371B83B
Show »

FASTA82692,731
Isoform 10 [UniParc].

Checksum: 1BC5B3BB0B105D6B
Show »

FASTA76085,152
Isoform 11 [UniParc].

Checksum: 9906E3592B6D9848
Show »

FASTA21924,013
Isoform 12 [UniParc].

Checksum: A6F0E2D8AFE8B426
Show »

FASTA1,012112,988
Isoform 13 [UniParc].

Checksum: 97107E7A7F961EC8
Show »

FASTA81791,530

References

« Hide 'large scale' references
[1]"Genomic organisation and alternative splicing of human RIM1, a gene implicated in autosomal dominant cone-rod dystrophy (CORD7)."
Johnson S., Halford S., Morris A.G., Patel R.J., Wilkie S.E., Hardcastle A.J., Moore A.T., Zhang K., Hunt D.M.
Genomics 81:304-314(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, VARIANT CORD7 HIS-820.
[2]"Identification of the alternative form of human RIM."
Aoyama M., Asai K., Shishikura T., Ohira M., Inuzuka H., Morohashi A., Kato T., Nakagawara A.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Neuroblastoma.
[3]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"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] (ISOFORMS 9; 10; 11; 12 AND 13).
Tissue: Brain, Small intestine and Thalamus.
[5]"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. expand/collapse author list , 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].
[6]"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 2).
[7]"Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin."
Coppola T., Magnin-Luethi S., Perret-Menoud V., Gattesco S., Schiavo G., Regazzi R.
J. Biol. Chem. 276:32756-32762(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 776-1692 (ISOFORMS 3; 4; 5; 6; 7 AND 8), MUTAGENESIS OF 796-LYS-LYS-797 AND 1591-ARG-ARG-1592, INTERACTION WITH SNAP25; SYT1 AND CACNA1B.
Tissue: Brain.
[8]"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.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1677; SER-1680; SER-1683 AND SER-1692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Solution structure of the PDZ domain of human KIAA0340 protein."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 585-694.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY190519 mRNA. Translation: AAO38848.1.
AB045726 mRNA. Translation: BAB87121.1.
AB051866 mRNA. Translation: BAB87242.1.
AB002338 mRNA. Translation: BAA20798.1. Different initiation.
AK296303 mRNA. Translation: BAH12309.1.
AK294868 mRNA. Translation: BAH11906.1.
AK295001 mRNA. Translation: BAH11945.1.
AK300853 mRNA. Translation: BAH13358.1.
AK309185 mRNA. No translation available.
AL160405 Genomic DNA. No translation available.
AL590011 expand/collapse EMBL AC list , AL034373, AL390056, AL445256 Genomic DNA. Translation: CAI16961.1.
AL034373 expand/collapse EMBL AC list , AL390056, AL445256, AL590011 Genomic DNA. Translation: CAI20558.1.
AL390056 expand/collapse EMBL AC list , AL034373, AL445256, AL590011 Genomic DNA. Translation: CAI21554.1.
AL445256 expand/collapse EMBL AC list , AL034373, AL390056, AL590011 Genomic DNA. Translation: CAI39598.1.
AL445256, AL035633 Genomic DNA. Translation: CAI39600.1. Sequence problems.
AL445256, AL035633 Genomic DNA. Translation: CAI39604.1.
AL035633, AL445256 Genomic DNA. Translation: CAI42135.1. Sequence problems.
AL035633, AL445256 Genomic DNA. Translation: CAI42139.1.
BC151853 mRNA. Translation: AAI51854.1.
BC152435 mRNA. Translation: AAI52436.1.
AF263305 mRNA. Translation: AAG23162.1.
AF263306 mRNA. Translation: AAG23163.1.
AF263307 mRNA. Translation: AAG23164.1.
AF263308 mRNA. Translation: AAG23165.1.
AF263309 mRNA. Translation: AAG23166.1.
AF263310 mRNA. Translation: AAG23167.1.
RefSeqNP_001161879.1. NM_001168407.1.
NP_001161880.1. NM_001168408.1.
NP_001161881.1. NM_001168409.1.
NP_001161882.1. NM_001168410.1.
NP_001161883.1. NM_001168411.1.
NP_055804.2. NM_014989.5.
UniGeneHs.485729.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSSNMR-A585-692[»]
ProteinModelPortalQ86UR5.
SMRQ86UR5. Positions 27-188, 583-691, 745-871, 1524-1671.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116646. 13 interactions.
IntActQ86UR5. 5 interactions.
MINTMINT-2808819.

PTM databases

PhosphoSiteQ86UR5.

Polymorphism databases

DMDM34395763.

Proteomic databases

PaxDbQ86UR5.
PRIDEQ86UR5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264839; ENSP00000264839; ENSG00000079841. [Q86UR5-4]
ENST00000370420; ENSP00000359448; ENSG00000079841.
ENST00000401910; ENSP00000385649; ENSG00000079841. [Q86UR5-12]
ENST00000414192; ENSP00000402273; ENSG00000079841. [Q86UR5-11]
ENST00000425662; ENSP00000411235; ENSG00000079841. [Q86UR5-10]
ENST00000491071; ENSP00000430101; ENSG00000079841. [Q86UR5-3]
ENST00000517827; ENSP00000428367; ENSG00000079841. [Q86UR5-9]
ENST00000517960; ENSP00000429959; ENSG00000079841. [Q86UR5-5]
ENST00000518273; ENSP00000430408; ENSG00000079841. [Q86UR5-6]
ENST00000520567; ENSP00000430502; ENSG00000079841. [Q86UR5-7]
ENST00000521978; ENSP00000428417; ENSG00000079841. [Q86UR5-1]
ENST00000522291; ENSP00000430932; ENSG00000079841. [Q86UR5-8]
ENST00000523963; ENSP00000428328; ENSG00000079841. [Q86UR5-13]
GeneID22999.
KEGGhsa:22999.
UCSCuc003pga.4. human. [Q86UR5-1]
uc003pgb.4. human. [Q86UR5-2]
uc003pgc.3. human. [Q86UR5-3]
uc010kas.1. human. [Q86UR5-9]

Organism-specific databases

CTD22999.
GeneCardsGC06P072653.
HGNCHGNC:17282. RIMS1.
HPAHPA039297.
MIM603649. phenotype.
606629. gene.
neXtProtNX_Q86UR5.
Orphanet1872. Cone rod dystrophy.
PharmGKBPA38220.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG286957.
HOGENOMHOG000082403.
HOVERGENHBG058147.
InParanoidQ86UR5.
KOK15291.
OMAERKKTPG.
OrthoDBEOG7BGHJV.
PhylomeDBQ86UR5.
TreeFamTF321703.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ86UR5.
BgeeQ86UR5.
GenevestigatorQ86UR5.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
2.60.40.150. 2 hits.
3.30.40.10. 1 hit.
InterProIPR000008. C2_dom.
IPR001478. PDZ.
IPR017455. Znf_FYVE-rel.
IPR010911. Znf_FYVE-typ.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00168. C2. 2 hits.
PF02318. FYVE_2. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTSM00239. C2. 2 hits.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 2 hits.
SSF50156. SSF50156. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEPS50004. C2. 2 hits.
PS50106. PDZ. 1 hit.
PS50916. RABBD. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRIMS1. human.
EvolutionaryTraceQ86UR5.
GeneWikiRIMS1.
GenomeRNAi22999.
NextBio43896.
PROQ86UR5.
SOURCESearch...

Entry information

Entry nameRIMS1_HUMAN
AccessionPrimary (citable) accession number: Q86UR5
Secondary accession number(s): A7MBN6 expand/collapse secondary AC list , B7Z2M0, B7Z2Q9, B7Z3S3, B7Z6S2, E7EX08, E9PCB7, E9PCZ1, E9PF48, E9PHF5, E9PHR1, O15048, Q5JY21, Q5JY25, Q5SZK1, Q8TDY9, Q8TDZ5, Q9HBA1, Q9HBA2, Q9HBA3, Q9HBA4, Q9HBA5, Q9HBA6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 126 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM