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Q96QF0 (RAB3I_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Rab-3A-interacting protein

Short name=Rab3A-interacting protein
Alternative name(s):
Rabin-3
SSX2-interacting protein
Gene names
Name:RAB3IP
Synonyms:RABIN8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. Together with RAB11A, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Ref.2 Ref.10 Ref.11

Subunit structure

Interacts with the N-terminal region of SSX2. Interacts with the GDP-bound forms of RAB3A, RAB3D, RAB8A and RAB8B. Ref.1 Ref.2 UniProtKB Q62739

Subcellular location

Cytoplasm. Nucleus. Cytoplasmcytoskeleton. Cell projectionlamellipodium. Note: Predominantly cytoplasmic but a small proportion colocalizes with SSX2 in the nucleus. Activation of protein kinase C results in redistribution to the periphery of lamellipodia. In the cytoskeleton, localizes to cortical actin. Ref.1 Ref.2

Tissue specificity

Expressed in brain, kidney, heart, pancreas and placenta. Not detected in skeletal muscle or liver. Ref.1 Ref.2

Sequence similarities

Belongs to the SEC2 family.

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 Ref.1 (identifier: Q96QF0-1)

Also known as: alpha2;

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 1 Ref.1 (identifier: Q96QF0-2)

Also known as: alpha1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
Isoform 3 Ref.1 (identifier: Q96QF0-3)

Also known as: beta1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     394-411: KCALTGQSKSCKHRIKLG → SLLYVTFLHTFDTFSRDS
     412-476: Missing.
Isoform 4 Ref.1 (identifier: Q96QF0-4)

Also known as: beta2;

The sequence of this isoform differs from the canonical sequence as follows:
     394-411: KCALTGQSKSCKHRIKLG → SLLYVTFLHTFDTFSRDS
     412-476: Missing.
Isoform 5 Ref.1 (identifier: Q96QF0-5)

Also known as: gamma1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     313-320: ADLSLYNE → KMCSHWPE
     321-476: Missing.
Isoform 6 Ref.1 (identifier: Q96QF0-6)

Also known as: gamma2;

The sequence of this isoform differs from the canonical sequence as follows:
     313-320: ADLSLYNE → KMCSHWPE
     321-476: Missing.
Isoform 7 (identifier: Q96QF0-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     313-331: ADLSLYNEFRLWKDEPTMD → VTHQGLSPLTLLILVSSHH
     332-476: Missing.
Note: No experimental confirmation available.
Isoform 8 (identifier: Q96QF0-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-222: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Rab-3A-interacting protein
PRO_0000097144

Regions

Coiled coil165 – 26096 Potential

Amino acid modifications

Modified residue1631Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 222222Missing in isoform 8.
VSP_051756
Alternative sequence1 – 1616Missing in isoform 1, isoform 3, isoform 5 and isoform 7. Ref.1
VSP_051755
Alternative sequence313 – 33119ADLSL…EPTMD → VTHQGLSPLTLLILVSSHH in isoform 7.
VSP_051758
Alternative sequence313 – 3208ADLSLYNE → KMCSHWPE in isoform 5 and isoform 6. Ref.1
VSP_051757
Alternative sequence321 – 476156Missing in isoform 5 and isoform 6. Ref.1
VSP_051759
Alternative sequence332 – 476145Missing in isoform 7.
VSP_051760
Alternative sequence394 – 41118KCALT…RIKLG → SLLYVTFLHTFDTFSRDS in isoform 3 and isoform 4. Ref.1
VSP_051761
Alternative sequence412 – 47665Missing in isoform 3 and isoform 4. Ref.1
VSP_051762

Experimental info

Sequence conflict1641P → Q in AAH59358. Ref.5
Sequence conflict2861N → D in BAB15391. Ref.3
Sequence conflict3561Missing in BAB15391. Ref.3
Sequence conflict4641M → V in BAB15391. Ref.3

Secondary structure

..... 476
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (alpha2) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: DD77781823038F15

FASTA47653,021
        10         20         30         40         50         60 
MGLKKMKGLS YDEAFAMAND PLEGFHEVNL ASPTSPDLLG VYESGTQEQT TSPSVIYRPH 

        70         80         90        100        110        120 
PSALSSVPIQ ANALDVSELP TQPVYSSPRR LNCAEISSIS FHVTDPAPCS TSGVTAGLTK 

       130        140        150        160        170        180 
LTTRKDNYNA EREFLQGATI TEACDGSDDI FGLSTDSLSR LRSPSVLEVR EKGYERLKEE 

       190        200        210        220        230        240 
LAKAQRELKL KDEECERLSK VRDQLGQELE ELTASLFEEA HKMVREANIK QATAEKQLKE 

       250        260        270        280        290        300 
AQGKIDVLQA EVAALKTLVL SSSPTSPTQE PLPGGKTPFK KGHTRNKSTS SAMSGSHQDL 

       310        320        330        340        350        360 
SVIQPIVKDC KEADLSLYNE FRLWKDEPTM DRTCPFLDKI YQEDIFPCLT FSKSELASAV 

       370        380        390        400        410        420 
LEAVENNTLS IEPVGLQPIR FVKASAVECG GPKKCALTGQ SKSCKHRIKL GDSSNYYYIS 

       430        440        450        460        470 
PFCRYRITSV CNFFTYIRYI QQGLVKQQDV DQMFWEVMQL RKEMSLAKLG YFKEEL 

« Hide

Isoform 1 (alpha1) [UniParc].

Checksum: ED659E364B5C75FA
Show »

FASTA46051,250
Isoform 3 (beta1) [UniParc].

Checksum: 00E0F63E76FCEB09
Show »

FASTA39543,446
Isoform 4 (beta2) [UniParc].

Checksum: B7C472F90DDD661C
Show »

FASTA41145,217
Isoform 5 (gamma1) [UniParc].

Checksum: 6C579A473B5C0B52
Show »

FASTA30433,234
Isoform 6 (gamma2) [UniParc].

Checksum: 00F8D4526DB2AEFC
Show »

FASTA32035,005
Isoform 7 [UniParc].

Checksum: B4BCBD28A3C81394
Show »

FASTA31534,270
Isoform 8 [UniParc].

Checksum: 33D7F36AA55989C8
Show »

FASTA25428,642

References

« Hide 'large scale' references
[1]"The cancer-related protein SSX2 interacts with the human homologue of a Ras-like GTPase interactor, RAB3IP, and a novel nuclear protein, SSX2IP."
de Bruijn D.R.H., dos Santos N.R., Kater-Baats E., Thijssen J., van den Berk L., Stap J., Balemans M., Schepens M., Merkx G., van Kessel A.G.
Genes Chromosomes Cancer 34:285-298(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), INTERACTION WITH SSX2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Testis.
[2]"A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport."
Hattula K., Furuhjelm J., Arffman A., Peranen J.
Mol. Biol. Cell 13:3268-3280(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAB3A; RAB8A AND RAB8B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 8).
Tissue: Small intestine and Teratocarcinoma.
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [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] (ISOFORMS 7 AND 8).
Tissue: Brain and Colon.
[6]"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.
[7]"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-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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].
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors."
Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.
J. Cell Biol. 191:367-381(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS GUANYL-NUCLEOTIDE EXCHANGE FACTOR.
[11]"A molecular network for de novo generation of the apical surface and lumen."
Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J., Martin-Belmonte F., Mostov K.E.
Nat. Cell Biol. 12:1035-1045(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ312896 mRNA. Translation: CAC59835.1.
AJ312897 mRNA. Translation: CAC59836.1.
AJ312898 mRNA. Translation: CAC59837.1.
AJ312899 mRNA. Translation: CAC59838.1.
AJ312900 mRNA. Translation: CAC59839.1.
AJ312901 mRNA. Translation: CAC59840.1.
AK026201 mRNA. Translation: BAB15391.1.
AK027566 mRNA. Translation: BAB55202.1.
AK027671 mRNA. Translation: BAB55283.1.
AC025263 Genomic DNA. No translation available.
BC015548 mRNA. Translation: AAH15548.1.
BC059358 mRNA. Translation: AAH59358.1.
CCDSCCDS41811.1. [Q96QF0-4]
CCDS44942.1. [Q96QF0-8]
CCDS8993.1. [Q96QF0-1]
CCDS8995.1. [Q96QF0-2]
CCDS8996.1. [Q96QF0-3]
RefSeqNP_001019818.1. NM_001024647.3. [Q96QF0-8]
NP_001265331.1. NM_001278402.1. [Q96QF0-8]
NP_071901.2. NM_022456.4. [Q96QF0-2]
NP_783322.1. NM_175623.3. [Q96QF0-1]
NP_783323.1. NM_175624.3. [Q96QF0-3]
NP_783324.1. NM_175625.3. [Q96QF0-4]
UniGeneHs.258209.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LHXX-ray3.05C/D/E/F173-248[»]
4LHYX-ray3.10C/D/E/F173-248[»]
4LHZX-ray3.20C/D/E/F173-248[»]
ProteinModelPortalQ96QF0.
SMRQ96QF0. Positions 173-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125566. 2 interactions.
DIPDIP-41703N.
IntActQ96QF0. 30 interactions.
MINTMINT-237210.

PTM databases

PhosphoSiteQ96QF0.

Polymorphism databases

DMDM71152025.

Proteomic databases

MaxQBQ96QF0.
PaxDbQ96QF0.
PRIDEQ96QF0.

Protocols and materials databases

DNASU117177.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247833; ENSP00000247833; ENSG00000127328. [Q96QF0-2]
ENST00000325555; ENSP00000323349; ENSG00000127328. [Q96QF0-8]
ENST00000362025; ENSP00000355381; ENSG00000127328. [Q96QF0-4]
ENST00000378815; ENSP00000368092; ENSG00000127328. [Q96QF0-7]
ENST00000417413; ENSP00000436304; ENSG00000127328. [Q96QF0-5]
ENST00000483530; ENSP00000419216; ENSG00000127328. [Q96QF0-3]
ENST00000550536; ENSP00000447300; ENSG00000127328. [Q96QF0-1]
ENST00000551641; ENSP00000448773; ENSG00000127328. [Q96QF0-8]
ENST00000552199; ENSP00000448944; ENSG00000127328. [Q96QF0-6]
ENST00000553099; ENSP00000448027; ENSG00000127328. [Q96QF0-8]
GeneID117177.
KEGGhsa:117177.
UCSCuc001svm.3. human. [Q96QF0-1]
uc001svn.3. human. [Q96QF0-3]
uc001svq.3. human. [Q96QF0-4]
uc021rao.1. human. [Q96QF0-7]

Organism-specific databases

CTD117177.
GeneCardsGC12P070132.
HGNCHGNC:16508. RAB3IP.
HPAHPA039794.
MIM608686. gene.
neXtProtNX_Q96QF0.
PharmGKBPA34136.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG299882.
HOVERGENHBG057034.
InParanoidQ96QF0.
KOK16779.
OMAAPIQANA.
OrthoDBEOG7KSX8Q.
PhylomeDBQ96QF0.
TreeFamTF313748.

Gene expression databases

ArrayExpressQ96QF0.
BgeeQ96QF0.
GenevestigatorQ96QF0.

Family and domain databases

InterProIPR009449. Sec2p.
[Graphical view]
PfamPF06428. Sec2p. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAB3IP.
GenomeRNAi117177.
NextBio80133.
PROQ96QF0.
SOURCESearch...

Entry information

Entry nameRAB3I_HUMAN
AccessionPrimary (citable) accession number: Q96QF0
Secondary accession number(s): B7WPJ6 expand/collapse secondary AC list , Q6PCE4, Q96A24, Q96QE6, Q96QE7, Q96QE8, Q96QE9, Q96QF1, Q9H673
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 104 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 chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM