Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8IWJ2 (GCC2_HUMAN)

Last modified January 19, 2010. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    GRIP and coiled-coil domain-containing protein 2
Alternative name(s):
    Golgi coiled-coil protein GCC185
    Ran-binding protein 2-like 4
      Short name=RanBP2L4
    CTCL tumor antigen se1-1
    CLL-associated antigen KW-11
    Renal carcinoma antigen NY-REN-53
Gene names
Name: GCC2
Synonyms: KIAA0336, RANBP2L4
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1583 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Probably involved in maintaining Golgi structure By similarity.

Subunit structure

Homodimer. Interacts (via its GRIP domain) to RAP6A and RAP9. Ref.12

Subcellular location

Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein Ref.12 Ref.8.

Tissue specificity

Ubiquitous. Ref.6

Domain

Extended rod-like protein with coiled-coil domains.

Sequence similarities

Contains 1 GRIP domain.

Sequence caution

The sequence AAH37774.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Cellular componentCytoplasm
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Cellular componentGolgi apparatus Ref.12

Inferred from direct assay. Source: UniProtKB

extrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionidentical protein binding Ref.12

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-1645335,EBI-1645335
RAB6AP203401EBI-1645335,EBI-1052826

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IWJ2-1)

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: Q8IWJ2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEDLVQDGVA...LSLKKENIKM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15831583GRIP and coiled-coil domain-containing protein 2
PRO_0000190074

Regions

Domain1508 – 155851GRIP
Coiled coil9 – 15171509 Potential
Compositional bias138 – 947810Glu-rich

Amino acid modifications

Modified residue1861Phosphoserine Ref.10
Modified residue13821Phosphoserine Ref.9 Ref.11
Modified residue14411Phosphoserine Ref.11
Modified residue15481Phosphoserine Ref.10 Ref.11

Natural variations

Alternative sequence11M → MEDLVQDGVASPATPGTGKS KLETLPKEDLIKFAKKQMML IQKAKSRCTELEKEIEELRS KPVTEGTGDIIKALTERLDA LLLEKAETEQQCLSLKKENI KM in isoform 2.
VSP_007733
Natural variant10331Q → E: dbSNP rs2718698. Ref.1 Ref.3 Ref.4
VAR_046635
Natural variant11971R → G: dbSNP rs1061202.
VAR_016101

Experimental info

Mutagenesis14871I → A: Slightly decreases RAB6 binding affinity. Decreases RAB9 binding affinity by 2-fold. Strongly decreases RAB6 or RAB9 binding affinity and abolishes Golgi localization; when associated with Ala-1494. Ref.12
Mutagenesis14941L → A: Decreases RAB6 binding affinity by 2-fold. Strongly decreases RAB9 binding affinity. Strongly decreases RAB6 or RAB9 binding affinity and abolishes Golgi localization; when associated with Ala-1487. Ref.12
Mutagenesis15171Y → A: No effect on RAB6A or RAB9 binding affinity. Ref.12
Sequence conflict593 – 5997NNKLSSE → TINSVQK in AAG34902. Ref.6
Sequence conflict836 – 8394SVKN → YCKK in AAG34902. Ref.6

Secondary structure

... 1583
Helix Strand Turn

Details...

Sequences

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

Last modified October 2, 2007. Version 3.
Checksum: 65D503FAE5969494

FASTA1,583184,657
        10         20         30         40         50         60 
MKQEVEDSVT KMGDAHKELE QSHINYVKEI ENLKNELMAV RSKYSEDKAN LQKQLEEAMN 

        70         80         90        100        110        120 
TQLELSEQLK FQNNSEDNVK KLQEEIEKIR PGFEEQILYL QKQLDATTDE KKETVTQLQN 

       130        140        150        160        170        180 
IIEANSQHYQ KNINSLQEEL LQLKAIHQEE VKELMCQIEA SAKEHEAEIN KLNELKENLV 

       190        200        210        220        230        240 
KQCEASEKNI QKKYECELEN LRKATSNANQ DNQICSILLQ ENTFVEQVVN EKVKHLEDTL 

       250        260        270        280        290        300 
KELESQHSIL KDEVTYMNNL KLKLEMDAQH IKDEFFHERE DLEFKINELL LAKEEQGCVI 

       310        320        330        340        350        360 
EKLKSELAGL NKQFCYTVEQ HNREVQSLKE QHQKEISELN ETFLSDSEKE KLTLMFEIQG 

       370        380        390        400        410        420 
LKEQCENLQQ EKQEAILNYE SLREIMEILQ TELGESAGKI SQEFESMKQQ QASDVHELQQ 

       430        440        450        460        470        480 
KLRTAFTEKD ALLETVNRLQ GENEKLLSQQ ELVPELENTI KNLQEKNGVY LLSLSQRDTM 

       490        500        510        520        530        540 
LKELEGKINS LTEEKDDFIN KLKNSHEEMD NFHKKCEREE RLILELGKKV EQTIQYNSEL 

       550        560        570        580        590        600 
EQKVNELTGG LEETLKEKDQ NDQKLEKLMV QMKVLSEDKE VLSAEVKSLY EENNKLSSEK 

       610        620        630        640        650        660 
KQLSRDLEVF LSQKEDVILK EHITQLEKKL QLMVEEQDNL NKLLENEQVQ KLFVKTQLYG 

       670        680        690        700        710        720 
FLKEMGSEVS EDSEEKDVVN VLQAVGESLA KINEEKCNLA FQRDEKVLEL EKEIKCLQEE 

       730        740        750        760        770        780 
SVVQCEELKS LLRDYEQEKV LLRKELEEIQ SEKEALQSDL LEMKNANEKT RLENQNLLIQ 

       790        800        810        820        830        840 
VEEVSQTCSK SEIHNEKEKC FIKEHENLKP LLEQKELRDR RAELILLKDS LAKSPSVKND 

       850        860        870        880        890        900 
PLSSVKELEE KIENLEKECK EKEEKINKIK LVAVKAKKEL DSSRKETQTV KEELESLRSE 

       910        920        930        940        950        960 
KDQLSASMRD LIQGAESYKN LLLEYEKQSE QLDVEKERAN NFEHRIEDLT RQLRNSTLQC 

       970        980        990       1000       1010       1020 
ETINSDNEDL LARIETLQSN AKLLEVQILE VQRAKAMVDK ELEAEKLQKE QKIKEHATTV 

      1030       1040       1050       1060       1070       1080 
NELEELQVQL QKQKKQLQKT MQELELVKKD AQQTTLMNME IADYERLMKE LNQKLTNKNN 

      1090       1100       1110       1120       1130       1140 
KIEDLEQEIK IQKQKQETLQ EEITSLQSSV QQYEEKNTKI KQLLVKTKKE LADSKQAETD 

      1150       1160       1170       1180       1190       1200 
HLILQASLKG ELEASQQQVE VYKIQLAEIT SEKHKIHEHL KTSAEQHQRT LSAYQQRVTA 

      1210       1220       1230       1240       1250       1260 
LQEECRAAKA EQATVTSEFE SYKVRVHNVL KQQKNKSMSQ AETEGAKQER EHLEMLIDQL 

      1270       1280       1290       1300       1310       1320 
KIKLQDSQNN LQINVSELQT LQSEHDTLLE RHNKMLQETV SKEAELREKL CSIQSENMMM 

      1330       1340       1350       1360       1370       1380 
KSEHTQTVSQ LTSQNEVLRN SFRDQVRHLQ EEHRKTVETL QQQLSKMEAQ LFQLKNEPTT 

      1390       1400       1410       1420       1430       1440 
RSPVSSQQSL KNLRERRNTD LPLLDMHTVT REEGEGMETT DTESVSSAST YTQSLEQLLN 

      1450       1460       1470       1480       1490       1500 
SPETKLEPPL WHAEFTKEEL VQKLSSTTKS ADHLNGLLRE TEATNAILME QIKLLKSEIR 

      1510       1520       1530       1540       1550       1560 
RLERNQEREK SAANLEYLKN VLLQFIFLKP GSERERLLPV INTMLQLSPE EKGKLAAVAQ 

      1570       1580 
GEEENASRSS GWASYLHSWS GLR 

« Hide

Isoform 2.

Checksum: 83B6135D9EB9440D
Show »

FASTA1,684195,910

References

« Hide 'large scale' references
[1]"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: 9205841] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-1033.
Tissue: Brain.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-1033.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-1033.
Tissue: Brain.
[5]"Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX."
Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G.
Blood 100:2123-2131(2002) [PubMed: 12200376] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-347 (ISOFORM 2).
[6]"Serological detection of cutaneous T-cell lymphoma-associated antigens."
Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.
Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001) [PubMed: 11149944] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-839, TISSUE SPECIFICITY.
Tissue: Testis.
[7]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed: 10508479] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[8]"GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network."
Luke M.R., Kjer-Nielsen L., Brown D.L., Stow J.L., Gleeson P.A.
J. Biol. Chem. 278:4216-4226(2003) [PubMed: 12446665] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1382, MASS SPECTROMETRY.
Tissue: Epithelium.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-1548, MASS SPECTROMETRY.
[11]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1382; SER-1441 AND SER-1548, MASS SPECTROMETRY.
[12]"Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185."
Burguete A.S., Fenn T.D., Brunger A.T., Pfeffer S.R.
Cell 132:286-298(2008) [PubMed: 18243103] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1446-1511, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RAB6A, MUTAGENESIS OF ILE-1487; LEU-1494 AND TYR-1517.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002334 mRNA. Translation: BAA20794.2. Different initiation.
AC012487 Genomic DNA. Translation: AAX88838.1.
AC068941 Genomic DNA. No translation available.
CH471182 Genomic DNA. Translation: EAW53882.1.
BC037774 mRNA. Translation: AAH37774.1. Sequence problems.
BC146789 mRNA. Translation: AAI46790.1.
AF432211 mRNA. Translation: AAL99918.1. Different initiation.
AF273042 mRNA. Translation: AAG34902.1. Different initiation.
IPIIPI00005631.
IPI00333197.
RefSeqNP_852118.1.
UniGeneHs.436505
Hs.469630

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BBPX-ray3.00D/E/F1446-1511[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ8IWJ2. 6 interactions.
STRINGQ8IWJ2.

PTM databases

PhosphoSiteQ8IWJ2.

Proteomic databases

PRIDEQ8IWJ2.

Genome annotation databases

EnsemblENST00000309863; ENSP00000307939; ENSG00000135968; Homo sapiens. [Genome view]
ENST00000409325; ENSP00000386860; ENSG00000135968; Homo sapiens. [Genome view]
GeneID9648.
KEGGhsa:9648.
UCSCuc002tec.1. human.

Organism-specific databases

CTD9648.
GeneCardsGC02P108524.
H-InvDBHIX0022004.
HIX0023314.
HGNCHGNC:23218. GCC2.
PharmGKBPA134876902.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG278534.
HOVERGENQ8IWJ2.
InParanoidQ8IWJ2.
OMACQIEASA.
OrthoDBEOG9T7BPP.
PhylomeDBQ8IWJ2.

Gene expression databases

ArrayExpressQ8IWJ2.
BgeeQ8IWJ2.
CleanExHS_GCC2.
GenevestigatorQ8IWJ2.
GermOnlineENSG00000135968. Homo sapiens.

Family and domain databases

InterProIPR000237. GRIP.
[Graphical view]
PfamPF01465. GRIP. 1 hit.
[Graphical view]
SMARTSM00755. Grip. 1 hit.
[Graphical view]
PROSITEPS50913. GRIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio36215.

Entry information

Entry nameGCC2_HUMAN
AccessionPrimary (citable) accession number: Q8IWJ2
Secondary accession number(s): A6H8X8 expand/collapse secondary AC list , O15045, Q4ZG46, Q8TDH3, Q9H2G8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: October 2, 2007
Last modified: January 19, 2010
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents