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Protein

GRIP and coiled-coil domain-containing protein 2

Gene

GCC2

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

Functioni

Golgin which probably tethers transport vesicles to the trans-Golgi network (TGN) and regulates vesicular transport between the endosomes and the Golgi. As a RAB9A effector it is involved in recycling of the mannose 6-phosphate receptor from the late endosomes to the TGN. May also play a role in transport between the recycling endosomes and the Golgi. Required for maintenance of the Golgi structure, it is involved in the biogenesis of noncentrosomal, Golgi-associated microtubules through recruitment of CLASP1 and CLASP2.3 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • Golgi ribbon formation Source: UniProtKB
  • late endosome to Golgi transport Source: UniProtKB
  • microtubule anchoring Source: UniProtKB
  • microtubule organizing center organization Source: UniProtKB
  • protein localization to Golgi apparatus Source: UniProtKB
  • protein targeting to Golgi Source: InterPro
  • protein targeting to lysosome Source: UniProtKB
  • recycling endosome to Golgi transport Source: UniProtKB
  • regulation of protein exit from endoplasmic reticulum Source: UniProtKB
  • retrograde transport, endosome to Golgi Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
GRIP and coiled-coil domain-containing protein 2
Alternative name(s):
185 kDa Golgi coiled-coil protein
Short name:
GCC185
CLL-associated antigen KW-11
CTCL tumor antigen se1-1
Ran-binding protein 2-like 4
Short name:
RanBP2L4
Renal carcinoma antigen NY-REN-53
Gene namesi
Name:GCC2
Synonyms:KIAA0336, RANBP2L4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:23218. GCC2.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: UniProtKB
  • membrane Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1588 – 15881I → A: Slightly decreases RAB6A binding affinity. Decreases RAB9A binding affinity by 2-fold. Strongly decreases RAB6A or RAB9A binding affinity and abolishes Golgi localization; when associated with A-1595. 1 Publication
Mutagenesisi1595 – 15951L → A: Decreases RAB6A binding affinity by 2-fold. Strongly decreases RAB9A binding affinity. Strongly decreases RAB6A or RAB9A binding affinity and abolishes Golgi localization; when associated with A-1588. 1 Publication
Mutagenesisi1618 – 16181Y → A: No effect on interaction with RAB6A and RAB9A. 2 Publications

Organism-specific databases

PharmGKBiPA134876902.

Polymorphism and mutation databases

BioMutaiGCC2.
DMDMi313104307.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16841684GRIP and coiled-coil domain-containing protein 2PRO_0000190074Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei14 – 141PhosphothreonineCombined sources
Modified residuei236 – 2361PhosphoserineCombined sources
Modified residuei1483 – 14831PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8IWJ2.
MaxQBiQ8IWJ2.
PaxDbiQ8IWJ2.
PRIDEiQ8IWJ2.

PTM databases

iPTMnetiQ8IWJ2.
PhosphoSiteiQ8IWJ2.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8IWJ2.
CleanExiHS_GCC2.
ExpressionAtlasiQ8IWJ2. baseline and differential.
GenevisibleiQ8IWJ2. HS.

Organism-specific databases

HPAiHPA035849.
HPA035850.

Interactioni

Subunit structurei

Homodimer. Interacts (via GRIP domain) with RAB6A (preferentially in its GTP-bound form). May interact (RAB6A-dependent) with ARL1; according to PubMed:19703403, RAB6A and ARL1 are not involved in GCC2 Golgi localization as proposed by PubMed:18243103. Interacts (probably via GRIP domain) with RAB9A (preferentially in its GTP-bound form). Interacts with CLASP1 and CLASP2; recruits both proteins to membranes of the TGN. Interacts with STX16.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1645320,EBI-1645320
RAB6AP203404EBI-1645320,EBI-1052826

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi115006. 28 interactions.
IntActiQ8IWJ2. 16 interactions.
STRINGi9606.ENSP00000307939.

Structurei

Secondary structure

1
1684
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1574 – 160532Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BBPX-ray3.00D/E/F1547-1612[»]
ProteinModelPortaliQ8IWJ2.
SMRiQ8IWJ2. Positions 1570-1607.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IWJ2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1609 – 165951GRIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1574 – 1684111Mediates interaction with RAB9AAdd
BLAST
Regioni1574 – 161340Mediates interaction with RAB6AAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili110 – 16181509Sequence analysisAdd
BLAST

Domaini

Extended rod-like protein with coiled-coil domains.

Sequence similaritiesi

Contains 1 GRIP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IUCE. Eukaryota.
ENOG410Y42S. LUCA.
GeneTreeiENSGT00730000111134.
HOGENOMiHOG000060191.
HOVERGENiHBG045522.
InParanoidiQ8IWJ2.
OMAiNANQDNQ.
PhylomeDBiQ8IWJ2.
TreeFamiTF332907.

Family and domain databases

Gene3Di1.10.220.60. 1 hit.
InterProiIPR032023. GCC2_Rab_bind.
IPR000237. GRIP.
[Graphical view]
PfamiPF01465. GRIP. 1 hit.
PF16704. Rab_bind. 1 hit.
[Graphical view]
SMARTiSM00755. Grip. 1 hit.
[Graphical view]
PROSITEiPS50913. GRIP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IWJ2-1) [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
MEDLVQDGVA SPATPGTGKS KLETLPKEDL IKFAKKQMML IQKAKSRCTE
60 70 80 90 100
LEKEIEELRS KPVTEGTGDI IKALTERLDA LLLEKAETEQ QCLSLKKENI
110 120 130 140 150
KMKQEVEDSV TKMGDAHKEL EQSHINYVKE IENLKNELMA VRSKYSEDKA
160 170 180 190 200
NLQKQLEEAM NTQLELSEQL KFQNNSEDNV KKLQEEIEKI RPGFEEQILY
210 220 230 240 250
LQKQLDATTD EKKETVTQLQ NIIEANSQHY QKNINSLQEE LLQLKAIHQE
260 270 280 290 300
EVKELMCQIE ASAKEHEAEI NKLNELKENL VKQCEASEKN IQKKYECELE
310 320 330 340 350
NLRKATSNAN QDNQICSILL QENTFVEQVV NEKVKHLEDT LKELESQHSI
360 370 380 390 400
LKDEVTYMNN LKLKLEMDAQ HIKDEFFHER EDLEFKINEL LLAKEEQGCV
410 420 430 440 450
IEKLKSELAG LNKQFCYTVE QHNREVQSLK EQHQKEISEL NETFLSDSEK
460 470 480 490 500
EKLTLMFEIQ GLKEQCENLQ QEKQEAILNY ESLREIMEIL QTELGESAGK
510 520 530 540 550
ISQEFESMKQ QQASDVHELQ QKLRTAFTEK DALLETVNRL QGENEKLLSQ
560 570 580 590 600
QELVPELENT IKNLQEKNGV YLLSLSQRDT MLKELEGKIN SLTEEKDDFI
610 620 630 640 650
NKLKNSHEEM DNFHKKCERE ERLILELGKK VEQTIQYNSE LEQKVNELTG
660 670 680 690 700
GLEETLKEKD QNDQKLEKLM VQMKVLSEDK EVLSAEVKSL YEENNKLSSE
710 720 730 740 750
KKQLSRDLEV FLSQKEDVIL KEHITQLEKK LQLMVEEQDN LNKLLENEQV
760 770 780 790 800
QKLFVKTQLY GFLKEMGSEV SEDSEEKDVV NVLQAVGESL AKINEEKCNL
810 820 830 840 850
AFQRDEKVLE LEKEIKCLQE ESVVQCEELK SLLRDYEQEK VLLRKELEEI
860 870 880 890 900
QSEKEALQSD LLEMKNANEK TRLENQNLLI QVEEVSQTCS KSEIHNEKEK
910 920 930 940 950
CFIKEHENLK PLLEQKELRD RRAELILLKD SLAKSPSVKN DPLSSVKELE
960 970 980 990 1000
EKIENLEKEC KEKEEKINKI KLVAVKAKKE LDSSRKETQT VKEELESLRS
1010 1020 1030 1040 1050
EKDQLSASMR DLIQGAESYK NLLLEYEKQS EQLDVEKERA NNFEHRIEDL
1060 1070 1080 1090 1100
TRQLRNSTLQ CETINSDNED LLARIETLQS NAKLLEVQIL EVQRAKAMVD
1110 1120 1130 1140 1150
KELEAEKLQK EQKIKEHATT VNELEELQVQ LQKQKKQLQK TMQELELVKK
1160 1170 1180 1190 1200
DAQQTTLMNM EIADYERLMK ELNQKLTNKN NKIEDLEQEI KIQKQKQETL
1210 1220 1230 1240 1250
QEEITSLQSS VQQYEEKNTK IKQLLVKTKK ELADSKQAET DHLILQASLK
1260 1270 1280 1290 1300
GELEASQQQV EVYKIQLAEI TSEKHKIHEH LKTSAEQHQR TLSAYQQRVT
1310 1320 1330 1340 1350
ALQEECRAAK AEQATVTSEF ESYKVRVHNV LKQQKNKSMS QAETEGAKQE
1360 1370 1380 1390 1400
REHLEMLIDQ LKIKLQDSQN NLQINVSELQ TLQSEHDTLL ERHNKMLQET
1410 1420 1430 1440 1450
VSKEAELREK LCSIQSENMM MKSEHTQTVS QLTSQNEVLR NSFRDQVRHL
1460 1470 1480 1490 1500
QEEHRKTVET LQQQLSKMEA QLFQLKNEPT TRSPVSSQQS LKNLRERRNT
1510 1520 1530 1540 1550
DLPLLDMHTV TREEGEGMET TDTESVSSAS TYTQSLEQLL NSPETKLEPP
1560 1570 1580 1590 1600
LWHAEFTKEE LVQKLSSTTK SADHLNGLLR ETEATNAILM EQIKLLKSEI
1610 1620 1630 1640 1650
RRLERNQERE KSAANLEYLK NVLLQFIFLK PGSERERLLP VINTMLQLSP
1660 1670 1680
EEKGKLAAVA QGEEENASRS SGWASYLHSW SGLR
Length:1,684
Mass (Da):195,910
Last modified:November 30, 2010 - v4
Checksum:i83B6135D9EB9440D
GO
Isoform 2 (identifier: Q8IWJ2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     22-45: LETLPKEDLIKFAKKQMMLIQKAK → NWRKKLKNSDQNLLLKELVILLRH
     46-1684: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:45
Mass (Da):5,043
Checksum:i01BB22944C997E56
GO

Sequence cautioni

The sequence AAG34902.1 differs from that shown. Reason: Frameshift at positions 694, 700, 937 and 940. Curated
The sequence AAH37774.1 differs from that shown.Wrong choice of CDS.Curated
The sequence AAI46790.1 differs from that shown.Wrong choice of CDS.Curated
The sequence AAL99918.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAX88838.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAA20794.2 differs from that shown.Wrong choice of CDS.Curated
The sequence EAW53882.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1134 – 11341Q → E.1 Publication
Corresponds to variant rs2718698 [ dbSNP | Ensembl ].
VAR_046635
Natural varianti1298 – 12981R → G.
Corresponds to variant rs1061202 [ dbSNP | Ensembl ].
VAR_016101

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei22 – 4524LETLP…IQKAK → NWRKKLKNSDQNLLLKELVI LLRH in isoform 2. 2 PublicationsVSP_040106Add
BLAST
Alternative sequencei46 – 16841639Missing in isoform 2. 2 PublicationsVSP_040107Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002334 mRNA. Translation: BAA20794.2. Sequence problems.
AC012487 Genomic DNA. Translation: AAX88838.1. Sequence problems.
AC068941 Genomic DNA. No translation available.
CH471182 Genomic DNA. Translation: EAW53882.1. Sequence problems.
BC037774 mRNA. Translation: AAH37774.1. Sequence problems.
BC146789 mRNA. Translation: AAI46790.1. Sequence problems.
AF432211 mRNA. Translation: AAL99918.1. Different initiation.
AF273042 mRNA. Translation: AAG34902.1. Frameshift.
CCDSiCCDS33268.1. [Q8IWJ2-1]
RefSeqiNP_852118.1. NM_181453.3.
XP_006712934.1. XM_006712871.1.
UniGeneiHs.436505.
Hs.469630.

Genome annotation databases

EnsembliENST00000309863; ENSP00000307939; ENSG00000135968. [Q8IWJ2-1]
ENST00000482325; ENSP00000419969; ENSG00000135968. [Q8IWJ2-3]
GeneIDi9648.
KEGGihsa:9648.
UCSCiuc002tec.4. human. [Q8IWJ2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002334 mRNA. Translation: BAA20794.2. Sequence problems.
AC012487 Genomic DNA. Translation: AAX88838.1. Sequence problems.
AC068941 Genomic DNA. No translation available.
CH471182 Genomic DNA. Translation: EAW53882.1. Sequence problems.
BC037774 mRNA. Translation: AAH37774.1. Sequence problems.
BC146789 mRNA. Translation: AAI46790.1. Sequence problems.
AF432211 mRNA. Translation: AAL99918.1. Different initiation.
AF273042 mRNA. Translation: AAG34902.1. Frameshift.
CCDSiCCDS33268.1. [Q8IWJ2-1]
RefSeqiNP_852118.1. NM_181453.3.
XP_006712934.1. XM_006712871.1.
UniGeneiHs.436505.
Hs.469630.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BBPX-ray3.00D/E/F1547-1612[»]
ProteinModelPortaliQ8IWJ2.
SMRiQ8IWJ2. Positions 1570-1607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115006. 28 interactions.
IntActiQ8IWJ2. 16 interactions.
STRINGi9606.ENSP00000307939.

PTM databases

iPTMnetiQ8IWJ2.
PhosphoSiteiQ8IWJ2.

Polymorphism and mutation databases

BioMutaiGCC2.
DMDMi313104307.

Proteomic databases

EPDiQ8IWJ2.
MaxQBiQ8IWJ2.
PaxDbiQ8IWJ2.
PRIDEiQ8IWJ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309863; ENSP00000307939; ENSG00000135968. [Q8IWJ2-1]
ENST00000482325; ENSP00000419969; ENSG00000135968. [Q8IWJ2-3]
GeneIDi9648.
KEGGihsa:9648.
UCSCiuc002tec.4. human. [Q8IWJ2-1]

Organism-specific databases

CTDi9648.
GeneCardsiGCC2.
H-InvDBHIX0023314.
HGNCiHGNC:23218. GCC2.
HPAiHPA035849.
HPA035850.
MIMi612711. gene.
neXtProtiNX_Q8IWJ2.
PharmGKBiPA134876902.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IUCE. Eukaryota.
ENOG410Y42S. LUCA.
GeneTreeiENSGT00730000111134.
HOGENOMiHOG000060191.
HOVERGENiHBG045522.
InParanoidiQ8IWJ2.
OMAiNANQDNQ.
PhylomeDBiQ8IWJ2.
TreeFamiTF332907.

Miscellaneous databases

EvolutionaryTraceiQ8IWJ2.
GeneWikiiGCC2.
GenomeRNAii9648.
NextBioi36215.
PROiQ8IWJ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IWJ2.
CleanExiHS_GCC2.
ExpressionAtlasiQ8IWJ2. baseline and differential.
GenevisibleiQ8IWJ2. HS.

Family and domain databases

Gene3Di1.10.220.60. 1 hit.
InterProiIPR032023. GCC2_Rab_bind.
IPR000237. GRIP.
[Graphical view]
PfamiPF01465. GRIP. 1 hit.
PF16704. Rab_bind. 1 hit.
[Graphical view]
SMARTiSM00755. Grip. 1 hit.
[Graphical view]
PROSITEiPS50913. GRIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-1134.
  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] (ISOFORM 2).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-448 (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 161-946 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Testis.
  7. 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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "A functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling."
    Reddy J.V., Burguete A.S., Sridevi K., Ganley I.G., Nottingham R.M., Pfeffer S.R.
    Mol. Biol. Cell 17:4353-4363(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB9A, MUTAGENESIS OF TYR-1618.
  10. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: FUNCTION, INTERACTION WITH CLASP1 AND CLASP2.
  12. "The trans-Golgi network golgin, GCC185, is required for endosome-to-Golgi transport and maintenance of Golgi structure."
    Derby M.C., Lieu Z.Z., Brown D., Stow J.L., Goud B., Gleeson P.A.
    Traffic 8:758-773(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells."
    Ganley I.G., Espinosa E., Pfeffer S.R.
    J. Cell Biol. 180:159-172(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STX16.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "The localization of the Golgin GCC185 is independent of Rab6A/A' and Arl1."
    Houghton F.J., Chew P.L., Lodeho S., Goud B., Gleeson P.A.
    Cell 138:787-794(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB6A, SUBCELLULAR LOCATION.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND THR-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1557-1612, SUBCELLULAR LOCATION, INTERACTION WITH ARL1; RAB6A AND RAB9A, MUTAGENESIS OF ILE-1588; LEU-1595 AND TYR-1618.

Entry informationi

Entry nameiGCC2_HUMAN
AccessioniPrimary (citable) accession number: Q8IWJ2
Secondary accession number(s): A6H8X8
, O15045, Q4ZG46, Q8TDH3, Q9H2G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: November 30, 2010
Last modified: April 13, 2016
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.