Q8IWJ2 (GCC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GCC2
Synonyms:	KIAA0336, RANBP2L4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1684 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9 Ref.11 Ref.12
Subunit structure	Homodimer. Interacts (via GRIP domain) with RAB6A (preferentially in its GTP-bound form). May interact (RAB6A-dependent) with ARL1; according to Ref.16, RAB6A and ARL1 are not involved in GCC2 Golgi localization as proposed by Ref.17. 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. Ref.9 Ref.11 Ref.13 Ref.16 Ref.17
Subcellular location	Cytoplasm. Golgi apparatus › trans-Golgi network membrane; Peripheral membrane protein Ref.8 Ref.9 Ref.12 Ref.16 Ref.17.
Tissue specificity	Ubiquitous. Ref.6
Domain	Extended rod-like protein with coiled-coil domains.
Sequence similarities	Contains 1 GRIP domain.
Sequence caution	The sequence AAG34902.1 differs from that shown. Reason: Frameshift at positions 694, 700, 937 and 940. The sequence AAH37774.1 differs from that shown. Reason: Wrong choice of CDS. The sequence AAI46790.1 differs from that shown. Reason: Wrong choice of CDS. The sequence AAL99918.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAX88838.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAA20794.2 differs from that shown. Reason: Wrong choice of CDS. The sequence EAW53882.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Golgi ribbon formation Inferred from mutant phenotype Ref.9Ref.12. Source: UniProtKB late endosome to Golgi transport Inferred from mutant phenotype Ref.9. Source: UniProtKB microtubule anchoring Inferred from mutant phenotype Ref.11. Source: UniProtKB microtubule organizing center organization Inferred from mutant phenotype Ref.11. Source: UniProtKB protein targeting to Golgi Inferred from electronic annotation. Source: InterPro protein targeting to lysosome Inferred from mutant phenotype Ref.9. Source: UniProtKB recycling endosome to Golgi transport Inferred from mutant phenotype Ref.12. Source: UniProtKB regulation of protein exit from endoplasmic reticulum Inferred from mutant phenotype Ref.12. Source: UniProtKB
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: HPA trans-Golgi network Inferred from direct assay Ref.9Ref.12. Source: UniProtKB
Molecular function	identical protein binding Inferred from physical interaction Ref.17. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1645320,EBI-1645320
RAB6A	P20340	4	EBI-1645320,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: Q8IWJ2-3)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1684

1684

GRIP and coiled-coil domain-containing protein 2

PRO_0000190074

Regions

Domain

1609 – 1659

51

GRIP

Region

1574 – 1684

111

Mediates interaction with RAB9A

Region

1574 – 1613

40

Mediates interaction with RAB6A

Coiled coil

110 – 1618

1509

Potential

Amino acid modifications

Modified residue

287

1

Phosphoserine Ref.14

Modified residue

1483

1

Phosphoserine Ref.10 Ref.15

Modified residue

1542

1

Phosphoserine Ref.15

Modified residue

1649

1

Phosphoserine Ref.14 Ref.15

Natural variations

Alternative sequence

22 – 45

24

LETLP…IQKAK → NWRKKLKNSDQNLLLKELVI LLRH in isoform 2.

VSP_040106

Alternative sequence

46 – 1684

1639

Missing in isoform 2.

VSP_040107

Natural variant

1134

1

Q → E. Ref.3
Corresponds to variant rs2718698 [ dbSNP | Ensembl ].

VAR_046635

Natural variant

1298

1

R → G.
Corresponds to variant rs1061202 [ dbSNP | Ensembl ].

VAR_016101

Experimental info

Mutagenesis

1588

1

I → 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. Ref.17

Mutagenesis

1595

1

L → 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. Ref.17

Mutagenesis

1618

1

Y → A: No effect on interaction with RAB6A and RAB9A. Ref.9 Ref.17

Secondary structure

1

.

.

.

1684

Helix Strand Turn

Details...

Helix

1574 – 1605

32

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 30, 2010. Version 4. Checksum: 83B6135D9EB9440D	FASTA	1,684	195,910
	10 20 30 40 50 60 MEDLVQDGVA SPATPGTGKS KLETLPKEDL IKFAKKQMML IQKAKSRCTE LEKEIEELRS 70 80 90 100 110 120 KPVTEGTGDI IKALTERLDA LLLEKAETEQ QCLSLKKENI KMKQEVEDSV TKMGDAHKEL 130 140 150 160 170 180 EQSHINYVKE IENLKNELMA VRSKYSEDKA NLQKQLEEAM NTQLELSEQL KFQNNSEDNV 190 200 210 220 230 240 KKLQEEIEKI RPGFEEQILY LQKQLDATTD EKKETVTQLQ NIIEANSQHY QKNINSLQEE 250 260 270 280 290 300 LLQLKAIHQE EVKELMCQIE ASAKEHEAEI NKLNELKENL VKQCEASEKN IQKKYECELE 310 320 330 340 350 360 NLRKATSNAN QDNQICSILL QENTFVEQVV NEKVKHLEDT LKELESQHSI LKDEVTYMNN 370 380 390 400 410 420 LKLKLEMDAQ HIKDEFFHER EDLEFKINEL LLAKEEQGCV IEKLKSELAG LNKQFCYTVE 430 440 450 460 470 480 QHNREVQSLK EQHQKEISEL NETFLSDSEK EKLTLMFEIQ GLKEQCENLQ QEKQEAILNY 490 500 510 520 530 540 ESLREIMEIL QTELGESAGK ISQEFESMKQ QQASDVHELQ QKLRTAFTEK DALLETVNRL 550 560 570 580 590 600 QGENEKLLSQ QELVPELENT IKNLQEKNGV YLLSLSQRDT MLKELEGKIN SLTEEKDDFI 610 620 630 640 650 660 NKLKNSHEEM DNFHKKCERE ERLILELGKK VEQTIQYNSE LEQKVNELTG GLEETLKEKD 670 680 690 700 710 720 QNDQKLEKLM VQMKVLSEDK EVLSAEVKSL YEENNKLSSE KKQLSRDLEV FLSQKEDVIL 730 740 750 760 770 780 KEHITQLEKK LQLMVEEQDN LNKLLENEQV QKLFVKTQLY GFLKEMGSEV SEDSEEKDVV 790 800 810 820 830 840 NVLQAVGESL AKINEEKCNL AFQRDEKVLE LEKEIKCLQE ESVVQCEELK SLLRDYEQEK 850 860 870 880 890 900 VLLRKELEEI QSEKEALQSD LLEMKNANEK TRLENQNLLI QVEEVSQTCS KSEIHNEKEK 910 920 930 940 950 960 CFIKEHENLK PLLEQKELRD RRAELILLKD SLAKSPSVKN DPLSSVKELE EKIENLEKEC 970 980 990 1000 1010 1020 KEKEEKINKI KLVAVKAKKE LDSSRKETQT VKEELESLRS EKDQLSASMR DLIQGAESYK 1030 1040 1050 1060 1070 1080 NLLLEYEKQS EQLDVEKERA NNFEHRIEDL TRQLRNSTLQ CETINSDNED LLARIETLQS 1090 1100 1110 1120 1130 1140 NAKLLEVQIL EVQRAKAMVD KELEAEKLQK EQKIKEHATT VNELEELQVQ LQKQKKQLQK 1150 1160 1170 1180 1190 1200 TMQELELVKK DAQQTTLMNM EIADYERLMK ELNQKLTNKN NKIEDLEQEI KIQKQKQETL 1210 1220 1230 1240 1250 1260 QEEITSLQSS VQQYEEKNTK IKQLLVKTKK ELADSKQAET DHLILQASLK GELEASQQQV 1270 1280 1290 1300 1310 1320 EVYKIQLAEI TSEKHKIHEH LKTSAEQHQR TLSAYQQRVT ALQEECRAAK AEQATVTSEF 1330 1340 1350 1360 1370 1380 ESYKVRVHNV LKQQKNKSMS QAETEGAKQE REHLEMLIDQ LKIKLQDSQN NLQINVSELQ 1390 1400 1410 1420 1430 1440 TLQSEHDTLL ERHNKMLQET VSKEAELREK LCSIQSENMM MKSEHTQTVS QLTSQNEVLR 1450 1460 1470 1480 1490 1500 NSFRDQVRHL QEEHRKTVET LQQQLSKMEA QLFQLKNEPT TRSPVSSQQS LKNLRERRNT 1510 1520 1530 1540 1550 1560 DLPLLDMHTV TREEGEGMET TDTESVSSAS TYTQSLEQLL NSPETKLEPP LWHAEFTKEE 1570 1580 1590 1600 1610 1620 LVQKLSSTTK SADHLNGLLR ETEATNAILM EQIKLLKSEI RRLERNQERE KSAANLEYLK 1630 1640 1650 1660 1670 1680 NVLLQFIFLK PGSERERLLP VINTMLQLSP EEKGKLAAVA QGEEENASRS SGWASYLHSW SGLR
	Isoform 2 [UniParc]. Checksum: 01BB22944C997E56	FASTA	45	5,043
	10 20 30 40 MEDLVQDGVA SPATPGTGKS KNWRKKLKNS DQNLLLKELV ILLRH

References

	« Hide 'large scale' referencesShow '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 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: 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. , 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-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: 15489334] [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: 12200376] [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: 11149944] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 161-946 (ISOFORM 1), 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 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: 16885419] [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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1483, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at the trans-Golgi network." Efimov A., Kharitonov A., Efimova N., Loncarek J., Miller P.M., Andreyeva N., Gleeson P., Galjart N., Maia A.R., McLeod I.X., Yates J.R. III, Maiato H., Khodjakov A., Akhmanova A., Kaverina I. Dev. Cell 12:917-930(2007) [PubMed: 17543864] [Abstract] 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: 17488291] [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: 18195106] [Abstract] Cited for: INTERACTION WITH STX16.
[14]	"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-287 AND SER-1649, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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-1483; SER-1542 AND SER-1649, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 19703403] [Abstract] Cited for: INTERACTION WITH RAB6A, SUBCELLULAR LOCATION.
[17]	"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 1557-1612, SUBCELLULAR LOCATION, INTERACTION WITH ARL1; RAB6A AND RAB9A, MUTAGENESIS OF ILE-1588; LEU-1595 AND TYR-1618.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00005631.
IPI00947067.

RefSeq

NP_852118.1. NM_181453.3.

UniGene

Hs.436505.
Hs.469630.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BBP	X-ray	3.00	D/E/F	1547-1612	[»]

ProteinModelPortal

Q8IWJ2.

SMR

Q8IWJ2. Positions 1570-1607.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8IWJ2. 13 interactions.

STRING

Q8IWJ2.

PTM databases

PhosphoSite

Q8IWJ2.

Polymorphism databases

DMDM

158931162.

Proteomic databases

PRIDE

Q8IWJ2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309863; ENSP00000307939; ENSG00000135968.
ENST00000409325; ENSP00000386860; ENSG00000135968.

GeneID

9648.

KEGG

hsa:9648.

UCSC

uc002tec.1. human.

Organism-specific databases

CTD

9648.

GeneCards

GC02P109065.

H-InvDB

HIX0023314.

HGNC

HGNC:23218. GCC2.

HPA

HPA035849.

MIM

612711. gene.

neXtProt

NX_Q8IWJ2.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00600000084031.

HOGENOM

HBG278534.

HOVERGEN

HBG045522.

InParanoid

Q8IWJ2.

OMA

CQIEASA.

OrthoDB

EOG4RFKS0.

PhylomeDB

Q8IWJ2.

Gene expression databases

ArrayExpress

Q8IWJ2.

Bgee

Q8IWJ2.

CleanEx

HS_GCC2.

Genevestigator

Q8IWJ2.

GermOnline

ENSG00000135968. Homo sapiens.

Family and domain databases

InterPro

IPR000237. GRIP.
[Graphical view]

Pfam

PF01465. GRIP. 1 hit.
[Graphical view]

SMART

SM00755. Grip. 1 hit.
[Graphical view]

PROSITE

PS50913. GRIP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

36215.

SOURCE

Search...

Entry information

Entry name

GCC2_HUMAN

Accession

Primary (citable) accession number: Q8IWJ2
Secondary accession number(s): A6H8X8 , O15045, Q4ZG46, Q8TDH3, Q9H2G8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 3, 2003
Last sequence update:	November 30, 2010
Last modified:	January 25, 2012
This is version 96 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.